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14-3-3epsilon phosphoprotein + H2O
14-3-3epsilon protein + phosphate
-
-
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
-
-
-
-
?
4-nitrophenyl methylphosphonate + H2O
4-nitrophenol + methylphosphonate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
a phosphoprotein + H2O
a protein + phosphate
-
the enzyme is specific from serinel/threonine-phosphorylated proteins including casein, histone H2a, phosphorylase kinase, or glycogen phosphorylase. The enzyme does not display detectable protein phosphatase activity toward a number of tyrosine-phosphorylated substrates
-
-
?
a phosphoprotein + H2O
dephosphorylated protein + phosphate
-
-
-
-
?
AAApTVA + H2O
AAATVA + phosphate
-
-
-
?
AGPALpSPVPPV + H2O
AGPALSPVPPV + phosphate
-
-
-
?
Ala-Arg-Thr-Cys-Arg-Ser-Gly-Ser(P)-Val-Tyr + H2O
Ala-Arg-Thr-Cys-Arg-Ser-Gly-Ser-Val-Tyr + phosphate
-
best substrate
-
-
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
-
-
-
-
?
ALSAGpSNEYLR + H2O
ALSAGSNEYLR + phosphate
-
-
-
?
ASQEPpSPAASA + H2O
ASQEPSPAASA + phosphate
-
-
-
?
beta-naphthyl phosphate + H2O
beta-naphthol + phosphate
-
-
-
-
?
biotin-DGDFEEIPEE(P)YLQNH2 + H2O
biotin-DGDFEEIPEEYLQNH2 + phosphate
-
-
-
-
?
cAMP dependent protein kinase + H2O
?
-
-
-
-
?
carrier protein-p53-phosphoserine + H2O
carrier protein-p53-serine + phosphate
-
-
-
-
?
carrier protein-PB1-phosphoserine + H2O
carrier protein-PB1-serine + phosphate
-
-
-
-
?
carrier protein-T3-phosphothreonine + H2O
carrier protein-T3-threonine + phosphate
carrier protein-T4-phosphothreonine + H2O
carrier protein-T4-threonine + phosphate
carrier protein-T5-phosphothreonine + H2O
carrier protein-T5-threonine + phosphate
-
-
-
-
?
chicken acidic leucine-rich epidermal growth factor-like domain-containing brain protein/neuroglycan C + H2O
?
-
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
-
-
?
DADEpYLPQQG + H2O
DADEYLPQQG + phosphate
DDApTVA + H2O
DDATVA + phosphate
-
-
-
?
DLDVPIPGRFDRRVS(P)VAAE + H2O
DLDVPIPGRFDRRVSVAAE + phosphate
-
-
-
-
?
DLDVPIPGRFDRRVSVAAE + H2O
? + phosphate
DLDVPIPGRFDRRVY(P)VAAE + H2O
DLDVPIPGRFDRRVYVAAE + phosphate
-
-
-
-
?
DRRVS(P)VAAE + H2O
DRRVSVAAE + phosphate
-
-
-
-
?
DRVY(P)IHPFHL + H2O
DRVYIHPFHL + phosphate
-
-
-
-
?
ENDpTINASL + H2O
ENDTINASL + phosphate
-
-
-
?
ENDpYINASL + H2O
ENDYINASL + phosphate
ESEMEpTPSAIN + H2O
ESEMETPSAIN + phosphate
-
-
-
?
ETTYERW(pT)TITQRER + H2O
ETTYERWTTITQRER + phosphate
-
-
-
?
FDRRVS(P)VAAE + H2O
FDRRVSVAAE + phosphate
-
-
-
-
?
FLRT(P)SCG + H2O
FLRTSCG + phosphate
-
-
-
-
?
FLRTS(P)CG + H2O
FLRTSCG + phosphate
-
-
-
-
?
FLRTT(P)CG + H2O
FLRTTCG + phosphate
-
-
-
-
?
fluorotyrosine phosphate + H2O
fluorotyrosine + phosphate
-
-
-
-
?
fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase + H2O
? + phosphate
-
-
-
-
?
fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase + H2O
fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase + phosphate
-
heterotrimeric phosphatase 2A catalyzing the dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase
-
-
?
FYDEEVDEMY(P)REAPIDKKGNFNY(P)VEFTR + H2O
FYDEEVDEMYREAPIDKKGNFNYVEFTR + phosphate
-
-
-
-
?
glycogen synthase + H2O
glycogen synthase + phosphate
glycogen synthase b + H2O
glycogen synthase I + phosphate
glycogen synthase D + H2O
glycogen synthase I + phosphate
heavy meromyosin + H2O
?
-
-
-
-
?
histone + H2O
histone + phosphate
-
-
-
-
?
HSAPPpSPEEKD + H2O
HSAPPSPEEKD + phosphate
-
-
-
?
KR(pT)IRR + H2O
KRTIRR + phosphate
KRpTIRR + H2O
KRTIRR + phosphate
microtubulin + H2O
?
-
-
-
-
?
myelin basic phosphoprotein + H2O
myelin basic protein + phosphate
myelin basic protein + H2O
? + phosphate
-
-
-
-
?
myosin light chain phosphate + H2O
myosin light chain + phosphate
-
myosin light chain phosphatase is a specific form of PP1
-
-
?
NFEDHpSAPPSP + H2O
NFEDHSAPPSP + phosphate
-
-
-
?
NIDAIRA(pS)LNIMSR + H2O
NIDAIRASLNIMSR + phosphate
-
-
-
?
NPCTEpTFTGTL + H2O
NPCTETFTGTL + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
p38 MAP kinase phosphoprotein
?
-
-
-
-
?
peptide mGluR3 + H2O
?
-
-
-
?
Phe-Arg-Arg-Leu-Ser(P)-Ile-Ser + H2O
Phe-Arg-Arg-Leu-Ser-Ile-Ser + phosphate
-
least effective substrate, corresponding to the alpha-subunit of protein phosphatase
-
-
?
phosphatidylinositol-(3,4,5)-triphosphate + H2O
?
the enzyme displays activity towards the D3 position of the phosphoinositide second messenger phosphatidylinositol (3,4,5)-triphosphate
-
-
?
phospho-Cdk2 + H2O
Cdk6 + phosphate
-
-
-
-
?
phospho-Cdk6 + H2O
Cdk6 + phosphate
-
-
-
-
?
phospho-D,L-tyrosine + H2O
D,L-tyrosine + phosphate
-
-
-
-
?
phospho-L-serine + H2O
L-serine + phosphate
-
-
-
-
?
phospho-L-threonine + H2O
L-threonine + phosphate
-
-
-
-
?
phospho-L-tyrosine + H2O
L-tyrosine + phosphate
phospho-MKK + H2O
MKK + phosphate
-
-
-
-
?
phospho-PA3347 + H2O
PA3347 + phosphate
-
dephosphorylation of Ser56 by PA3346
-
-
?
phospho-TAK1 + H2O
TAK1 + phosphate
-
-
-
-
?
phospho-threonylpeptide + H2O
threonylpeptide + phosphate
-
-
-
-
?
phosphoangiotensin + H2O
angiotensin + phosphate
-
phosphorylated at Tyr
-
-
?
phosphocasein + H2O
casein + phosphate
phosphohistone + H2O
histone + phosphate
phosphohistone H1 + H2O
histone H1 + phosphate
-
-
-
-
?
phosphomyosin light chain + H2O
myosin light chain + phosphate
phosphophosphorylase kinase + H2O
phosphorylase kinase + phosphate
phosphoprotamine + H2O
protamine + phosphate
phosphoprotein + H2O
protein + phosphate
phosphoprotein K15F + H2O
protein K15F + phosphate
-
-
-
-
?
phosphoprotein R20A + H2O
protein R20A + phosphate
-
-
-
-
?
phosphoprotein RII + H2O
protein RII + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
phosphopyruvate kinase + H2O
pyruvate kinase + phosphate
phosphorylase a + H2O
?
-
-
-
-
?
phosphorylase a + H2O
? + phosphate
-
-
-
-
?
phosphorylase a + H2O
phosphorylase b + phosphate
phosphorylated 3-hydroxy 3-methylglutaryl coenzyme A reductase + H2O
3-hydroxy 3-methylglutaryl coenzyme A reductase + phosphate
-
-
-
-
?
phosphorylated 80S-ribosome + H2O
80S-ribosome + phosphate
-
-
-
-
?
phosphorylated acetyl-CoA carboxylase + H2O
acetyl-CoA carboxylase + phosphate
-
i.e. EC 6.4.1.2, phosphorylated
-
-
?
phosphorylated AD P-Tau + H2O
AD P-Tau + phosphate
-
-
-
-
?
phosphorylated Akt protein + H2O
Akt protein + phosphate
-
-
the dephosphorylation leads to inhibition of Akt protein
-
?
phosphorylated Akt1 + H2O
Akt1 + phosphate
-
-
-
-
?
phosphorylated alpha-casein + H2O
alpha-casein + phosphate
-
-
-
-
?
phosphorylated alpha-subunit of eukaryotic peptide initiation factor 2 + H2O
alpha-subunit of eukaryotic peptide initiation factor + phosphate
-
-
-
-
?
phosphorylated alpha-subunit of succinyl-CoA synthetase + H2O
alpha-subunit of succinyl-CoA synthetase + phosphate
-
activity is lower than towards phosphorylated nucleoside-diphosphate kinase
-
-
?
phosphorylated androgen receptor + H2O
androgen receptor + phosphate
-
-
the dephosphorylation leads to inhibition of androgen receptor
-
?
phosphorylated angiomotin + H2O
angiomotin + phosphate
-
-
-
-
?
phosphorylated AP-1/AP-2 + H2O
AP-1/AP-2 + phosphate
-
-
the dephosphorylation leads to inhibition of AP-1/AP-2
-
?
phosphorylated APC protein + H2O
APC protein + phosphate
-
-
the dephosphorylation leads to inhibition of APC protein
-
?
phosphorylated apoptosis signal-regulating kinase 1 + H2O
apoptosis signal-regulating kinase 1 + phosphate
phosphorylated ASK1 + H2O
ASK1 + phosphate
-
ASK1 is inactivated by the isoform PP2Ceta
-
-
?
phosphorylated ataxia telangiectasia and Rad3-related + H2O
ataxia telangiectasia and Rad3-related + phosphate
-
-
-
-
?
phosphorylated ataxia telangiectasia mutated kinase + H2O
ataxia telangiectasia mutated kinase + phosphate
phosphorylated ATM and Rad 3 related kinase + H2O
ATM and Rad 3 related kinase + phosphate
-
-
-
?
phosphorylated ATM protein + H2O
ATM protein + phosphate
-
-
the dephosphorylation leads to inhibition of ATM protein
-
?
phosphorylated atypical protein kinase C + H2O
atypical protein kinase C + phosphate
-
-
-
-
?
phosphorylated aurora A + H2O
aurora A + phosphate
phosphorylated axin + H2O
axin + phosphate
-
-
the dephosphorylation leads to inhibition of axin
-
?
phosphorylated B-catenin + H2O
B-catenin + phosphate
-
-
the dephosphorylation leads to activation of B-catenin
-
?
phosphorylated BAD protein + H2O
BAD protein + phosphate
-
-
the dephosphorylation leads to activation of BAD protein
-
?
phosphorylated BAX protein + H2O
BAX protein + phosphate
-
-
the dephosphorylation leads to activation of BAX protein
-
?
phosphorylated BCKDH complex + H2O
BCKDH complex + phosphate
-
i.e. branched-chain alpha-keto acid dehydrogenase, phosphorylated
-
-
?
phosphorylated BCL-2 + H2O
BCL-2 + phosphate
-
-
the dephosphorylation leads to inhibition of BCL-2
-
?
phosphorylated Bcl2 + H2O
Bcl2 + phosphate
-
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
-
-
-
-
?
phosphorylated brain proteins + H2O
brain proteins + phosphate
-
e.g. DARPP-32, G-substrate, both phosphorylated at threonine, similar amino acid sequences and phosphorylation sites, protein K-F.
-
-
?
phosphorylated c-Jun N-terminal kinase + H2O
c-Jun N-terminal kinase + phosphate
-
-
-
?
phosphorylated c-MET + H2O
c-MET + phosphate
-
-
the dephosphorylation leads to inhibition of c-MET
-
?
phosphorylated c-Myc + H2O
c-Myc + phosphate
phosphorylated Ca2+/calmodulin-dependent protein kinase II + H2O
Ca2+/calmodulin-dependent protein kinase II + phosphate
phosphorylated CaBP4 + H2O
CaBP4 + phosphate
-
-
-
-
?
phosphorylated calmodulin-like domain of protein kinase + H2O
calmodulin-like domain of protein kinase + phosphate
-
-
-
-
?
phosphorylated calpain + H2O
calpain + phosphate
-
-
the dephosphorylation leads to inhibition of calpain
-
?
phosphorylated CAM kinase IV + H2O
CAM kinase IV + phosphate
-
-
the dephosphorylation leads to inhibition of CAM kinase IV
-
?
phosphorylated cAMP-dependent protein kinase + H2O
cAMP-dependent protein kinase + phosphate
phosphorylated carboxypeptidase D + H2O
carboxypeptidase D + phosphate
-
-
the dephosphorylation leads to inhibition of carboxypeptidase D
-
?
phosphorylated CAS protein + H2O
CAS protein + phosphate
-
-
the dephosphorylation leads to inhibition of CAS protein
-
?
phosphorylated casein (PKA) + H2O
casein (PKA) + phosphate
phosphorylated casein + H2O
casein + phosphate
phosphorylated Cav1.2 + H2O
Cav1.2 + phosphate
phosphorylated Cbp1 + H2o
Cbp1 + phosphate
-
-
-
-
?
phosphorylated Cdc25c + H2O
Cdc25c + phosphate
-
-
the dephosphorylation leads to inhibition of Cdc25c
-
?
phosphorylated Cdc6 protein + H2O
Cdc6 protein + phosphate
-
-
the dephosphorylation leads to activation of Cdc6 protein
-
?
phosphorylated Cdk1 + H2O
Cdk1 + phosphate
-
-
-
-
?
phosphorylated CFTRCXCR2 + H2O
CFTRCXCR2 + phosphate
-
-
the dephosphorylation leads to inhibition of CFTRCXCR2
-
?
phosphorylated chemotaxis protein CheA + H2O
chemotaxis protein CheA + phosphate
-
activity is lower than towards phosphorylated nucleoside-diphosphate kinase
-
-
?
phosphorylated Chk1 + H2O
Chk1 + phosphate
-
-
-
-
?
phosphorylated Chk1 protein + H2O
Chk1 protein + phosphate
-
-
the dephosphorylation leads to inhibition of Chk1 protein
-
?
phosphorylated Chk2 + H2O
Chk2 + phosphate
phosphorylated cyclin G1 + H2O
cyclin G1 + phosphate
-
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
-
-
the dephosphorylation leads to inhibition of DARP-32
-
?
phosphorylated deoxycytidine kinase + H2O
deoxycytidine kinase + phosphate
-
protein phosphatase 2A negatively regulates deoxycytidine kinase activity via Ser-74 dephosphorylation
-
-
?
phosphorylated DNA-dependent protein kinase + H2O
DNA-dependent protein kinase + phosphate
phosphorylated DNA-protease K + H2O
DNA-protease K + phosphate
-
-
-
-
?
phosphorylated doublecortin + H2O
doublecortin + phosphate
-
-
-
-
?
phosphorylated E-cadherin + H2O
E-cadherin + phosphate
-
-
the dephosphorylation leads to activation of E-cadherin
-
?
phosphorylated Ebola virus VP30 protein + H2O
Ebola virus VP30 protein + phosphate
-
-
-
-
?
phosphorylated ERK + H2O
ERK + phosphate
phosphorylated ERK protein + H2O
ERK protein + phosphate
-
-
the dephosphorylation leads to inhibition of ERK protein
-
?
phosphorylated ERK-2 + H2O
ERK-2 + phosphate
phosphorylated ERK1 + H2O
ERK1 + phosphate
-
-
-
-
?
phosphorylated ERK2 + H2O
ERK2 + phosphate
phosphorylated ERK5 + H2O
ERK5 + phosphate
-
dephosphorylation at Thr218 and Tyr220 residues, dephosphorylation site sequences, overview
-
-
?
phosphorylated estrogen receptor A + H2O
estrogen receptor A + phosphate
-
-
the dephosphorylation leads to inhibition of estrogen receptor A
-
?
phosphorylated extracellular-signal-regulated kinase + H2O
extracellular-signal-regulated kinase + phosphate
-
PP2A is involved in the inactivation, but not the activation, of extracellular-signal-regulated kinase
-
-
?
phosphorylated glucocorticoid receptor-heat shock protein 90 + H2O
glucocorticoid receptor-heat shock protein 90 + phosphate
-
-
-
?
phosphorylated glycogen phosphorylase + H2O
glycogen phosphorylase + phosphate
-
-
-
-
?
phosphorylated glycogen phosphorylase a + H2O
glycogen phosphorylase a + phosphate
phosphorylated glycogen phosphorylase alpha + H2O
glycogen phosphorylase alpha + phosphate
-
-
-
-
?
phosphorylated Gp130 protein + H2O
Gp130 protein + phosphate
-
-
the dephosphorylation leads to activation of Gp130 protein
-
?
phosphorylated GSK3beta + H2O
GSK3beta + phosphate
laforin dephosphorylates the inhibitory Ser9 of GSK3beta
-
-
?
phosphorylated H2AX + H2O
H2AX + phosphate
phosphorylated HAND-1 + H2O
HAND-1 + phosphate
-
-
the dephosphorylation leads to inhibition of HAND-1
-
?
phosphorylated HAND-2 + H2O
HAND-2 + phosphate
-
-
the dephosphorylation leads to inhibition of HAND-2
-
?
phosphorylated HDAC4 + H2O
HDAC4 + phosphate
-
-
the dephosphorylation leads to inhibition of HDAC4
-
?
phosphorylated High mobility group box 1 protein + H2O
High mobility group box 1 protein + phosphate
-
-
-
-
?
phosphorylated histone + H2O
histone + phosphate
phosphorylated histone 2A member X + H2O
histone 2A member X + phosphate
-
-
-
-
?
phosphorylated histone deacetylase 3 + H2O
histone deacetylase 3 + phosphate
phosphorylated histone deacetylase 7 + H2O
histone deacetylase 7 + phosphate
-
-
-
-
?
phosphorylated histone h1 (PKA) + H2O
histone h1 (PKA) + phosphate
phosphorylated histone h1 (PKC) + H2O
histone h1 (PKC) + phosphate
phosphorylated histone H3 + H2O
histone H3 + phosphate
-
dephosphorylation of histone H3 at Ser10 by PP1 is required for DNA methylation of some loci
-
-
?
phosphorylated histone IIA + H2O
histone IIA + phosphate
-
-
-
-
?
phosphorylated hormone-sensitive lipase + H2O
hormone-sensitive lipase + phosphate
phosphorylated Hsp90 + H2O
Hsp90 + phosphate
-
PP5 positively regulates the function of Hsp90 to maintain cellular homeostasis during proteotoxic stresses
-
-
?
phosphorylated IkappaB kinase + H2O
IkappaB kinase + phosphate
phosphorylated IKKB + H2O
IKKB + phosphate
-
-
the dephosphorylation leads to inhibition of IKKB
-
?
phosphorylated IKKB protein + H2O
IKKB protein + phosphate
-
-
the dephosphorylation leads to activation of IKKB protein
-
?
phosphorylated ILK1 + H2O
ILK1 + phosphate
phosphorylated INAD-protein + H2O
INAD-protein + phosphate
phosphorylated inhibitor-1 + H2O
inhibitor-1 + phosphate
-
-
-
-
?
phosphorylated inhibitor-2 + H2O
inhibitor-2 + phosphate
-
-
-
-
?
phosphorylated JNK protein + H2O
JNK protein + phosphate
phosphorylated JNK1 + H2O
JNK1 + phosphate
-
dephosphorylation at Thr183 and Tyr185 residues, dephosphorylation site sequences, overview
-
-
?
phosphorylated katanin p60 + H2O
katanin p60 + phosphate
-
-
-
-
?
phosphorylated keratin 8 + H2O
keratin 8 + phosphate
-
dephosphorylates at phospho-Ser431
-
-
?
phosphorylated KSR protein + H2O
KSR protein + phosphate
-
-
the dephosphorylation leads to activation of KSR protein
-
?
phosphorylated lamban + H2O
lamban + phosphate
phosphorylated Mdm2 protein + H2O
Mdm2 protein + phosphate
-
-
the dephosphorylation leads to activation of Mdm2 protein
-
?
phosphorylated MEK3 + H2O
MEK3 + phosphate
-
-
the dephosphorylation leads to inhibition of MEK3
-
?
phosphorylated MEKK3 + H2O
MEKK3 + phosphate
-
-
the dephosphorylation leads to inhibition of MEKK3
-
?
phosphorylated messenger ribonucleoprotein + H2O
messenger ribonucleoprotein + phosphate
-
-
-
-
?
phosphorylated microtubule associated protein + H2O
microtubule associated protein + phosphate
-
-
-
-
?
phosphorylated Mid1 + H2O
Mid1 + phosphate
-
-
-
-
?
phosphorylated Mih1 + H2O
Mih1 + phosphate
-
protein phosphatase 2A associated with Cdc55 dephosphorylates Mih1
-
-
?
phosphorylated mitogen-activated protein kinase kinase 3 + H2O
mitogen-activated protein kinase kinase 3 + phosphate
-
-
-
-
?
phosphorylated mitogen-activated protein kinase Pmk1p + H2O
mitogen-activated protein kinase Pmk1p + phosphate
phosphorylated MKK3b + H2O
MKK3b + phosphate
-
MKK3b is inactivated by the isoforms PP2Calpha and PP2Cbeta
-
-
?
phosphorylated MKK4 + H2O
MKK4 + phosphate
phosphorylated MKK6b + H2O
MKK6b + phosphate
-
MKK6b is inactivated by the isoforms PP2Calpha and PP2Cbeta
-
-
?
phosphorylated MKK7 + H2O
MKK7 + phosphate
-
MKK7 is inactivated by the isoforms PP2Calpha and PP2Cbeta
-
-
?
phosphorylated mouse double minute 2 homologue + H2O
mouse double minute 2 homologue + phosphate
-
-
-
-
?
phosphorylated myelin basic protein + H2O
?
-
-
-
-
?
phosphorylated myelin basic protein + H2O
myelin basic protein + phosphate
phosphorylated myosin light chain + H2O
myosin light chain + phosphate
phosphorylated myosin light chain 2 + H2O
myosin light chain 2 + phosphate
-
preferred target substrate for PP1 in the thick filament
-
-
?
phosphorylated myosin light chain peptide + H2O
myosin light chain peptide + phosphate
-
KAKTTKKRPQRATSNVFS
-
-
?
phosphorylated NDEL1 + H2O
NDEL1 + phosphate
-
PP4c selectively dephosphorylates NDEL1 at T219
-
-
?
phosphorylated nemo protein + H2O
nemo protein + phosphate
-
-
the dephosphorylation leads to inhibition of nemo protein
-
?
phosphorylated nucleoside-diphosphate kinase + H2O
nucleoside-diphosphate kinase + phosphate
phosphorylated nucleotide diphosphate kinase 2 + H2O
nucleotide diphosphate kinase 2 + phosphate
-
-
-
-
?
phosphorylated occludin + H2O
occludin + phosphate
-
-
the dephosphorylation leads to inhibition of occludin
-
?
phosphorylated P107 + H2O
P107 + phosphate
-
-
the dephosphorylation leads to inhibition of P107
-
?
phosphorylated p38 + H2O
p38 + phosphate
phosphorylated p38alpha + H2O
p38alpha + phosphate
phosphorylated p53 + H2O
p53 + phosphate
phosphorylated p53 protein + H2O
p53 protein + phosphate
-
-
the dephosphorylation leads to activation of p53 protein
-
?
phosphorylated p53-binding protein 1 + H2O
p53-binding protein 1 + phosphate
-
p53-binding protein 1 is dephosphorylated at Ser25 and Ser1778
-
-
?
phosphorylated PACS-1 + H2O
PACS-1 + phosphate
-
-
the dephosphorylation leads to inhibition of PACS-1
-
?
phosphorylated Par-3 + H2O
Par-3 + phosphate
-
predominantly the alpha-isoform of PP1 binds phosphorylated Par-3 and specifically dephosphorylates at Ser-144 and Ser-824
-
-
?
phosphorylated Par-6 + H2O
Par-6 + phosphate
-
-
-
-
?
phosphorylated paxillin + H2O
paxillin + phosphate
-
-
the dephosphorylation leads to inhibition of paxillin
-
?
phosphorylated penicillin-binding protein + H2O
penicillin-binding protein + phosphate
phosphorylated peptide + H2O
peptide + phosphate
-
PP2Cdelta prefers the dephosphorylation at diphosphorylated T(P)X(P)Y sequence compared to monophosphorylated T(P)XY sequence
-
-
?
phosphorylated period + H2O
period + phosphate
-
-
the dephosphorylation leads to activation of period
-
?
phosphorylated phosphoenolpyruvate carboxylase + H2O
phosphoenolpyruvate carboxylase + phosphate
-
-
-
-
?
phosphorylated phosphorylase a + H2O
phosphorylase a + phosphate
phosphorylated phosphorylase alpha + H2O
phosphorylase alpha + phosphate
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
phosphorylated phytochrome A + H2O
phytochrome A + phosphate
-
PAPP2C dephosphorylates both native oat phytochrome A and a point mutant of S598A, whereas an N-terminal deletion of 65 amino acids prevents dephosphorylation
-
-
?
phosphorylated phytochrome B + H2O
phytochrome B + phosphate
-
phytochrome B is autophosphorylated, the N-terminal extension-deleted phytochrome B shows no apparent autophosphorylation activity
-
-
?
phosphorylated PIM protein + H2O
PIM protein + phosphate
-
-
the dephosphorylation leads to inhibition of PIM protein
-
?
phosphorylated PKCbeta II + H2O
PKBbeta II + phosphate
-
-
the dephosphorylation leads to inhibition of PKCbeta II
-
?
phosphorylated PKCdelta + H2O
PKCdelta + phosphate
-
-
the dephosphorylation leads to inhibition of PKCdelta
-
?
phosphorylated Polo-like kinase 1 + H2O
Polo-like kinase 1 + phosphate
-
-
-
-
?
phosphorylated pRb protein + H2O
pRb protein + phosphate
phosphorylated protein kinase CK2alpha + H2O
protein kinase CK2alpha + phosphate
-
-
-
?
phosphorylated protein kinase Hs11 + H2O
protein kinase Hs11 + phosphate
phosphorylated protein phosphatase inhibitor-1 + H2O
protein phosphatase inhibitor-1 + phosphate
phosphorylated Prz1 + H2o
Prz1 + phosphate
phosphorylated pyruvate dehydrogenase + H2O
pyruvate dehydrogenase + phosphate
phosphorylated Raf + H2O
Raf + phosphate
-
Raf is dephosphorylated at Ser259
-
-
?
phosphorylated Raf-1 kinase + H2O
Raf 1 kinase + phosphate
phosphorylated Raf1 + H2O
Raf-1 + phosphate
-
-
-
-
?
phosphorylated Raf1 + H2O
Raf1 + phosphate
-
-
the dephosphorylation leads to activation of Raf1
-
?
phosphorylated RalA + H2O
RalA + phosphate
-
-
the dephosphorylation leads to inhibition of RalA
-
?
phosphorylated RelA + H2O
RelA + phosphate
-
-
the dephosphorylation leads to inhibition of RelA
-
?
phosphorylated retinoblastoma protein + H2O
retinoblastoma protein + phosphate
phosphorylated rhodopsin + H2O
rhodopsin + phosphate
-
-
-
-
?
phosphorylated RNA polymerase II + H2O
RNA polymerase II + phosphate
phosphorylated SCR protein + H2O
SCR protein + phosphate
-
-
the dephosphorylation leads to inhibition of SCR protein
-
?
phosphorylated securin + H2O
securin + phosphate
phosphorylated Ser/Thr protein kinase + H2O
DNA-dependent Ser/Thr protein kinase + phosphate
-
-
-
?
phosphorylated seratonin + H2O
seratonin + phosphate
-
-
the dephosphorylation leads to activation of seratonin
-
?
phosphorylated serine-phosphorylated glycogen phosphorylase + H2O
glycogen phosphorylase + phosphate
-
-
-
-
?
phosphorylated serine/threonine protein kinase + H2O
serine/threonine protein kinase + phosphate
phosphorylated Shc protein + H2O
Shc protein + phosphate
-
-
the dephosphorylation leads to inhibition of Shc protein
-
?
phosphorylated Sp1 + H2O
Sp1 + phosphate
-
-
the dephosphorylation leads to activation of Sp1
-
?
phosphorylated spliceosome-associated protein 155 + H2O
spliceosome-associated protein 155 + phosphate
phosphorylated sprouty + H2O
sprouty + phosphate
-
-
the dephosphorylation leads to activation of sprouty
-
?
phosphorylated Src protein + H2O
Src protein + phosphate
-
-
the dephosphorylation leads to inhibition of Src protein
-
?
phosphorylated stress-activated protein kinase + H2O
stress-activated protein kinase + phosphate
phosphorylated TAK1-binding protein 1 + H2O
TAK1-binding protein 1 + phosphate
-
-
-
-
?
phosphorylated Tau + H2O
Tau + phosphate
-
the Balpha regulatory subunit of PP2A facilitates dephosphorylation of the phosphorylated Tau
-
-
?
phosphorylated tau protein + H2O
tau protein + phosphate
-
-
the dephosphorylation leads to activation of tau protein
-
?
phosphorylated tau-factor + H2O
tau-factor + phosphate
-
-
-
-
?
phosphorylated Tcn1/Crz1 + H2O
Tcn1/Crz1 + phosphate
phosphorylated TRAF2 + H2O
TRAF2 + phosphate
-
-
the dephosphorylation leads to inhibition of TRAF2
-
?
phosphorylated transforming growth factor beta-activated kinase 1 + H2O
transforming growth factor beta-activated kinase 1 + phosphate
-
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
phosphorylated tropomyosin-related kinase A + H2O
tropomyosin-related kinase A + phosphate
-
two neuron-enriched regulatory subunits, B'beta and B'delta, recruit PP2A into a complex with tropomyosin-related kinase A to dephosphorylate the nerve growth factor receptor on Ser/Thr residues and to potentiate its intrinsic tyrosine kinase activity
-
-
?
phosphorylated troponin + H2O
troponin + phosphate
-
-
-
-
?
phosphorylated troponin I + H2O
troponin I + phosphate
-
preferred target substrate for PP1 in the thin filament
-
-
?
phosphorylated troponin T + H2O
troponin T + phosphate
-
preferred target substrate for PP1 in the thin filament
-
-
?
phosphorylated tumor suppressor protein p53 + H2O
tumor suppressor protein p53 + phosphate
-
dephosphorylation at Thr55
-
-
?
phosphorylated UNG2 + H2O
UNG2 + phosphate
-
dephosphorylation at Thr residues, identification of dephosphorylation site sequences, overview
-
-
?
phosphorylated vimentin + H2O
vimentin + phosphate
-
-
the dephosphorylation leads to activation of vimentin
-
?
phosphoserine-casein + H2O
casein + phosphate
-
-
-
-
?
phosphoserine-myelin basic protein + H2O
myelin basic protein + phosphate
-
-
-
-
?
phosphoserine-RCML + H2O
RCML + phosphate
-
i.e. reduced carboxyamidomethylated and maleylated lysozyme containing phosphoserine
-
-
?
phosphospectrin + H2O
spectrin + phosphate
-
-
-
-
?
phosphothreonine + H2O
threonine + phosphate
-
-
-
?
phosphotyrosine-casein + H2O
casein + phosphate
-
-
-
-
?
phosphotyrosine-myelin basic protein + H2O
myelin basic protein + phosphate
-
-
-
-
?
phosphotyrosine-RCML + H2O
RCML + phosphate
-
i.e. reduced carboxyamidomethylated and maleylated lysozyme containing phosphotyrosine
-
-
?
PIPGRFDRRVS(P)VAAE + H2O
PIPGRFDRRVSVAAE + phosphate
-
-
-
-
?
PVARTpSPLQTP + H2O
PVARTSPLQTP + phosphate
-
-
-
?
Raf proto-oncogene serine/threonine protein kinase + H2O
dephosphorylated Raf proto-oncogene serine/threonine protein kinase + phosphate
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
-
-
-
-
?
RGRGSpSVGGGS + H2O
RGRGSSVGGGS + phosphate
-
-
-
?
RII peptide + H2O
? + phosphate
-
-
-
-
?
RRA(pS)VA + H2O
RRASVA + phosphate
RRA(pT)VA + H2O
RRATVA + phosphate
RRApSVA + H2O
RRASVA + phosphate
-
-
-
?
RRApTVA + H2O
RRATVA + phosphate
RRAS(P)VA + H2O
RRASVA + phosphate
RRAT(P)VA + H2O
RRATVA + phosphate
RRLIEDAE(pY)AARG + H2O
RRLIEDAEYAARG + phosphate
RRLIEDAEY(P)AARG + H2O
RRLIEDAEYAARG + phosphate
-
synthetic substrate
-
-
?
RRREEET(P)EE + H2O
RRREEETEE + phosphate
Lambdavirus lambda
-
-
-
-
?
serine/threonine-phosphorylated myelin basic protein + H2O
myelin basic protein + phosphate
-
-
-
-
?
SQLHIpTPGTAY + H2O
SQLHITPGTAY + phosphate
-
-
-
?
SSpSLESLQTAVAEVTLNGNIPFHRPR + H2O
SSSLESLQTAVAEVTLNGNIPFHRPR + phosphate
-
-
-
-
?
synthetic peptides with phosphotyrosyl residues + H2O
synthetic peptides + phosphate
tetrafluorotyrosine phosphate + H2O
tetrafluorotyrosine + phosphate
-
-
-
-
?
threonine-phosphorylated lipocortin I + H2O
lipocortin I + phosphate
-
-
-
-
?
tumor necrosis factor receptor-associated factor 6 + H2O
?
-
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 myelin basic protein + H2O
myelin basic protein + phosphate
-
-
-
-
?
tyrosine-phosphorylated sEGF-R + H2O
phosphorylated sEGF-R + phosphate
-
-
-
-
?
UNC-89 + H2O
?
-
the protein kinase 2 region of UNC-89 specifically interacts with SCPL-1
-
-
?
VARKLpSAREQR + H2O
VARKLSAREQR + phosphate
-
-
-
?
vasodilator associated phosphoprotein + H2O
vasodilator associated protein + phosphate
-
-
-
-
?
WHLADpSPAVNG + H2O
WHLADSPAVNG + phosphate
-
-
-
?
YLRSIpSLPVPV + H2O
YLRSISLPVPV + phosphate
-
-
-
?
[a peptide]-serine/threonine phosphate + H2O
[a peptide]-serine/threonine + phosphate
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
[AKT1 protein]-serine/threonine phosphate + H2O
[AKT1 protein]-serine/threonine + phosphate
-
-
-
-
?
[alpha-casein]-serine/threonine phosphate + H2O
[alpha-casein]-serine/threonine + phosphate
-
-
-
?
[anti-anti-sigma factor SpoIIAA]-serine/threonine phosphate + H2O
[anti-anti-sigma factor SpoIIAA]-serine/threonine + phosphate
[anti-sigma factor antagonist protein]-serine/threonine phosphate + H2O
[anti-sigma factor antagonist protein]-serine/threonine + phosphate
[aquaporin-2]-serine/threonine phosphate + H2O
[aquaporin-2]-serine/threonine + phosphate
[casein]-serine/threonine phosphate + H2O
[casein]-serine/threonine + phosphate
-
-
-
?
[ComD]-serine/threonine phosphate + H2O
[ComD]-serine/threonine + phosphate
-
substrate is a competence-specific receptor of the TCS ComDE system
-
-
?
[CpG]-serine/threonine phosphate + H2O
[CpG]-serine/threonine + phosphate
[DivIVA]-serine/threonine phosphate + H2O
[DivIVA]-serine/threonine + phosphate
-
substrate is a protein involved in cell division
-
-
?
[EF-G translation factor]-serine/threonine phosphate + H2O
[EF-G translation factor]-serine/threonine + phosphate
[EF-Tu translation factor]-serine/threonine phosphate + H2O
[EF-Tu translation factor]-serine/threonine + phosphate
[elongation factor 2alpha]-serine/threonine phosphate + H2O
[elongation factor 2alpha]-serine/threonine + phosphate
-
-
-
?
[EmbR]-serine/threonine phosphate + H2O
[EmbR]-serine/threonine + phosphate
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
[GraR]-serine/threonine phosphate + H2O
[GraR]-serine/threonine + phosphate
substrate is a TCS response regulator
-
-
?
[HPr kinase]-serine/threonine phosphate + H2O
[HPr kinase]-serine/threonine + phosphate
[HPr protein]-serine/threonine phosphate + H2O
[HPr protein]-serine/threonine + phosphate
[MAP1B protein]-serine/threonine phosphate + H2O
[MAP1B protein]-serine/threonine + phosphate
[MAP2 protein]-serine/threonine phosphate + H2O
[MAP2 protein]-serine/threonine + phosphate
-
-
-
?
[MapZ]-serine/threonine phosphate + H2O
[MapZ]-serine/threonine + phosphate
-
substrate is a protein involved in cell division
-
-
?
[MgrA]-serine/threonine phosphate + H2O
[MgrA]-serine/threonine + phosphate
substrate is a global transcriptional regulator
-
-
?
[MurC]-serine/threonine phosphate + H2O
[MurC]-serine/threonine + phosphate
-
substrate is a protein involved in peptydoglycan synthesis
-
-
?
[myelin basic protein]-serine/threonine phosphate + H2O
[myelin basic protein]-serine/threonine + phosphate
[P-HLP]-serine/threonine phosphate + H2O
[P-HLP]-serine/threonine + phosphate
[P35]-serine/threonine phosphate + H2O
[P35]-serine/threonine + phosphate
substrate is a Mn2+-dependent inorganic diphosphatase
-
-
?
[PAK1]-serine phosphate + H2O
[PAK1]-serine + phosphate
dephosphorylation at Ser144
-
-
?
[PapA5]-serine/threonine phosphate + H2O
[PapA5]-serine/threonine + phosphate
[PBPA]-serine/threonine phosphate + H2O
[PBPA]-serine/threonine + phosphate
[Pkn5]-serine/threonine phosphate + H2O
[Pkn5]-serine/threonine + phosphate
[PknA]-serine/threonine phosphate + H2O
[PknA]-serine/threonine + phosphate
[PknB]-serine/threonine phosphate + H2O
[PknB]-serine/threonine + phosphate
[PknH]-serine/threonine phosphate + H2O
[PknH]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling and cell growth
-
-
?
[PknJ]-serine/threonine phosphate + H2O
[PknJ]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling and cell growth
-
-
?
[PpaC]-serine/threonine phosphate + H2O
[PpaC]-serine/threonine + phosphate
substrate is an inorganic diphosphatase
-
-
?
[PrkC]-serine/threonine phosphate + H2O
[PrkC]-serine/threonine + phosphate
[PrkD]-serine/threonine phosphate + H2O
[PrkD]-serine/threonine + phosphate
substrate PrkD is a dual-specificity tyrosine phosphorylation-regulated kinase
-
-
?
[PrkG]-serine/threonine phosphate + H2O
[PrkG]-serine/threonine + phosphate
substrate PrkG is a dual-specificity tyrosine phosphorylation-regulated kinase
-
-
?
[protein DivIVA]-serine/threonine phosphate + H2O
[protein DivIVA]-serine/threonine + phosphate
[protein I-1]-serine/threonine phosphate + H2O
[protein I-1]-serine/threonine + phosphate
[protein Jag]-serine/threonine phosphate + H2O
[protein Jag]-serine/threonine + phosphate
[protein LocZ]-serine/threonine phosphate + H2O
[protein locZ]-serine/threonine + phosphate
[protein PII]-serine/threonine phosphate + H2O
[protein PII]-serine/threonine + phosphate
the substrate is a protein involved in nitrogen assimilation
-
-
?
[protein]-L-serine phosphate + H2O
[protein]-L-serine + phosphate
[protein]-L-threonine phosphate + H2O
[protein]-L-threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
[PurA]-serine/threonine phosphate + H2O
[PurA]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling and cell aggregation
-
-
?
[PykA]-serine/threonine phosphate + H2O
[PykA]-serine/threonine + phosphate
i.e. pyruvate kinase
-
-
?
[RitR]-serine/threonine phosphate + H2O
[RitR]-serine/threonine + phosphate
-
substrate is a transcriptional regulator
-
-
?
[RR06]-serine/threonine phosphate + H2O
[RR06]-serine/threonine + phosphate
-
substrate is a TCS response regulator
-
-
?
[Rv0019c]-serine/threonine phosphate + H2O
[Rv0019c]-serine/threonine + phosphate
substrate is a FHA-domain-containing protein interacting with FtsZ, GtsQ, and PapA5, cell division
-
-
?
[S-adenosylhomocysteine hydrolase]-serine/threonine phosphate + H2O
[S-adenosylhomocysteine hydrolase]-serine/threonine + phosphate
-
-
-
?
[SP-STK kinase]-serine/threonine phosphate + H2O
[SP-STK kinase]-serine/threonine + phosphate
[SP-STK]-serine/threonine phosphate + H2O
[SP-STK]-serine/threonine + phosphate
[Stk1]-serine/threonine phosphate + H2O
[Stk1]-serine/threonine + phosphate
[StkP]-serine/threonine phosphate + H2O
[StkP]-serine/threonine + phosphate
-
substrate is a serine/threonine protein kinase involved in cell signaling
-
-
?
[Stk]-serine/threonine phosphate + H2O
[Stk]-serine/threonine + phosphate
-
i.e. Stk P5AP, the substrate is a serine/threonine protein kinase involved in cell signaling, antibiotic resistance, and peptydoglycan biosynthesis
-
-
?
[superoxide dismutase]-serine/threonine phosphate + H2O
[superoxide dismutase]-serine/threonine + phosphate
[tau protein]-serine/threonine phosphate + H2O
[tau protein]-serine/threonine + phosphate
-
-
-
?
[tubulin]-serine/threonine phosphate + H2O
[tubulin]-serine/threonine + phosphate
PP2A preferentially dephosphorylates unassembled tubulin
-
-
?
[VAV2]-threonine phosphate + H2O
[VAV2]-threonine + phosphate
dephosphorylation at Thr423
-
-
?
[YegI kinase]-serine/threonine phosphate + H2O
[YegI kinase]-serine/threonine + phosphate
[YezB]-serine/threonine phosphate + H2O
[YezB]-serine/threonine + phosphate
-
-
-
?
additional information
?
-
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
-
-
-
-
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
-
-
-
-
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
-
-
-
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
-
-
-
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
-
-
-
?
carrier protein-T3-phosphothreonine + H2O
carrier protein-T3-threonine + phosphate
-
-
-
-
?
carrier protein-T3-phosphothreonine + H2O
carrier protein-T3-threonine + phosphate
-
-
-
-
?
carrier protein-T4-phosphothreonine + H2O
carrier protein-T4-threonine + phosphate
-
-
-
-
?
carrier protein-T4-phosphothreonine + H2O
carrier protein-T4-threonine + phosphate
-
-
-
-
?
DADEpYLPQQG + H2O
DADEYLPQQG + phosphate
-
-
-
-
?
DADEpYLPQQG + H2O
DADEYLPQQG + phosphate
-
-
-
-
?
DLDVPIPGRFDRRVSVAAE + H2O
? + phosphate
-
peptide sequence corresponding to the R11 subunit of cAMP-dependent protein kinase
-
-
?
DLDVPIPGRFDRRVSVAAE + H2O
? + phosphate
-
peptide sequence corresponding to the R11 subunit of cAMP-dependent protein kinase
-
-
?
ENDpYINASL + H2O
ENDYINASL + phosphate
-
-
-
-
?
ENDpYINASL + H2O
ENDYINASL + phosphate
-
-
-
-
?
glycogen synthase + H2O
glycogen synthase + phosphate
-
-
-
-
?
glycogen synthase + H2O
glycogen synthase + phosphate
-
serine-phosphorylated glycogen synthase
-
-
?
glycogen synthase b + H2O
glycogen synthase I + phosphate
-
-
-
-
?
glycogen synthase b + H2O
glycogen synthase I + phosphate
-
-
-
-
?
glycogen synthase D + H2O
glycogen synthase I + phosphate
-
-
-
-
?
glycogen synthase D + H2O
glycogen synthase I + phosphate
-
-
-
-
r
KR(pT)IRR + H2O
KRTIRR + phosphate
-
-
-
?
KR(pT)IRR + H2O
KRTIRR + phosphate
-
-
-
?
KRpTIRR + H2O
KRTIRR + phosphate
-
-
-
-
?
KRpTIRR + H2O
KRTIRR + phosphate
-
-
-
-
?
myelin basic phosphoprotein + H2O
myelin basic protein + phosphate
-
-
-
-
?
myelin basic phosphoprotein + H2O
myelin basic protein + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
very low activity
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
Lambdavirus lambda
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
very low activity
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
very low activity
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p38 + H2O
?
-
-
-
-
?
phospho-L-tyrosine + H2O
L-tyrosine + phosphate
-
-
-
-
?
phospho-L-tyrosine + H2O
L-tyrosine + phosphate
-
-
-
-
?
phospho-L-tyrosine + H2O
L-tyrosine + phosphate
-
preferred substrate
-
-
?
phosphocasein + H2O
casein + phosphate
-
-
-
-
?
phosphocasein + H2O
casein + phosphate
-
-
-
-
?
phosphocasein + H2O
casein + phosphate
-
-
-
-
?
phosphocasein + H2O
casein + phosphate
-
-
-
-
?
phosphocasein + H2O
casein + phosphate
-
-
-
-
?
phosphocasein + H2O
casein + phosphate
-
-
-
-
?
phosphocasein + H2O
casein + phosphate
-
-
-
-
?
phosphocasein + H2O
casein + phosphate
-
-
-
?
phosphocasein + H2O
casein + phosphate
-
-
-
-
?
phosphocasein + H2O
casein + phosphate
-
-
-
-
?
phosphohistone + H2O
histone + phosphate
-
-
-
-
?
phosphohistone + H2O
histone + phosphate
-
-
-
-
?
phosphohistone + H2O
histone + phosphate
-
-
-
-
?
phosphohistone + H2O
histone + phosphate
-
-
-
-
?
phosphohistone + H2O
histone + phosphate
-
-
-
-
?
phosphohistone + H2O
histone + phosphate
-
-
-
-
?
phosphohistone + H2O
histone + phosphate
-
-
-
-
?
phosphohistone + H2O
histone + phosphate
-
-
-
-
?
phosphomyosin light chain + H2O
myosin light chain + phosphate
-
-
-
-
?
phosphomyosin light chain + H2O
myosin light chain + phosphate
-
-
-
-
?
phosphomyosin light chain + H2O
myosin light chain + phosphate
-
-
-
-
?
phosphophosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
specific for alpha-subunit
-
-
?
phosphophosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
specific for alpha-subunit
-
-
?
phosphophosphorylase kinase + H2O
phosphorylase kinase + phosphate
Lambdavirus lambda
-
specific for alpha-subunit
-
-
?
phosphophosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
specific for alpha-subunit
-
-
?
phosphophosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
specific for alpha-subunit
-
-
?
phosphophosphorylase kinase + H2O
phosphorylase kinase + phosphate
specific for alpha-subunit
-
-
?
phosphophosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
specific for alpha-subunit
-
-
?
phosphoprotamine + H2O
protamine + phosphate
-
-
-
-
?
phosphoprotamine + H2O
protamine + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
modulation of pyruvate dehydrogenase complex
-
-
?
phosphoprotein + H2O
protein + phosphate
-
phosphatase PP3 stimulates the initiation of DNA-synthesis
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
677568, 678107, 679065, 680788, 680919, 682091, 682953, 690925, 691077, 691081, 691177, 692550, 695126, 729150, 729715, 729741, 730348 -
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
role in cAMP catabolism
-
-
?
phosphoprotein + H2O
protein + phosphate
-
role of phosphatases in smooth muscle contractile systems
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
capable of dephosphorylating the major proteins involved in control of glycogen metabolism, glycolysis, gluconeogenesis, aromatic amino acid breakdown, fatty acid, cholesterol, and protein synthesis
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
involved in the intracellular mechanism through which adrenocortical steroidogenesis is regulated, acting at a point after cAMP generation and action but proximal to the side-chain cleavage of cholesterol
-
-
?
phosphoprotein + H2O
protein + phosphate
-
involved in regulating exocytosis from the rat parotid gland via a cAMP-mediated process
-
-
?
phosphoprotein + H2O
protein + phosphate
-
control of cholesterol genesis
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
134600, 134601, 134613, 134616, 134617, 134621, 134630, 134632, 134650, 134655, 134656, 134659, 134678 -
-
?
phosphoproteins + H2O
proteins + phosphate
-
comparison of amino acid sequence of substrates at phosphorylated sites
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
Lambdavirus lambda
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
Lambdavirus lambda
-
hydrolyzes phosphoseryl, phosphotyrosyl and phosphothreonyl substrates
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
most of the substrates are phosphorylated by cAMP and cGMP dependent protein kinases, other substrates are phosphorylated by calmodulin dependent multiprotein kinase
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
134595, 134596, 134597, 134598, 134603, 134608, 134613, 134620, 134621, 134623, 134624, 134625, 134628, 134633, 134636, 134638, 134644, 134648, 134649, 134652, 134653, 134658, 134670 -
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
134607, 134610, 134611, 134612, 134613, 134638, 134642, 134643, 134647, 134651, 134663, 134664, 134666, 134671, 134672, 134673 -
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
-
-
?
phosphopyruvate kinase + H2O
pyruvate kinase + phosphate
-
-
-
-
?
phosphopyruvate kinase + H2O
pyruvate kinase + phosphate
-
regulation of protein kinase during the transition to anoxia and back to the normoxic state
-
-
?
phosphopyruvate kinase + H2O
pyruvate kinase + phosphate
-
-
-
-
?
phosphorylase a + H2O
phosphorylase b + phosphate
-
-
-
-
?
phosphorylase a + H2O
phosphorylase b + phosphate
-
-
-
-
?
phosphorylase a + H2O
phosphorylase b + phosphate
-
-
-
-
r
phosphorylase a + H2O
phosphorylase b + phosphate
-
-
-
-
?
phosphorylase a + H2O
phosphorylase b + phosphate
-
-
-
-
?
phosphorylase a + H2O
phosphorylase b + phosphate
-
-
-
-
?
phosphorylase a + H2O
phosphorylase b + phosphate
-
-
-
-
?
phosphorylase a + H2O
phosphorylase b + phosphate
-
-
-
-
?
phosphorylase a + H2O
phosphorylase b + phosphate
-
-
-
-
?
phosphorylated apoptosis signal-regulating kinase 1 + H2O
apoptosis signal-regulating kinase 1 + phosphate
-
PGAM5 acts as a specific protein Ser/Thr phosphatase that activates apoptosis signal-regulating kinase 1 by dephosphorylation of inhibitory sites (phosphorylation of Thr-838), PGAM5 serves as a specialized activator of apoptosis signal-regulating kinase 1
-
-
?
phosphorylated apoptosis signal-regulating kinase 1 + H2O
apoptosis signal-regulating kinase 1 + phosphate
-
PGAM5 acts as a specific protein Ser/Thr phosphatase that activates apoptosis signal-regulating kinase 1 by dephosphorylation of inhibitory sites (phosphorylation of Thr-838), PGAM5 serves as a specialized activator of apoptosis signal-regulating kinase 1
-
-
?
phosphorylated apoptosis signal-regulating kinase 1 + H2O
apoptosis signal-regulating kinase 1 + phosphate
apoptosis signal-regulating kinase 1 is transiently activated by autophosphorylation at Thr845
-
-
?
phosphorylated ataxia telangiectasia mutated kinase + H2O
ataxia telangiectasia mutated kinase + phosphate
-
-
-
-
?
phosphorylated ataxia telangiectasia mutated kinase + H2O
ataxia telangiectasia mutated kinase + phosphate
-
-
-
?
phosphorylated aurora A + H2O
aurora A + phosphate
-
-
the dephosphorylation leads to inhibition of aurora A
-
?
phosphorylated aurora A + H2O
aurora A + phosphate
-
-
-
-
?
phosphorylated c-Myc + H2O
c-Myc + phosphate
-
-
-
-
?
phosphorylated c-Myc + H2O
c-Myc + phosphate
-
-
the dephosphorylation leads to inhibition of c-Myc
-
?
phosphorylated c-Myc + H2O
c-Myc + phosphate
-
PP2A plays an important role in control of proto-oncogene c-Myc by destabilization of c-Myc and promotion of its ubiquitin-mediated degradation, PP2a has tumor-suppressor activity, c-Myc regulation is essential for normal cell function, overview
-
-
?
phosphorylated c-Myc + H2O
c-Myc + phosphate
-
dephosphorylation of Ser62, PP2A binds to c-Myc via targeting by regulatory subunit B56alpha, overview
-
-
?
phosphorylated Ca2+/calmodulin-dependent protein kinase II + H2O
Ca2+/calmodulin-dependent protein kinase II + phosphate
-
dephosphorylation of the autophosphorylated Thr286, PPM1F negatively regulates the multifunctional Ca2+/calmodulin-dependent protein kinase II, e.g. reducing the phosphorylation of vimentin
-
-
?
phosphorylated Ca2+/calmodulin-dependent protein kinase II + H2O
Ca2+/calmodulin-dependent protein kinase II + phosphate
-
dephosphorylation of the autophosphorylated Thr286 leading to CaMKII inactivation in vitro, PPM1F interacts with multifunctional Ca2+/calmodulin-dependent protein kinase II involving multiple regions independently of the phosphatase activity, analysis overview
-
-
?
phosphorylated cAMP-dependent protein kinase + H2O
cAMP-dependent protein kinase + phosphate
-
phosphorylated at Ser-95
-
-
?
phosphorylated cAMP-dependent protein kinase + H2O
cAMP-dependent protein kinase + phosphate
-
regulatory subunit
-
-
?
phosphorylated casein (PKA) + H2O
casein (PKA) + phosphate
-
-
-
-
?
phosphorylated casein (PKA) + H2O
casein (PKA) + phosphate
-
-
-
-
?
phosphorylated casein (PKA) + H2O
casein (PKA) + phosphate
-
-
-
-
?
phosphorylated casein + H2O
casein + phosphate
-
-
-
-
?
phosphorylated casein + H2O
casein + phosphate
-
-
-
?
phosphorylated casein + H2O
casein + phosphate
-
-
-
-
?
phosphorylated casein + H2O
casein + phosphate
-
-
-
?
phosphorylated casein + H2O
casein + phosphate
-
-
-
-
?
phosphorylated Cav1.2 + H2O
Cav1.2 + phosphate
-
-
the dephosphorylation leads to inhibition of Cav1.2
-
?
phosphorylated Cav1.2 + H2O
Cav1.2 + phosphate
-
PP2A dephosphorylates Cav1.2 at serine 1866
-
-
?
phosphorylated Cav1.2 + H2O
Cav1.2 + phosphate
binding of PP2A to the L-type calcium channel Cav1.2 next to Ser1928, its main PKA site, is critical for Ser1928 dephosphorylation
-
-
?
phosphorylated Cav1.2 + H2O
Cav1.2 + phosphate
binding of PP2A to the L-type calcium channel Cav1.2 next to Ser1928, its main PKA site, is critical for Ser1928 dephosphorylation, interaction study, overview
-
-
?
phosphorylated Chk2 + H2O
Chk2 + phosphate
-
-
-
-
?
phosphorylated Chk2 + H2O
Chk2 + phosphate
-
-
the dephosphorylation leads to inhibition of Chk2
-
?
phosphorylated DNA-dependent protein kinase + H2O
DNA-dependent protein kinase + phosphate
-
-
-
-
?
phosphorylated DNA-dependent protein kinase + H2O
DNA-dependent protein kinase + phosphate
-
activation of DNA-dependent protein kinase to repair DNA double strand breaks by the process of nonhomologous end joining
-
-
?
phosphorylated ERK + H2O
ERK + phosphate
-
-
-
?
phosphorylated ERK + H2O
ERK + phosphate
binds heat shock transcription factor 4 in a complex with ERK, controlling transcription factor DNA binding
-
-
?
phosphorylated ERK-2 + H2O
ERK-2 + phosphate
-
-
-
?
phosphorylated ERK-2 + H2O
ERK-2 + phosphate
preferred substrate
-
-
?
phosphorylated ERK2 + H2O
ERK2 + phosphate
-
-
-
-
?
phosphorylated ERK2 + H2O
ERK2 + phosphate
-
PP2A acts as a gate-keeper of extracellular signal-regulated kinase, ERK, activity in neuronal PC12 cells, the PP2A regulatory subunits Balpha and Bdelta target the PP2A heterotrimer to dephosphorylate and inactivate ERK, silencing of B subunits leads to hyperactivation of ERK stimulated by constitutively active MEK1, overview
-
-
?
phosphorylated ERK2 + H2O
ERK2 + phosphate
-
dephosphorylation of the activation loop threonine of ERK
-
-
?
phosphorylated glycogen phosphorylase a + H2O
glycogen phosphorylase a + phosphate
-
-
-
-
?
phosphorylated glycogen phosphorylase a + H2O
glycogen phosphorylase a + phosphate
-
inactivation of the substrate enzyme, overview
-
-
?
phosphorylated H2AX + H2O
H2AX + phosphate
-
-
the dephosphorylation leads to inhibition of H2AX
-
?
phosphorylated H2AX + H2O
H2AX + phosphate
-
the Pph3p complex is required for dephosphorylation of H2AX, Pph21p (PP2Ac ortholog) is not involved in H2AX dephosphorylation
-
-
?
phosphorylated H2AX + H2O
H2AX + phosphate
-
the Pph3p complex is required for dephosphorylation of H2AX, Pph21p (PP2Ac ortholog) is not involved in H2AX dephosphorylation
-
-
?
phosphorylated histone + H2O
histone + phosphate
-
-
-
-
?
phosphorylated histone + H2O
histone + phosphate
-
-
-
?
phosphorylated histone deacetylase 3 + H2O
histone deacetylase 3 + phosphate
-
dephosphorylation at Ser424, PP4 negatively regulates the activity of histone deacetylase 3 by direct protein-protein interaction also involving the so-repressors N-CoR and SMRT
-
-
?
phosphorylated histone deacetylase 3 + H2O
histone deacetylase 3 + phosphate
-
PP4 regulates histone deacetylase 3, HDAC3, activity by dephosphorylation of Ser424, and by direct protein-protein interaction of active PP4 which is complexed with HDAC3 via the N-terminus of the deacetylase, PP4 is the limiting factor and is not saturating in the complex in vivo
-
-
?
phosphorylated histone deacetylase 3 + H2O
histone deacetylase 3 + phosphate
-
i.e. HDAC3, a class I histone deacetylase, dephosphorylation at Ser424 of the protein kinase CK2 phosphoacceptor site
-
-
?
phosphorylated histone deacetylase 3 + H2O
histone deacetylase 3 + phosphate
-
PP4 dephosphorylates Ser424
-
-
?
phosphorylated histone h1 (PKA) + H2O
histone h1 (PKA) + phosphate
-
-
-
-
?
phosphorylated histone h1 (PKA) + H2O
histone h1 (PKA) + phosphate
-
-
-
-
?
phosphorylated histone h1 (PKA) + H2O
histone h1 (PKA) + phosphate
-
-
-
-
?
phosphorylated histone h1 (PKC) + H2O
histone h1 (PKC) + phosphate
-
-
-
-
?
phosphorylated histone h1 (PKC) + H2O
histone h1 (PKC) + phosphate
-
-
-
-
?
phosphorylated histone h1 (PKC) + H2O
histone h1 (PKC) + phosphate
-
-
-
-
?
phosphorylated hormone-sensitive lipase + H2O
hormone-sensitive lipase + phosphate
-
-
-
-
?
phosphorylated hormone-sensitive lipase + H2O
hormone-sensitive lipase + phosphate
-
-
-
-
?
phosphorylated IkappaB kinase + H2O
IkappaB kinase + phosphate
-
PP2A positively regulates multicomponent Ikappa kinase signaling, eventhough it inhibits its activity by dephosphorylation, positive regulation requires PP2A-IKK complex formation, suppression of the complex formation attenuates IKK T loop phosphorylation and activation, PP2A inhibition attenuates TNFalpha-induced IKK degradation, overview
-
-
?
phosphorylated IkappaB kinase + H2O
IkappaB kinase + phosphate
-
formation of PP2A-IKK complexes, determination of interaction sites
-
-
?
phosphorylated IkappaB kinase + H2O
IkappaB kinase + phosphate
-
PP2A positively regulates multicomponent Ikappa kinase signaling, eventhough it inhibits its activity by dephosphorylation, positive regulation requires PP2A-IKK complex formation, suppression of the complex formation attenuates IKK T loop phosphorylation and activation, PP2A inhibition attenuates TNFalpha-induced IKK degradation, overview
-
-
?
phosphorylated IkappaB kinase + H2O
IkappaB kinase + phosphate
-
formation of PP2A-IKK complexes, determination of interaction sites
-
-
?
phosphorylated ILK1 + H2O
ILK1 + phosphate
-
negative regulation of Wnt signaling
-
-
?
phosphorylated ILK1 + H2O
ILK1 + phosphate
-
Wip1
-
-
?
phosphorylated INAD-protein + H2O
INAD-protein + phosphate
-
INAD-protein is inactivation no afterpotential D-protein
-
-
?
phosphorylated INAD-protein + H2O
INAD-protein + phosphate
-
INAD-protein is inactivation no afterpotential D-protein
-
-
?
phosphorylated JNK protein + H2O
JNK protein + phosphate
-
-
-
-
?
phosphorylated JNK protein + H2O
JNK protein + phosphate
-
-
the dephosphorylation leads to inhibition of JNK protein
-
?
phosphorylated lamban + H2O
lamban + phosphate
-
-
-
-
?
phosphorylated lamban + H2O
lamban + phosphate
-
the substrate enzyme regulates the activity of the Ca2+-ATPase pump on the sarcoplasmic reticulum and is a key regulator of both basal contractility and the heart's beta-agonist responses, overview
dephosphorylated phospholamban exhibits an inhibitory effect on SERCA2a
-
?
phosphorylated lamban + H2O
lamban + phosphate
-
-
-
-
?
phosphorylated lamban + H2O
lamban + phosphate
-
the substrate enzyme regulates the activity of the Ca2+-ATPase pump on the sarcoplasmic reticulum and is a key regulator of both basal contractility and the heart's beta-agonist responses, overview
dephosphorylated phospholamban exhibits an inhibitory effect on SERCA2a
-
?
phosphorylated lamban + H2O
lamban + phosphate
-
-
-
-
?
phosphorylated lamban + H2O
lamban + phosphate
-
the substrate enzyme regulates the activity of the Ca2+-ATPase pump on the sarcoplasmic reticulum and is a key regulator of both basal contractility and the heart's beta-agonist responses, overview
dephosphorylated phospholamban exhibits an inhibitory effect on SERCA2a
-
?
phosphorylated lamban + H2O
lamban + phosphate
-
-
-
-
?
phosphorylated lamban + H2O
lamban + phosphate
-
the substrate enzyme regulates the activity of the Ca2+-ATPase pump on the sarcoplasmic reticulum and is a key regulator of both basal contractility and the heart's beta-agonist responses, overview
dephosphorylated phospholamban exhibits an inhibitory effect on SERCA2a
-
?
phosphorylated mitogen-activated protein kinase Pmk1p + H2O
mitogen-activated protein kinase Pmk1p + phosphate
-
-
-
-
?
phosphorylated mitogen-activated protein kinase Pmk1p + H2O
mitogen-activated protein kinase Pmk1p + phosphate
-
-
-
-
?
phosphorylated MKK4 + H2O
MKK4 + phosphate
-
-
the dephosphorylation leads to inhibition of MKK4
-
?
phosphorylated MKK4 + H2O
MKK4 + phosphate
-
MKK4 is inactivated by the isoforms PP2Calpha and PP2Cbeta
-
-
?
phosphorylated myelin basic protein + H2O
myelin basic protein + phosphate
-
-
-
-
?
phosphorylated myelin basic protein + H2O
myelin basic protein + phosphate
-
-
-
-
?
phosphorylated myelin basic protein + H2O
myelin basic protein + phosphate
-
-
-
-
?
phosphorylated myelin basic protein + H2O
myelin basic protein + phosphate
-
-
-
-
?
phosphorylated myosin light chain + H2O
myosin light chain + phosphate
-
dephosphorylation at Thr696
-
-
?
phosphorylated myosin light chain + H2O
myosin light chain + phosphate
-
isozyme PP1delta regulates smooth muscle relaxation
-
-
?
phosphorylated myosin light chain + H2O
myosin light chain + phosphate
-
isozyme PP1delta, the reaction involves the RVxF-containing myosin phosphatase targeting subunit 1, MYPT1
-
-
?
phosphorylated myosin light chain + H2O
myosin light chain + phosphate
-
isozyme PP1delta regulates smooth muscle relaxation
-
-
?
phosphorylated myosin light chain + H2O
myosin light chain + phosphate
-
isozyme PP1delta, the reaction involves the RVxF-containing myosin phosphatase targeting subunit 1, MYPT1
-
-
?
phosphorylated nucleoside-diphosphate kinase + H2O
nucleoside-diphosphate kinase + phosphate
-
-
-
-
?
phosphorylated nucleoside-diphosphate kinase + H2O
nucleoside-diphosphate kinase + phosphate
-
dephosphorylation of nucleoside-diphosphate kinase leads to loss of enzymatic activity, an efficient mode of posttranslational modification of the enzyme crucial to cellular development. Decreasing order of efficiency: nucleoside-diphosphate kinase from Homo sapiens, nucleoside-diphosphate kinase from Pseudomonas aeruginosa, nucleoside-diphosphate kinase from Escherichia coli, nucleoside-diphosphate kinase from yeast
-
-
?
phosphorylated p38 + H2O
p38 + phosphate
-
-
-
-
?
phosphorylated p38 + H2O
p38 + phosphate
-
-
-
?
phosphorylated p38 + H2O
p38 + phosphate
-
-
-
-
?
phosphorylated p38alpha + H2O
p38alpha + phosphate
-
mediation of a negative feedback loop of the p38 MAPK-p53 signaling pathway
-
-
?
phosphorylated p38alpha + H2O
p38alpha + phosphate
-
substrate is a MAPK, identification of dephosphorylation at Thr residues, dephosphorylation site sequences, activity with wild-type and mutant p38alpha proteins, overview
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
-
-
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
-
the B56-containing PP2A acts partly through p53 suppressing apoptosis
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
-
-
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
-
dephosphorylation of Ser15 by PP1, no activity with PP2A, PP1 inhibition leads to hyperphosphorylation of p53, PP1 has regulatory function
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
-
dephosphorylation of Ser15 by PP1, no activity with PP2A
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
-
-
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
-
dephosphorylation of Ser15 by PP1, no activity with PP2A, PP1 inhibition leads to hyperphosphorylation of p53, PP1 has regulatory function
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
-
dephosphorylation of Ser15 by PP1, no activity with PP2A
-
-
?
phosphorylated penicillin-binding protein + H2O
penicillin-binding protein + phosphate
-
-
-
-
?
phosphorylated penicillin-binding protein + H2O
penicillin-binding protein + phosphate
-
-
-
-
?
phosphorylated phosphorylase a + H2O
phosphorylase a + phosphate
-
-
-
-
?
phosphorylated phosphorylase a + H2O
phosphorylase a + phosphate
-
-
-
-
?
phosphorylated phosphorylase a + H2O
phosphorylase a + phosphate
-
-
-
?
phosphorylated phosphorylase alpha + H2O
phosphorylase alpha + phosphate
-
-
-
?
phosphorylated phosphorylase alpha + H2O
phosphorylase alpha + phosphate
-
-
-
-
?
phosphorylated phosphorylase alpha + H2O
phosphorylase alpha + phosphate
-
-
-
?
phosphorylated phosphorylase alpha + H2O
phosphorylase alpha + phosphate
-
-
-
-
?
phosphorylated phosphorylase alpha + H2O
phosphorylase alpha + phosphate
-
-
-
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
-
-
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
-
-
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
isozyme PP1 preferentially dephosphorylates the beta-subunit of phosphorylase kinase, isozyme PP2 preferentially dephosphorylates the alpha-subunit of phosphorylase kinase
-
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
-
-
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
-
-
-
?
phosphorylated pRb protein + H2O
pRb protein + phosphate
-
-
-
-
?
phosphorylated pRb protein + H2O
pRb protein + phosphate
-
ceramide prevents retinoblastoma gene product pRb protein hyperphosphorylation by PP1 activation, nerve growth factor deprivation in sympathetic neurons leads to inhibition of PP1 and hyperphosphorylation of pRb protein
-
-
?
phosphorylated protein kinase Hs11 + H2O
protein kinase Hs11 + phosphate
-
contributes to its delocalization and destruction
-
-
?
phosphorylated protein kinase Hs11 + H2O
protein kinase Hs11 + phosphate
-
at high Ca2+ concentrations
-
-
?
phosphorylated protein phosphatase inhibitor-1 + H2O
protein phosphatase inhibitor-1 + phosphate
-
-
-
-
?
phosphorylated protein phosphatase inhibitor-1 + H2O
protein phosphatase inhibitor-1 + phosphate
-
-
-
-
?
phosphorylated Prz1 + H2o
Prz1 + phosphate
-
-
-
-
?
phosphorylated Prz1 + H2o
Prz1 + phosphate
-
induction of calcineurin itself and the Pmc1 CXa2+ ATPase
-
-
?
phosphorylated pyruvate dehydrogenase + H2O
pyruvate dehydrogenase + phosphate
-
-
-
-
?
phosphorylated pyruvate dehydrogenase + H2O
pyruvate dehydrogenase + phosphate
-
-
-
-
?
phosphorylated Raf-1 kinase + H2O
Raf 1 kinase + phosphate
-
phosphatase 2A dephosphorylates Raf-1 Ser259 in response to mitogens
-
-
?
phosphorylated Raf-1 kinase + H2O
Raf 1 kinase + phosphate
-
activation of Raf-1 by dephopshorylation at Ser259
-
-
?
phosphorylated Raf-1 kinase + H2O
Raf 1 kinase + phosphate
-
phosphatase 2A dephosphorylates Raf-1 Ser259 in response to mitogens
-
-
?
phosphorylated Raf-1 kinase + H2O
Raf 1 kinase + phosphate
-
activation of Raf-1 by dephopshorylation at Ser259
-
-
?
phosphorylated retinoblastoma protein + H2O
retinoblastoma protein + phosphate
-
-
-
-
?
phosphorylated retinoblastoma protein + H2O
retinoblastoma protein + phosphate
-
-
-
-
?
phosphorylated RNA polymerase II + H2O
RNA polymerase II + phosphate
-
-
-
-
?
phosphorylated RNA polymerase II + H2O
RNA polymerase II + phosphate
-
dephosphorylation of the carboxyterminal domain
-
-
?
phosphorylated securin + H2O
securin + phosphate
-
-
-
-
?
phosphorylated securin + H2O
securin + phosphate
-
-
the dephosphorylation leads to activation of securin
-
?
phosphorylated serine/threonine protein kinase + H2O
serine/threonine protein kinase + phosphate
-
-
-
-
?
phosphorylated serine/threonine protein kinase + H2O
serine/threonine protein kinase + phosphate
-
-
-
-
?
phosphorylated spliceosome-associated protein 155 + H2O
spliceosome-associated protein 155 + phosphate
-
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
-
-
?
phosphorylated spliceosome-associated protein 155 + H2O
spliceosome-associated protein 155 + phosphate
-
i.e. Sap155, a U2 small nuclear ribonucleoprotein particle component
-
-
?
phosphorylated stress-activated protein kinase + H2O
stress-activated protein kinase + phosphate
-
-
-
-
?
phosphorylated stress-activated protein kinase + H2O
stress-activated protein kinase + phosphate
-
-
-
-
?
phosphorylated Tcn1/Crz1 + H2O
Tcn1/Crz1 + phosphate
-
-
-
-
?
phosphorylated Tcn1/Crz1 + H2O
Tcn1/Crz1 + phosphate
-
promotes its translocation into the nucleus and exposure of a transcription activation domain
-
-
?
phosphorylated transforming growth factor-beta-activated kinase 1 + H2O
transforming growth factor-beta-activated kinase 1 + phosphate
-
transforming growth factor-beta-activated kinase 1 is inactivated by the isoforms PP2Cbeta and PP2Cepsilon
-
-
?
phosphorylated transforming growth factor-beta-activated kinase 1 + H2O
transforming growth factor-beta-activated kinase 1 + phosphate
-
Thr187 in transforming growth factor-beta-activated kinase 1 is a major dephosphorylation target of PP2A, PP2A plays a pivotal role as a negative regulator of transforming growth factor-beta-activated kinase 1 activation in response to transforming growth factor-beta 1
-
-
?
Rad53p + H2O
?
-
a complex of Pph3p and Psy2p may dephosphorylate Rad53p after it has been activated and phosphorylated in response to methylmethanesulfonate, but a cisplatin-induced activation and phosphorylation of Rad53p may require a complex of Pph3, Psy4p and Psy2p for dephosphorylation
-
-
?
Rad53p + H2O
?
-
a complex of Pph3p and Psy2p may dephosphorylate Rad53p after it has been activated and phosphorylated in response to methylmethanesulfonate, but a cisplatin-induced activation and phosphorylation of Rad53p may require a complex of Pph3, Psy4p and Psy2p for dephosphorylation
-
-
?
RRA(pS)VA + H2O
RRASVA + phosphate
-
-
-
?
RRA(pS)VA + H2O
RRASVA + phosphate
-
-
-
?
RRA(pT)VA + H2O
RRATVA + phosphate
-
-
-
?
RRA(pT)VA + H2O
RRATVA + phosphate
-
-
-
?
RRA(pT)VA + H2O
RRATVA + phosphate
-
-
-
?
RRA(pT)VA + H2O
RRATVA + phosphate
-
-
-
?
RRApSVA + H2O
?
-
-
-
-
?
RRApSVA + H2O
?
-
-
-
-
?
RRApTVA + H2O
?
-
-
-
-
?
RRApTVA + H2O
?
-
-
-
-
?
RRApTVA + H2O
RRATVA + phosphate
-
-
-
-
?
RRApTVA + H2O
RRATVA + phosphate
-
-
-
-
?
RRApTVA + H2O
RRATVA + phosphate
-
-
-
-
?
RRApTVA + H2O
RRATVA + phosphate
-
-
-
?
RRApTVA + H2O
RRATVA + phosphate
-
-
-
-
?
RRApTVA + H2O
RRATVA + phosphate
-
a protein concentration at 15 ng per reaction was found to be optimal for dephosphorylation of the synthetic peptide RRApTVA, maximum enzyme activity can be achieved in the presence of 100 ng of substrate
-
-
?
RRApTVA + H2O
RRATVA + phosphate
-
-
-
-
?
RRAS(P)VA + H2O
RRASVA + phosphate
-
synthetic substrate
-
-
?
RRAS(P)VA + H2O
RRASVA + phosphate
-
synthetic substrate
-
-
?
RRAT(P)VA + H2O
RRATVA + phosphate
-
synthetic substrate
-
-
?
RRAT(P)VA + H2O
RRATVA + phosphate
-
synthetic substrate
-
-
?
RRLIEDAE(pY)AARG + H2O
RRLIEDAEYAARG + phosphate
-
-
-
?
RRLIEDAE(pY)AARG + H2O
RRLIEDAEYAARG + phosphate
-
-
-
?
synthetic peptides with phosphotyrosyl residues + H2O
synthetic peptides + phosphate
-
-
-
-
?
synthetic peptides with phosphotyrosyl residues + H2O
synthetic peptides + phosphate
-
selectivity toward phosphopeptide substrates
-
-
?
[a peptide]-serine/threonine phosphate + H2O
[a peptide]-serine/threonine + phosphate
-
-
-
?
[a peptide]-serine/threonine phosphate + H2O
[a peptide]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
Streptococcus pneumoniae serotype 4
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
Streptococcus pneumoniae serotype 4 Rx1
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[anti-anti-sigma factor SpoIIAA]-serine/threonine phosphate + H2O
[anti-anti-sigma factor SpoIIAA]-serine/threonine + phosphate
-
-
-
?
[anti-anti-sigma factor SpoIIAA]-serine/threonine phosphate + H2O
[anti-anti-sigma factor SpoIIAA]-serine/threonine + phosphate
-
-
-
?
[anti-sigma factor antagonist protein]-serine/threonine phosphate + H2O
[anti-sigma factor antagonist protein]-serine/threonine + phosphate
-
-
-
?
[anti-sigma factor antagonist protein]-serine/threonine phosphate + H2O
[anti-sigma factor antagonist protein]-serine/threonine + phosphate
-
-
-
?
[aquaporin-2]-serine/threonine phosphate + H2O
[aquaporin-2]-serine/threonine + phosphate
-
-
-
-
?
[aquaporin-2]-serine/threonine phosphate + H2O
[aquaporin-2]-serine/threonine + phosphate
-
-
-
-
?
[aquaporin-2]-serine/threonine phosphate + H2O
[aquaporin-2]-serine/threonine + phosphate
-
-
-
-
?
[CpG]-serine/threonine phosphate + H2O
[CpG]-serine/threonine + phosphate
substrate is a ribosome-associated GTPase
-
-
?
[CpG]-serine/threonine phosphate + H2O
[CpG]-serine/threonine + phosphate
substrate is a ribosome-associated GTPase
-
-
?
[EF-G translation factor]-serine/threonine phosphate + H2O
[EF-G translation factor]-serine/threonine + phosphate
-
-
-
?
[EF-G translation factor]-serine/threonine phosphate + H2O
[EF-G translation factor]-serine/threonine + phosphate
-
-
-
?
[EF-Tu translation factor]-serine/threonine phosphate + H2O
[EF-Tu translation factor]-serine/threonine + phosphate
-
-
-
?
[EF-Tu translation factor]-serine/threonine phosphate + H2O
[EF-Tu translation factor]-serine/threonine + phosphate
-
-
-
?
[EF-Tu translation factor]-serine/threonine phosphate + H2O
[EF-Tu translation factor]-serine/threonine + phosphate
-
-
-
?
[EF-Tu translation factor]-serine/threonine phosphate + H2O
[EF-Tu translation factor]-serine/threonine + phosphate
-
-
-
?
[EF-Tu translation factor]-serine/threonine phosphate + H2O
[EF-Tu translation factor]-serine/threonine + phosphate
-
-
-
?
[EmbR]-serine/threonine phosphate + H2O
[EmbR]-serine/threonine + phosphate
substrate is a transcriptional regulator of embCAB operon
-
-
?
[EmbR]-serine/threonine phosphate + H2O
[EmbR]-serine/threonine + phosphate
substrate is a transcriptional regulator of embCAB operon
-
-
?
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
the substrate is a FHA-domain-containing protein involved in hemolysin-coregulated protein 1 (Hcp1) secretion
-
-
?
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
the substrate is a FHA-domain-containing protein involved in hemolysin-coregulated protein 1 (Hcp1) secretion
-
-
?
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
the substrate is a FHA-domain-containing protein involved in hemolysin-coregulated protein 1 (Hcp1) secretion
-
-
?
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
the substrate is a FHA-domain-containing protein involved in hemolysin-coregulated protein 1 (Hcp1) secretion
-
-
?
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
the substrate is a FHA-domain-containing protein involved in hemolysin-coregulated protein 1 (Hcp1) secretion
-
-
?
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
the substrate is a FHA-domain-containing protein involved in hemolysin-coregulated protein 1 (Hcp1) secretion
-
-
?
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
the substrate is a FHA-domain-containing protein involved in hemolysin-coregulated protein 1 (Hcp1) secretion
-
-
?
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
the substrate is a FHA-domain-containing protein involved in hemolysin-coregulated protein 1 (Hcp1) secretion
-
-
?
[HPr kinase]-serine/threonine phosphate + H2O
[HPr kinase]-serine/threonine + phosphate
-
-
-
?
[HPr kinase]-serine/threonine phosphate + H2O
[HPr kinase]-serine/threonine + phosphate
-
-
-
?
[HPr protein]-serine/threonine phosphate + H2O
[HPr protein]-serine/threonine + phosphate
substrate is a phosphocarrier protein involved in the phosphotransferase system
-
-
?
[HPr protein]-serine/threonine phosphate + H2O
[HPr protein]-serine/threonine + phosphate
substrate is a phosphocarrier protein involved in the phosphotransferase system
-
-
?
[HPr protein]-serine/threonine phosphate + H2O
[HPr protein]-serine/threonine + phosphate
substrate is a phosphocarrier protein involved in the phosphotransferase system
-
-
?
[HPr protein]-serine/threonine phosphate + H2O
[HPr protein]-serine/threonine + phosphate
substrate is a phosphocarrier protein involved in the phosphotransferase system
-
-
?
[HPr protein]-serine/threonine phosphate + H2O
[HPr protein]-serine/threonine + phosphate
substrate is a phosphocarrier protein involved in the phosphotransferase system
-
-
?
[HPr protein]-serine/threonine phosphate + H2O
[HPr protein]-serine/threonine + phosphate
substrate is a phosphocarrier protein involved in the phosphotransferase system
-
-
?
[MAP1B protein]-serine/threonine phosphate + H2O
[MAP1B protein]-serine/threonine + phosphate
-
-
-
?
[MAP1B protein]-serine/threonine phosphate + H2O
[MAP1B protein]-serine/threonine + phosphate
enzyme calcineurin dephosphorylates mode I sites only of MAP1B phosphorylation
-
-
?
[MAP1B protein]-serine/threonine phosphate + H2O
[MAP1B protein]-serine/threonine + phosphate
enzyme PP1 dephosphorylates mode II sites only of MAP1B phosphorylation
-
-
?
[MAP1B protein]-serine/threonine phosphate + H2O
[MAP1B protein]-serine/threonine + phosphate
enzyme PP2A can dephosphorylate both modes of MAP1B phosphorylation
-
-
?
[myelin basic protein]-serine/threonine phosphate + H2O
[myelin basic protein]-serine/threonine + phosphate
-
-
-
-
?
[myelin basic protein]-serine/threonine phosphate + H2O
[myelin basic protein]-serine/threonine + phosphate
-
-
-
?
[P-HLP]-serine/threonine phosphate + H2O
[P-HLP]-serine/threonine + phosphate
substrate is a histone-like protein
-
-
?
[P-HLP]-serine/threonine phosphate + H2O
[P-HLP]-serine/threonine + phosphate
substrate is a histone-like protein
-
-
?
[PapA5]-serine/threonine phosphate + H2O
[PapA5]-serine/threonine + phosphate
-
-
-
?
[PapA5]-serine/threonine phosphate + H2O
[PapA5]-serine/threonine + phosphate
-
-
-
?
[PBPA]-serine/threonine phosphate + H2O
[PBPA]-serine/threonine + phosphate
substrate is a cell wall biosynthesis protein
-
-
?
[PBPA]-serine/threonine phosphate + H2O
[PBPA]-serine/threonine + phosphate
substrate is a cell wall biosynthesis protein
-
-
?
[Pkn5]-serine/threonine phosphate + H2O
[Pkn5]-serine/threonine + phosphate
substrate is a negative effector protein of development, vegetative growth and formation of fruiting bodies
-
-
?
[Pkn5]-serine/threonine phosphate + H2O
[Pkn5]-serine/threonine + phosphate
substrate is a negative effector protein of development, vegetative growth and formation of fruiting bodies
-
-
?
[PknA]-serine/threonine phosphate + H2O
[PknA]-serine/threonine + phosphate
-
-
-
?
[PknA]-serine/threonine phosphate + H2O
[PknA]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling, cell growth and division, cell survival
-
-
?
[PknA]-serine/threonine phosphate + H2O
[PknA]-serine/threonine + phosphate
-
-
-
?
[PknA]-serine/threonine phosphate + H2O
[PknA]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling, cell growth and division, cell survival
-
-
?
[PknB]-serine/threonine phosphate + H2O
[PknB]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling and cell growth
-
-
?
[PknB]-serine/threonine phosphate + H2O
[PknB]-serine/threonine + phosphate
-
substrate is a serine/threonine protein kinase involved in cell signaling
-
-
?
[PrkC]-serine/threonine phosphate + H2O
[PrkC]-serine/threonine + phosphate
substrate PrkC or BA-Stk1 is a serine/threonine protein kinase involved in cell signaling, survival within macrophages, and virulence
-
-
?
[PrkC]-serine/threonine phosphate + H2O
[PrkC]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling, biofilm formation, and sporulation
-
-
?
[PrkC]-serine/threonine phosphate + H2O
[PrkC]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling, biofilm formation, and sporulation
-
-
?
[protein DivIVA]-serine/threonine phosphate + H2O
[protein DivIVA]-serine/threonine + phosphate
Streptococcus pneumoniae serotype 4
a protein substrate of Ser/Thr protein kinase (StkP), as recombinant FLAG-tagged protein
-
-
?
[protein DivIVA]-serine/threonine phosphate + H2O
[protein DivIVA]-serine/threonine + phosphate
a protein substrate of Ser/Thr protein kinase (StkP), as recombinant FLAG-tagged protein
-
-
?
[protein DivIVA]-serine/threonine phosphate + H2O
[protein DivIVA]-serine/threonine + phosphate
Streptococcus pneumoniae serotype 4 Rx1
a protein substrate of Ser/Thr protein kinase (StkP), as recombinant FLAG-tagged protein
-
-
?
[protein DivIVA]-serine/threonine phosphate + H2O
[protein DivIVA]-serine/threonine + phosphate
a protein substrate of Ser/Thr protein kinase (StkP), as recombinant FLAG-tagged protein
-
-
?
[protein I-1]-serine/threonine phosphate + H2O
[protein I-1]-serine/threonine + phosphate
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 I-1]-serine/threonine phosphate + H2O
[protein I-1]-serine/threonine + phosphate
substrate is a regulatory subunit I-1 (PPP1R1A) of phosphatase PP1
-
-
?
[protein Jag]-serine/threonine phosphate + H2O
[protein Jag]-serine/threonine + phosphate
Streptococcus pneumoniae serotype 4
i.e. EloR or Spr1851 protein, a cytoplasmic protein and putative RNA-binding protein
-
-
?
[protein Jag]-serine/threonine phosphate + H2O
[protein Jag]-serine/threonine + phosphate
i.e. EloR or Spr1851 protein, a cytoplasmic protein and putative RNA-binding protein
-
-
?
[protein Jag]-serine/threonine phosphate + H2O
[protein Jag]-serine/threonine + phosphate
Streptococcus pneumoniae serotype 4 Rx1
i.e. EloR or Spr1851 protein, a cytoplasmic protein and putative RNA-binding protein
-
-
?
[protein Jag]-serine/threonine phosphate + H2O
[protein Jag]-serine/threonine + phosphate
i.e. EloR or Spr1851 protein, a cytoplasmic protein and putative RNA-binding protein
-
-
?
[protein LocZ]-serine/threonine phosphate + H2O
[protein locZ]-serine/threonine + phosphate
Streptococcus pneumoniae serotype 4
a protein substrate of Ser/Thr protein kinase (StkP), as recombinant FLAG-tagged protein
-
-
?
[protein LocZ]-serine/threonine phosphate + H2O
[protein locZ]-serine/threonine + phosphate
a protein substrate of Ser/Thr protein kinase (StkP), as recombinant FLAG-tagged protein
-
-
?
[protein LocZ]-serine/threonine phosphate + H2O
[protein locZ]-serine/threonine + phosphate
Streptococcus pneumoniae serotype 4 Rx1
a protein substrate of Ser/Thr protein kinase (StkP), as recombinant FLAG-tagged protein
-
-
?
[protein LocZ]-serine/threonine phosphate + H2O
[protein locZ]-serine/threonine + phosphate
a protein substrate of Ser/Thr protein kinase (StkP), as recombinant FLAG-tagged protein
-
-
?
[protein]-L-serine phosphate + H2O
[protein]-L-serine + phosphate
-
the enzyme dephosphorylates phosphoseryl residues in casein, mixed histones, and phosphorylase a, but not phosphotyrosyl residues in reduced, carboxyamidomethylated and maleylated lysozyme
-
-
?
[protein]-L-serine phosphate + H2O
[protein]-L-serine + phosphate
-
-
-
?
[protein]-L-serine phosphate + H2O
[protein]-L-serine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[SP-STK kinase]-serine/threonine phosphate + H2O
[SP-STK kinase]-serine/threonine + phosphate
-
-
-
?
[SP-STK kinase]-serine/threonine phosphate + H2O
[SP-STK kinase]-serine/threonine + phosphate
-
-
-
?
[SP-STK]-serine/threonine phosphate + H2O
[SP-STK]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling
-
-
?
[SP-STK]-serine/threonine phosphate + H2O
[SP-STK]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling
-
-
?
[Stk1]-serine/threonine phosphate + H2O
[Stk1]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling, membrane integrity, cell division, and cell wall biosynthesis
-
-
?
[Stk1]-serine/threonine phosphate + H2O
[Stk1]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling and cell aggregation
-
-
?
[superoxide dismutase]-serine/threonine phosphate + H2O
[superoxide dismutase]-serine/threonine + phosphate
-
-
-
?
[superoxide dismutase]-serine/threonine phosphate + H2O
[superoxide dismutase]-serine/threonine + phosphate
-
-
-
?
[superoxide dismutase]-serine/threonine phosphate + H2O
[superoxide dismutase]-serine/threonine + phosphate
-
-
-
?
[YegI kinase]-serine/threonine phosphate + H2O
[YegI kinase]-serine/threonine + phosphate
dephosphorylation of autophosphorylated Escherichia coli YegI. Gene yegI encodes the partner kinase YegI of PphC
-
-
?
[YegI kinase]-serine/threonine phosphate + H2O
[YegI kinase]-serine/threonine + phosphate
dephosphorylation of autophosphorylated Escherichia coli YegI. Gene yegI encodes the partner kinase YegI of PphC
-
-
?
additional information
?
-
-
PAPP2C indirectly mediates the dephosphorylation of phytochrome-interacting factor 3 via the dephosphorylation of phytochromes
-
-
?
additional information
?
-
different mutants: mutations in genes involved in the ethylene signal transduction pathway and a mutation at the start of exon 2
-
-
?
additional information
?
-
different mutants: mutations in genes involved in the ethylene signal transduction pathway and a mutation at the start of exon 2
-
-
?
additional information
?
-
-
different mutants: mutations in genes involved in the ethylene signal transduction pathway and a mutation at the start of exon 2
-
-
?
additional information
?
-
-
no activity on p-nitrophenyl phosphate, when assayed at pH 7.5 or at pH 10.5
-
-
?
additional information
?
-
residues at 97-201 are essential for bovine retina CaN subunit A phosphatase activity
-
-
?
additional information
?
-
-
residues at 97-201 are essential for bovine retina CaN subunit A phosphatase activity
-
-
?
additional information
?
-
-
the holoenzyme plays a role in organelle assembly and is essential for maturation of the centrosome, overview, PP4 depletion results in disrupted centrosome maturation and a decreased number of chiasmata between homologous chromosomes during meiosis in oocytes
-
-
?
additional information
?
-
-
GST-tagged PGAM5 does not dephosphorylate phospho-Tyr peptides (like END-pYINASL or DADEpYLIPQQG)
-
-
?
additional information
?
-
-
HLH-11, a member of basic helix-loop-helix proteins, binds to calcineurin catalytic subunit Tax-6, probably regulating TAX-6 as a transcription factor and/or a functional regulator. HLH-11 is involved in regulation of many developmental processes such as cell proliferation and differentiation, sex determination and myogenesis, HLH-11 deletion phenotype, overview
-
-
?
additional information
?
-
the minimal PP1-binding domains of regulators GADD34, PNUTS, and spinophilin bind PP1x02with strong affinities. The catalytic domain PPZ1cat binds GADD34 less effectively, as compared to the phosphatase PP1, largely due to an inability of GADD34552-567 to productively bind the PhiPhi motif binding pocket, pulldown assays, overview. The altered PhiPhi binding pocket and the presence of the Z1-helix negatively impact the binding of the regulators to PPZ1. PPZ1, compared to PP1alpha, does not effectively pull down either PNUTS or spinophilin (about 85% less binding)
-
-
?
additional information
?
-
-
the minimal PP1-binding domains of regulators GADD34, PNUTS, and spinophilin bind PP1x02with strong affinities. The catalytic domain PPZ1cat binds GADD34 less effectively, as compared to the phosphatase PP1, largely due to an inability of GADD34552-567 to productively bind the PhiPhi motif binding pocket, pulldown assays, overview. The altered PhiPhi binding pocket and the presence of the Z1-helix negatively impact the binding of the regulators to PPZ1. PPZ1, compared to PP1alpha, does not effectively pull down either PNUTS or spinophilin (about 85% less binding)
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of diverse cellular processes and signaling pathways including embryonic development, cell proliferation, cell death, circadian rhythm and cancer, overview, knockout of the PP2A regulator alpha4 causes p53-regulated apoptosis correlated with increased phosphorylation of p53 and JNK, PP2A is involved in regulation of PERIOD degradation and de/phosphorylation important in cricadian rhythm, overview
-
-
?
additional information
?
-
-
the holoenzyme plays a role in organelle assembly and is essential for maturation of the centrosome, phylogenetic tree and PPP phosphome, overviewe
-
-
?
additional information
?
-
-
GST-tagged PGAM5 does not dephosphorylate phospho-Tyr peptides (like END-pYINASL or DADEpYLIPQQG)
-
-
?
additional information
?
-
PphC displays low preference for pSer/pThr/pTyr peptides, the minimal activity against phosphopeptides is in contrast to the ability of PphC to dephosphorylate the pSer-containing protein substrate beta-casein. PphC may require additional residues for substrate recognition and/or binding that are not present in the phosphopeptides
-
-
?
additional information
?
-
-
PphC displays low preference for pSer/pThr/pTyr peptides, the minimal activity against phosphopeptides is in contrast to the ability of PphC to dephosphorylate the pSer-containing protein substrate beta-casein. PphC may require additional residues for substrate recognition and/or binding that are not present in the phosphopeptides
-
-
?
additional information
?
-
the enzyme is a dual-specificity Ser/Thr/Tyr phosphatase also exhibiting the activity of EC 3.1.3.48
-
-
?
additional information
?
-
PphC displays low preference for pSer/pThr/pTyr peptides, the minimal activity against phosphopeptides is in contrast to the ability of PphC to dephosphorylate the pSer-containing protein substrate beta-casein. PphC may require additional residues for substrate recognition and/or binding that are not present in the phosphopeptides
-
-
?
additional information
?
-
the enzyme is involved in regulation of many biological processes, e.g. glycogen metabolism, cell-cycle progression, and muscle relaxation, regulatory mechanism involving myosin phosphatase targeting subunit MYPT1 in smooth muscle relaxation, overview
-
-
?
additional information
?
-
myosin phosphatase targeting subunit MYPT1 increases myosine specificity of PP1, interaction and binding structure, overview
-
-
?
additional information
?
-
-
PP1 contains a surface hydrophobic pocket on the catalytic subunit which is important in recognizing cellular regulators via their consensus RVxF motifs, regulation of the enzyme, overview
-
-
?
additional information
?
-
-
PP2A is involved in the maintenance of E-cadherin-mediated cell-cell adhesion through recruitment of IQGAP1, an effector of small GTPase Rac
-
-
?
additional information
?
-
-
PP2A regulates a wide variety of cellular signal transduction pathways, and performs positive regulation of Raf1-MEK1/2-ERK1/2 signaling at multiple steps of the pathway, overview
-
-
?
additional information
?
-
-
PP4 activates c-Jun N-terminal kinase JNK-1 and is required for JNK-1 stability in prostate cancer cells, PP4 is involved in the MAPK signaling pathway, overview
-
-
?
additional information
?
-
-
PP4 is involved in TNFalpha signalling, PP4 down-regulates IRS-4 and mediates TNFalpha-induced IRS-4 degradation, overview
-
-
?
additional information
?
-
PP5 affects many signaling pathways regulating cell growth and cellular stress response
-
-
?
additional information
?
-
-
PP5 affects many signaling pathways regulating cell growth and cellular stress response
-
-
?
additional information
?
-
-
PP5 is involved in MAPK signal pathways, PP5 suppresses the hypoxia-induced ASK-1/MKK-4/JNK signaling via two mechanisms, 1. by association to ASK-1, 2. by suppressing the phosphorylation of MKK-4, JNK, and c-Jun, overview
-
-
?
additional information
?
-
-
Ppp5 is involved in signalling pathways that control cellular responses to stress, glucocorticoids, and DNA damage, molecular basis for N-terminal tetratricopeptide repeat domain TPR-mediated regulation of Ppp5
-
-
?
additional information
?
-
-
regulation and function of the stably associated calcium/calmodulin-dependent protein kinase IV/protein serine/threonine phosphatase 2A signaling complex, PP2A is negatively regulating the kinase, interaction requires the Ca2+/CaM-binding autoinhibitory domain of CaMKIV
-
-
?
additional information
?
-
-
the cystic fibrosis transmembrane conductance regulator, a cAMP-activated chloride channel at the apical surface of epithelia, is regulated by a direct interaction with the protein phosphatase 2A
-
-
?
additional information
?
-
the enzyme is critical in many calcium-dependent signaling transduction pathways
-
-
?
additional information
?
-
-
the enzyme is critical in many calcium-dependent signaling transduction pathways
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of diverse cellular processes and signaling pathways including embryonic development, cell proliferation, cell death, and cancer, overview, PP5 is involved in stress response negatively regulating ASK-1 dependent apoptosis and promoting tumor growth, PP2A is regulated by the small t antigen of SV40 and polyomavirus, and is involved in targeting of nuclear transcription factors, e.g. HAND1 and HAND2, overview
-
-
?
additional information
?
-
-
the holoenzyme plays a role in organelle assembly and is essential for maturation of the centrosome and regulation of chromatin activities, it is involved in spliceosomal assembly via interaction with the survival of motor neuron complexes, PP4 regulates several cellular signalling routes, including the NF-kappaB and the target of rapamycin pathways, PP4 plays a role in DNA damage response and decrease histone deacetylase activity, phylogenetic tree and PPP phosphome, overview
-
-
?
additional information
?
-
-
the Pro33 isoform of integrin beta3 enhances outside-in signaling in platelets by regulating the activation of serine/threonine phosphatases
-
-
?
additional information
?
-
-
direct interaction between the N terminus of Rattus norvegicus adenylyl cyclase AC8 and the active catalytic subunit of PP2A activates the dephosphorylation activity
-
-
?
additional information
?
-
-
PP4 interacts with the TNFalpha-inducible insulin receptor substrate-4, IRS-4, the interaction is increased after TNFalpha-stimulation
-
-
?
additional information
?
-
-
substrate specificity of isozyme PP2Cdelta, overview
-
-
?
additional information
?
-
-
substrate specificity of PP2A isozymes
-
-
?
additional information
?
-
-
the different serine/threonine protein phosphatases are associated to a variety of other proteins, e.g. PP1 has about 50 associated proteins, PP5 contains an extended N-terminal domain with three tetratricopeptide repeat, TPR, motifs which possesses autoinhibitory function and are important for interaction with other proteins
-
-
?
additional information
?
-
the enzyme performs metal-mediated substrate hydrolysis
-
-
?
additional information
?
-
-
the enzyme performs metal-mediated substrate hydrolysis
-
-
?
additional information
?
-
-
dephosphorylates protein kinase C alpha/betaII on threonine 638/641
-
-
?
additional information
?
-
-
no activity on phosphoserine substrates
-
-
?
additional information
?
-
-
phosphothreonine-containing peptides with the sequence pTXpY are physiological substrates
-
-
?
additional information
?
-
-
PP2A potently dephosphorylates the mitotic protein monoclonal 2 site on topoisomerase II alpha
-
-
?
additional information
?
-
-
PP2A does not modify the activity of no receptor potential A-protein
-
-
?
additional information
?
-
-
PP2Ac associates with the integrin alphaIIbbeta3 complex in platelets, the alphaIIb membrane proximal region containing the KVGFFKR sequence can support the direct interaction of PP2Ac
-
-
?
additional information
?
-
PP5 binds the A-subunit of the PP2A holoenzyme, which functions to tether the catalytic (PP2Ac) and substrate targeting B-subunits of PP2A
-
-
?
additional information
?
-
-
PP5 binds the A-subunit of the PP2A holoenzyme, which functions to tether the catalytic (PP2Ac) and substrate targeting B-subunits of PP2A
-
-
?
additional information
?
-
PP5 is a potentially important regulator of both hormone- and stress-induced signaling networks that enable a cell to respond appropriately to genomic stress
-
-
?
additional information
?
-
-
PP5 is a potentially important regulator of both hormone- and stress-induced signaling networks that enable a cell to respond appropriately to genomic stress
-
-
?
additional information
?
-
laforin shows diminished in vitro dephosphorylation of p-nitrophenyl phosphate in the presence of glucose polymers
-
-
?
additional information
?
-
laforin shows diminished in vitro dephosphorylation of p-nitrophenyl phosphate in the presence of glucose polymers
-
-
?
additional information
?
-
laforin shows diminished in vitro dephosphorylation of p-nitrophenyl phosphate in the presence of glucose polymers
-
-
?
additional information
?
-
laforin shows diminished in vitro dephosphorylation of p-nitrophenyl phosphate in the presence of glucose polymers
-
-
?
additional information
?
-
laforin shows diminished in vitro dephosphorylation of p-nitrophenyl phosphate in the presence of glucose polymers
-
-
?
additional information
?
-
laforin shows diminished in vitro dephosphorylation of p-nitrophenyl phosphate in the presence of glucose polymers
-
-
?
additional information
?
-
laforin shows diminished in vitro dephosphorylation of p-nitrophenyl phosphate in the presence of glucose polymers
-
-
?
additional information
?
-
laforin shows diminished in vitro dephosphorylation of p-nitrophenyl phosphate in the presence of glucose polymers
-
-
?
additional information
?
-
laforin shows diminished in vitro dephosphorylation of p-nitrophenyl phosphate in the presence of glucose polymers
-
-
?
additional information
?
-
-
little activity is observed with 4-nitrophenyl sulfate and 4-nitrophenyl thiophosphate
-
-
?
additional information
?
-
malin is an E3 ubiquitin ligase that promotes the degradation of laforin
-
-
?
additional information
?
-
malin is an E3 ubiquitin ligase that promotes the degradation of laforin
-
-
?
additional information
?
-
malin is an E3 ubiquitin ligase that promotes the degradation of laforin
-
-
?
additional information
?
-
malin is an E3 ubiquitin ligase that promotes the degradation of laforin
-
-
?
additional information
?
-
malin is an E3 ubiquitin ligase that promotes the degradation of laforin
-
-
?
additional information
?
-
malin is an E3 ubiquitin ligase that promotes the degradation of laforin
-
-
?
additional information
?
-
malin is an E3 ubiquitin ligase that promotes the degradation of laforin
-
-
?
additional information
?
-
malin is an E3 ubiquitin ligase that promotes the degradation of laforin
-
-
?
additional information
?
-
malin is an E3 ubiquitin ligase that promotes the degradation of laforin
-
-
?
additional information
?
-
MKP-5 does not dephosphorylate ERK
-
-
?
additional information
?
-
MKP-5 does not dephosphorylate ERK
-
-
?
additional information
?
-
MKP-5 does not dephosphorylate ERK
-
-
?
additional information
?
-
MKP-5 does not dephosphorylate ERK
-
-
?
additional information
?
-
MKP-5 does not dephosphorylate ERK
-
-
?
additional information
?
-
MKP-5 does not dephosphorylate ERK
-
-
?
additional information
?
-
MKP-5 does not dephosphorylate ERK
-
-
?
additional information
?
-
MKP-5 does not dephosphorylate ERK
-
-
?
additional information
?
-
MKP-5 does not dephosphorylate ERK
-
-
?
additional information
?
-
-
PP2A dephosphorylates all four 14-3-3 binding sites in the class IIa histone deacetylase 7, PP2A constitutively dephosphorylates histone deacetylase 7 to control its biological functions as a regulator of T cell apoptosis and endothelial cell functions
-
-
?
additional information
?
-
-
physical and functional interaction of the phosphatase calcineurin with a group of modulators, the RCAN protein family, e.g. proteins Cabin1 and AKAP79, a valine-rich region within the RCAN carboxyl region is essential for binding to the docking site in calcineurin, overview. Competition by substrates and modulators for a common docking site appears to be an essential mechanism in the regulation of Ca2+-calcineurin signaling
-
-
?
additional information
?
-
-
regulation of cellular PP1 by phosphorylation of the CPI-17 family, C-kinase-activated PP1 inhibitors, overview
-
-
?
additional information
?
-
-
the enzyme is cleaved by caspase-3, PP1 inhibitor Inh3 harbors 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
-
-
?
additional information
?
-
-
kinesin-8 KIF18A interacts with protein phosphatase 1
-
-
?
additional information
?
-
no activity with RRAYVA, ENDYINASL, DADEYLIPQQG, DPVARTSPLQT, PIMPASPQKGH, and EVFCFSQRRKE
-
-
?
additional information
?
-
the PP2A/Balpha trimeric enzyme interacts with a domain encompassing the microtubule-binding repeats and upstream proline-rich region of the longest adult tau 2N/4R-Tau isoform containing 2 N-terminal inserts (2N) and four microtubule-binding repeats. PP2A is reported to be the only phosphatase mediating dephosphorylation of the neuronal phosphorylated betaIII tubulin isoform, which inhibits MAP2-stimulated microtubule assembly
-
-
?
additional information
?
-
the PP2A/Balpha trimeric enzyme interacts with a domain encompassing the microtubule-binding repeats and upstream proline-rich region of the longest adult tau 2N/4R-Tau isoform containing 2 N-terminal inserts (2N) and four microtubule-binding repeats. PP2A is reported to be the only phosphatase mediating dephosphorylation of the neuronal phosphorylated betaIII tubulin isoform, which inhibits MAP2-stimulated microtubule assembly
-
-
?
additional information
?
-
the PP2A/Balpha trimeric enzyme interacts with a domain encompassing the microtubule-binding repeats and upstream proline-rich region of the longest adult tau 2N/4R-Tau isoform containing 2 N-terminal inserts (2N) and four microtubule-binding repeats. PP2A is reported to be the only phosphatase mediating dephosphorylation of the neuronal phosphorylated betaIII tubulin isoform, which inhibits MAP2-stimulated microtubule assembly
-
-
?
additional information
?
-
although the specificity of the PP1 catalytic domains is low, PP1 dephosphorylates its substrates with high specificity. To achieve this, PP1 interacts with more than 100 distinct regulatory subunits, namely, inhibitory proteins that potently inhibit phosphatase activity by binding and blocking the active site, and targeting proteins, proteins that localize PP1 to distinct regions of the cell while also directly modulating PP1-substrate interactions. Many PP1 targeting subunits, such as NIPP1, enhance the binding of specific substrates. PP1 substrates bind directly to enzyme PP1, bind to other domains that are part of the PP1 regulatory proteins to enhance dephosphorylation or are dephosphorylated because PP1 is localized in proximity to the substrate via its targeting proteins
-
-
?
additional information
?
-
although the specificity of the PP1 catalytic domains is low, PP1 dephosphorylates its substrates with high specificity. To achieve this, PP1 interacts with more than 100 distinct regulatory subunits, namely, inhibitory proteins that potently inhibit phosphatase activity by binding and blocking the active site, and targeting proteins, proteins that localize PP1 to distinct regions of the cell while also directly modulating PP1-substrate interactions. Many PP1 targeting subunits, such as NIPP1, enhance the binding of specific substrates. PP1 substrates bind directly to enzyme PP1, bind to other domains that are part of the PP1 regulatory proteins to enhance dephosphorylation or are dephosphorylated because PP1 is localized in proximity to the substrate via its targeting proteins
-
-
?
additional information
?
-
calcineurin is regulated by calcium, which is required for activation. Calcineurin binds directly to its substrates via protein interaction motifs that are also used by regulatory proteins
-
-
?
additional information
?
-
calcineurin is regulated by calcium, which is required for activation. Calcineurin binds directly to its substrates via protein interaction motifs that are also used by regulatory proteins
-
-
?
additional information
?
-
enzyme PP2A is a major tau and MAP2 phosphatase, but it can only dephosphorylate these phospho-MAPs when they are not bound to microtubules
-
-
?
additional information
?
-
enzyme PP2A is a major tau and MAP2 phosphatase, but it can only dephosphorylate these phospho-MAPs when they are not bound to microtubules
-
-
?
additional information
?
-
enzyme PP2A is a major tau and MAP2 phosphatase, but it can only dephosphorylate these phospho-MAPs when they are not bound to microtubules
-
-
?
additional information
?
-
human protein VHR is a dual specificity protein phosphatase 3, that also exhibits tyrosine phosphatase activity, EC 3.1.3.48
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of diverse cellular processes and signaling pathways including circadian rhythm and apoptosis, overview
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of diverse cellular processes and signaling pathways including embryonic development, cell proliferation, cell death, and cancer, overview, PP5 is involved in stress response negatively regulating ASK-1 dependent apoptosis and promoting tumor growth
-
-
?
additional information
?
-
-
direct interaction between the N terminus of Rattus norvegicus adenylyl cyclase AC8 and the active catalytic subunit of PP2A activates the dephosphorylation activity
-
-
?
additional information
?
-
-
the expression of wild type PP2A catalytic subunit suppresses the MAPK kinase 3 phosphorylation
-
-
?
additional information
?
-
-
calcineurin is a Ca2+/calmodulin-dependent protein phosphatase
-
-
?
additional information
?
-
enzyme PrpC has phosphatase activity in vitro, being able to dephosphorylate the artificial substrate 4-nitrophenyl phosphate, and phospho-Ser/Thr residues in peptides, as well as phospho-alpha-casein
-
-
?
additional information
?
-
-
enzyme PrpC has phosphatase activity in vitro, being able to dephosphorylate the artificial substrate 4-nitrophenyl phosphate, and phospho-Ser/Thr residues in peptides, as well as phospho-alpha-casein
-
-
?
additional information
?
-
enzyme PrpC has phosphatase activity in vitro, being able to dephosphorylate the artificial substrate 4-nitrophenyl phosphate, and phospho-Ser/Thr residues in peptides, as well as phospho-alpha-casein
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of diverse cellular processes and signaling pathways including circadian rhythm, moluating the circadian transcription factor FRQ, and apoptosis, overview
-
-
?
additional information
?
-
in vivo expression and response pattern of PP2A gene to environmental stress
-
-
?
additional information
?
-
in vivo expression and response pattern of PP2A gene to environmental stress
-
-
?
additional information
?
-
in vivo expression and response pattern of PP2A gene to environmental stress
-
-
?
additional information
?
-
-
in vivo expression and response pattern of PP2A gene to environmental stress
-
-
?
additional information
?
-
-
no activity with p-nitrophenyl phosphate
-
-
?
additional information
?
-
-
the enzyme is involved in bacterial swarming activity and biofilm formation, PA3346 is the only of seven orphan response regulators inthe organism that is trans-phosphorylated by HptB
-
-
?
additional information
?
-
-
ceramide-induced cell survival mechanism, overview
-
-
?
additional information
?
-
-
PP2A is involved in central sensitization, PP2A negatively regulates the phosphorylation of N-methyl-D-aspartate, NMDA, receptors in response to capsaicin induction in the spinal cord
-
-
?
additional information
?
-
-
PP2A modulates Akt activity, role of PP2A holoenzyme and subunits in MAPK signaling pathways, overview
-
-
?
additional information
?
-
PP5 acts as an effector in Rac GTPase signalling via interaction of its N-terminal TPR domain with Rac-GTP, PP5 inhibition results in blockage of KCNH2 channel stimulation by thyroid hormone and by Rac in pituitary cells, overview
-
-
?
additional information
?
-
-
dephosphorylates the endotoxic lipopolysaccharide of Escherichia coli 055B5
-
-
?
additional information
?
-
-
PP2A is a multifunctional enzyme, direct interaction with the adenovirus E4orf4 protein via the regulatory subunit initiation virus-induced growth arrest in yeast cells, signal transduction is mediated by Cdc55 interacting with both PP2A catalytic subunit in absence of the Tpd3 subunit and E4orf4, mechanism involving the Tpd3 yeast subunit, overview
-
-
?
additional information
?
-
-
the holoenzyme plays a role in organelle assembly and is essential for maturation of the centrosome, PP4 homologues participate in the nutrient sensing pathway, pathway modeling overview, and confers resistance to the anticancer DNA-binding agents cisplatin and oxaliplatin, phylogenetic tree and PPP phosphome, overview
-
-
?
additional information
?
-
-
PP2A is a multifunctional enzyme, direct interaction with the adenovirus E4orf4 protein via the regulatory subunit
-
-
?
additional information
?
-
-
the enzyme preforms dephosphorylation of phosphoserine, phosphothreonine, and also phosphotyrosine residues
-
-
?
additional information
?
-
SP-PTP possesses a tyrosine phosphatase activity that varies based on the type of substrates and reaction conditions. Enzyme SP-PTP also possesses Ser/Thr phosphatase activity dephosphorylating the autophosphorylated SP-STKK, i.e. the kinase domain of kinase SP-STK
-
-
?
additional information
?
-
SP-PTP possesses a tyrosine phosphatase activity that varies based on the type of substrates and reaction conditions. Enzyme SP-PTP also possesses Ser/Thr phosphatase activity dephosphorylating the autophosphorylated SP-STKK, i.e. the kinase domain of kinase SP-STK
-
-
?
additional information
?
-
SP-PTP possesses a tyrosine phosphatase activity that varies based on the type of substrates and reaction conditions. Enzyme SP-PTP also possesses Ser/Thr phosphatase activity dephosphorylating the autophosphorylated SP-STKK, i.e. the kinase domain of kinase SP-STK
-
-
?
additional information
?
-
no activity with TEVGKRI(pY)RLVGDKN
-
-
?
additional information
?
-
no activity with TEVGKRI(pY)RLVGDKN
-
-
?
additional information
?
-
-
no activity with TEVGKRI(pY)RLVGDKN
-
-
?
additional information
?
-
no activity with TEVGKRI(pY)RLVGDKN
-
-
?
additional information
?
-
the enzyme shows dual specificity, protein tyrosine/serine/threonine phosphatase activity
-
-
?
additional information
?
-
the enzyme shows dual specificity, protein tyrosine/serine/threonine phosphatase activity
-
-
?
additional information
?
-
the enzyme shows dual specificity, protein tyrosine/serine/threonine phosphatase activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase + H2O
fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase + phosphate
-
heterotrimeric phosphatase 2A catalyzing the dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase
-
-
?
myosin light chain phosphate + H2O
myosin light chain + phosphate
-
myosin light chain phosphatase is a specific form of PP1
-
-
?
phospho-Cdk2 + H2O
Cdk6 + phosphate
-
-
-
-
?
phospho-Cdk6 + H2O
Cdk6 + phosphate
-
-
-
-
?
phospho-L-serine + H2O
L-serine + phosphate
-
-
-
-
?
phospho-L-threonine + H2O
L-threonine + phosphate
-
-
-
-
?
phospho-L-tyrosine + H2O
L-tyrosine + phosphate
-
preferred substrate
-
-
?
phospho-MKK + H2O
MKK + phosphate
-
-
-
-
?
phospho-PA3347 + H2O
PA3347 + phosphate
-
dephosphorylation of Ser56 by PA3346
-
-
?
phospho-TAK1 + H2O
TAK1 + phosphate
-
-
-
-
?
phosphocasein + H2O
casein + phosphate
-
-
-
?
phosphoprotein + H2O
protein + phosphate
phosphopyruvate kinase + H2O
pyruvate kinase + phosphate
-
regulation of protein kinase during the transition to anoxia and back to the normoxic state
-
-
?
phosphorylated c-Myc + H2O
c-Myc + phosphate
phosphorylated Ca2+/calmodulin-dependent protein kinase II + H2O
Ca2+/calmodulin-dependent protein kinase II + phosphate
-
dephosphorylation of the autophosphorylated Thr286, PPM1F negatively regulates the multifunctional Ca2+/calmodulin-dependent protein kinase II, e.g. reducing the phosphorylation of vimentin
-
-
?
phosphorylated Cav1.2 + H2O
Cav1.2 + phosphate
binding of PP2A to the L-type calcium channel Cav1.2 next to Ser1928, its main PKA site, is critical for Ser1928 dephosphorylation
-
-
?
phosphorylated Cbp1 + H2o
Cbp1 + phosphate
-
-
-
-
?
phosphorylated cyclin G1 + H2O
cyclin G1 + phosphate
-
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
-
activation of DNA-dependent protein kinase to repair DNA double strand breaks by the process of nonhomologous end joining
-
-
?
phosphorylated Ebola virus VP30 protein + H2O
Ebola virus VP30 protein + phosphate
-
-
-
-
?
phosphorylated ERK1 + H2O
ERK1 + phosphate
-
-
-
-
?
phosphorylated ERK2 + H2O
ERK2 + phosphate
phosphorylated glycogen phosphorylase a + H2O
glycogen phosphorylase a + phosphate
-
inactivation of the substrate enzyme, overview
-
-
?
phosphorylated H2AX + H2O
H2AX + phosphate
phosphorylated High mobility group box 1 protein + H2O
High mobility group box 1 protein + phosphate
-
-
-
-
?
phosphorylated histone deacetylase 3 + H2O
histone deacetylase 3 + phosphate
phosphorylated IkappaB kinase + H2O
IkappaB kinase + phosphate
phosphorylated ILK1 + H2O
ILK1 + phosphate
-
negative regulation of Wnt signaling
-
-
?
phosphorylated lamban + H2O
lamban + phosphate
phosphorylated myosin light chain + H2O
myosin light chain + phosphate
phosphorylated nucleoside-diphosphate kinase + H2O
nucleoside-diphosphate kinase + phosphate
-
dephosphorylation of nucleoside-diphosphate kinase leads to loss of enzymatic activity, an efficient mode of posttranslational modification of the enzyme crucial to cellular development. Decreasing order of efficiency: nucleoside-diphosphate kinase from Homo sapiens, nucleoside-diphosphate kinase from Pseudomonas aeruginosa, nucleoside-diphosphate kinase from Escherichia coli, nucleoside-diphosphate kinase from yeast
-
-
?
phosphorylated p38 + H2O
p38 + phosphate
-
-
-
-
?
phosphorylated p38alpha + H2O
p38alpha + phosphate
-
mediation of a negative feedback loop of the p38 MAPK-p53 signaling pathway
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
phosphorylated penicillin-binding protein + H2O
penicillin-binding protein + phosphate
phosphorylated phosphoenolpyruvate carboxylase + H2O
phosphoenolpyruvate carboxylase + phosphate
-
-
-
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
isozyme PP1 preferentially dephosphorylates the beta-subunit of phosphorylase kinase, isozyme PP2 preferentially dephosphorylates the alpha-subunit of phosphorylase kinase
-
-
?
phosphorylated pRb protein + H2O
pRb protein + phosphate
-
ceramide prevents retinoblastoma gene product pRb protein hyperphosphorylation by PP1 activation, nerve growth factor deprivation in sympathetic neurons leads to inhibition of PP1 and hyperphosphorylation of pRb protein
-
-
?
phosphorylated protein kinase Hs11 + H2O
protein kinase Hs11 + phosphate
-
contributes to its delocalization and destruction
-
-
?
phosphorylated Prz1 + H2o
Prz1 + phosphate
-
induction of calcineurin itself and the Pmc1 CXa2+ ATPase
-
-
?
phosphorylated Raf-1 kinase + H2O
Raf 1 kinase + phosphate
phosphorylated Raf1 + H2O
Raf-1 + phosphate
-
-
-
-
?
phosphorylated rhodopsin + H2O
rhodopsin + phosphate
-
-
-
-
?
phosphorylated RNA polymerase II + H2O
RNA polymerase II + phosphate
-
-
-
-
?
phosphorylated securin + H2O
securin + phosphate
-
-
-
-
?
phosphorylated serine/threonine protein kinase + H2O
serine/threonine protein kinase + phosphate
phosphorylated spliceosome-associated protein 155 + H2O
spliceosome-associated protein 155 + phosphate
-
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
-
-
?
phosphorylated Tcn1/Crz1 + H2O
Tcn1/Crz1 + phosphate
-
promotes its translocation into the nucleus and exposure of a transcription activation domain
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
[AKT1 protein]-serine/threonine phosphate + H2O
[AKT1 protein]-serine/threonine + phosphate
-
-
-
-
?
[anti-anti-sigma factor SpoIIAA]-serine/threonine phosphate + H2O
[anti-anti-sigma factor SpoIIAA]-serine/threonine + phosphate
[anti-sigma factor antagonist protein]-serine/threonine phosphate + H2O
[anti-sigma factor antagonist protein]-serine/threonine + phosphate
[aquaporin-2]-serine/threonine phosphate + H2O
[aquaporin-2]-serine/threonine + phosphate
[ComD]-serine/threonine phosphate + H2O
[ComD]-serine/threonine + phosphate
-
substrate is a competence-specific receptor of the TCS ComDE system
-
-
?
[CpG]-serine/threonine phosphate + H2O
[CpG]-serine/threonine + phosphate
[DivIVA]-serine/threonine phosphate + H2O
[DivIVA]-serine/threonine + phosphate
-
substrate is a protein involved in cell division
-
-
?
[EF-G translation factor]-serine/threonine phosphate + H2O
[EF-G translation factor]-serine/threonine + phosphate
[EF-Tu translation factor]-serine/threonine phosphate + H2O
[EF-Tu translation factor]-serine/threonine + phosphate
[elongation factor 2alpha]-serine/threonine phosphate + H2O
[elongation factor 2alpha]-serine/threonine + phosphate
-
-
-
?
[EmbR]-serine/threonine phosphate + H2O
[EmbR]-serine/threonine + phosphate
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
[GraR]-serine/threonine phosphate + H2O
[GraR]-serine/threonine + phosphate
substrate is a TCS response regulator
-
-
?
[HPr kinase]-serine/threonine phosphate + H2O
[HPr kinase]-serine/threonine + phosphate
[HPr protein]-serine/threonine phosphate + H2O
[HPr protein]-serine/threonine + phosphate
[MAP1B protein]-serine/threonine phosphate + H2O
[MAP1B protein]-serine/threonine + phosphate
[MAP2 protein]-serine/threonine phosphate + H2O
[MAP2 protein]-serine/threonine + phosphate
-
-
-
?
[MapZ]-serine/threonine phosphate + H2O
[MapZ]-serine/threonine + phosphate
-
substrate is a protein involved in cell division
-
-
?
[MgrA]-serine/threonine phosphate + H2O
[MgrA]-serine/threonine + phosphate
substrate is a global transcriptional regulator
-
-
?
[MurC]-serine/threonine phosphate + H2O
[MurC]-serine/threonine + phosphate
-
substrate is a protein involved in peptydoglycan synthesis
-
-
?
[P-HLP]-serine/threonine phosphate + H2O
[P-HLP]-serine/threonine + phosphate
[P35]-serine/threonine phosphate + H2O
[P35]-serine/threonine + phosphate
substrate is a Mn2+-dependent inorganic diphosphatase
-
-
?
[PapA5]-serine/threonine phosphate + H2O
[PapA5]-serine/threonine + phosphate
[PBPA]-serine/threonine phosphate + H2O
[PBPA]-serine/threonine + phosphate
[Pkn5]-serine/threonine phosphate + H2O
[Pkn5]-serine/threonine + phosphate
[PknA]-serine/threonine phosphate + H2O
[PknA]-serine/threonine + phosphate
[PknB]-serine/threonine phosphate + H2O
[PknB]-serine/threonine + phosphate
[PknH]-serine/threonine phosphate + H2O
[PknH]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling and cell growth
-
-
?
[PknJ]-serine/threonine phosphate + H2O
[PknJ]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling and cell growth
-
-
?
[PpaC]-serine/threonine phosphate + H2O
[PpaC]-serine/threonine + phosphate
substrate is an inorganic diphosphatase
-
-
?
[PrkC]-serine/threonine phosphate + H2O
[PrkC]-serine/threonine + phosphate
[PrkD]-serine/threonine phosphate + H2O
[PrkD]-serine/threonine + phosphate
substrate PrkD is a dual-specificity tyrosine phosphorylation-regulated kinase
-
-
?
[PrkG]-serine/threonine phosphate + H2O
[PrkG]-serine/threonine + phosphate
substrate PrkG is a dual-specificity tyrosine phosphorylation-regulated kinase
-
-
?
[protein I-1]-serine/threonine phosphate + H2O
[protein I-1]-serine/threonine + phosphate
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]-L-serine phosphate + H2O
[protein]-L-serine + phosphate
[protein]-L-threonine phosphate + H2O
[protein]-L-threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
[PurA]-serine/threonine phosphate + H2O
[PurA]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling and cell aggregation
-
-
?
[PykA]-serine/threonine phosphate + H2O
[PykA]-serine/threonine + phosphate
i.e. pyruvate kinase
-
-
?
[RitR]-serine/threonine phosphate + H2O
[RitR]-serine/threonine + phosphate
-
substrate is a transcriptional regulator
-
-
?
[RR06]-serine/threonine phosphate + H2O
[RR06]-serine/threonine + phosphate
-
substrate is a TCS response regulator
-
-
?
[Rv0019c]-serine/threonine phosphate + H2O
[Rv0019c]-serine/threonine + phosphate
substrate is a FHA-domain-containing protein interacting with FtsZ, GtsQ, and PapA5, cell division
-
-
?
[S-adenosylhomocysteine hydrolase]-serine/threonine phosphate + H2O
[S-adenosylhomocysteine hydrolase]-serine/threonine + phosphate
-
-
-
?
[SP-STK kinase]-serine/threonine phosphate + H2O
[SP-STK kinase]-serine/threonine + phosphate
[SP-STK]-serine/threonine phosphate + H2O
[SP-STK]-serine/threonine + phosphate
[Stk1]-serine/threonine phosphate + H2O
[Stk1]-serine/threonine + phosphate
[StkP]-serine/threonine phosphate + H2O
[StkP]-serine/threonine + phosphate
-
substrate is a serine/threonine protein kinase involved in cell signaling
-
-
?
[Stk]-serine/threonine phosphate + H2O
[Stk]-serine/threonine + phosphate
-
i.e. Stk P5AP, the substrate is a serine/threonine protein kinase involved in cell signaling, antibiotic resistance, and peptydoglycan biosynthesis
-
-
?
[superoxide dismutase]-serine/threonine phosphate + H2O
[superoxide dismutase]-serine/threonine + phosphate
[tau protein]-serine/threonine phosphate + H2O
[tau protein]-serine/threonine + phosphate
-
-
-
?
[tubulin]-serine/threonine phosphate + H2O
[tubulin]-serine/threonine + phosphate
PP2A preferentially dephosphorylates unassembled tubulin
-
-
?
[YegI kinase]-serine/threonine phosphate + H2O
[YegI kinase]-serine/threonine + phosphate
[YezB]-serine/threonine phosphate + H2O
[YezB]-serine/threonine + phosphate
-
-
-
?
additional information
?
-
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
modulation of pyruvate dehydrogenase complex
-
-
?
phosphoprotein + H2O
protein + phosphate
-
phosphatase PP3 stimulates the initiation of DNA-synthesis
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
role in cAMP catabolism
-
-
?
phosphoprotein + H2O
protein + phosphate
-
role of phosphatases in smooth muscle contractile systems
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
capable of dephosphorylating the major proteins involved in control of glycogen metabolism, glycolysis, gluconeogenesis, aromatic amino acid breakdown, fatty acid, cholesterol, and protein synthesis
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
involved in the intracellular mechanism through which adrenocortical steroidogenesis is regulated, acting at a point after cAMP generation and action but proximal to the side-chain cleavage of cholesterol
-
-
?
phosphoprotein + H2O
protein + phosphate
-
involved in regulating exocytosis from the rat parotid gland via a cAMP-mediated process
-
-
?
phosphoprotein + H2O
protein + phosphate
-
control of cholesterol genesis
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphorylated c-Myc + H2O
c-Myc + phosphate
-
-
-
-
?
phosphorylated c-Myc + H2O
c-Myc + phosphate
-
PP2A plays an important role in control of proto-oncogene c-Myc by destabilization of c-Myc and promotion of its ubiquitin-mediated degradation, PP2a has tumor-suppressor activity, c-Myc regulation is essential for normal cell function, overview
-
-
?
phosphorylated ERK2 + H2O
ERK2 + phosphate
-
-
-
-
?
phosphorylated ERK2 + H2O
ERK2 + phosphate
-
PP2A acts as a gate-keeper of extracellular signal-regulated kinase, ERK, activity in neuronal PC12 cells, the PP2A regulatory subunits Balpha and Bdelta target the PP2A heterotrimer to dephosphorylate and inactivate ERK, silencing of B subunits leads to hyperactivation of ERK stimulated by constitutively active MEK1, overview
-
-
?
phosphorylated H2AX + H2O
H2AX + phosphate
-
the Pph3p complex is required for dephosphorylation of H2AX, Pph21p (PP2Ac ortholog) is not involved in H2AX dephosphorylation
-
-
?
phosphorylated H2AX + H2O
H2AX + phosphate
-
the Pph3p complex is required for dephosphorylation of H2AX, Pph21p (PP2Ac ortholog) is not involved in H2AX dephosphorylation
-
-
?
phosphorylated histone deacetylase 3 + H2O
histone deacetylase 3 + phosphate
-
dephosphorylation at Ser424, PP4 negatively regulates the activity of histone deacetylase 3 by direct protein-protein interaction also involving the so-repressors N-CoR and SMRT
-
-
?
phosphorylated histone deacetylase 3 + H2O
histone deacetylase 3 + phosphate
-
PP4 regulates histone deacetylase 3, HDAC3, activity by dephosphorylation of Ser424, and by direct protein-protein interaction of active PP4 which is complexed with HDAC3 via the N-terminus of the deacetylase, PP4 is the limiting factor and is not saturating in the complex in vivo
-
-
?
phosphorylated IkappaB kinase + H2O
IkappaB kinase + phosphate
-
PP2A positively regulates multicomponent Ikappa kinase signaling, eventhough it inhibits its activity by dephosphorylation, positive regulation requires PP2A-IKK complex formation, suppression of the complex formation attenuates IKK T loop phosphorylation and activation, PP2A inhibition attenuates TNFalpha-induced IKK degradation, overview
-
-
?
phosphorylated IkappaB kinase + H2O
IkappaB kinase + phosphate
-
PP2A positively regulates multicomponent Ikappa kinase signaling, eventhough it inhibits its activity by dephosphorylation, positive regulation requires PP2A-IKK complex formation, suppression of the complex formation attenuates IKK T loop phosphorylation and activation, PP2A inhibition attenuates TNFalpha-induced IKK degradation, overview
-
-
?
phosphorylated lamban + H2O
lamban + phosphate
-
the substrate enzyme regulates the activity of the Ca2+-ATPase pump on the sarcoplasmic reticulum and is a key regulator of both basal contractility and the heart's beta-agonist responses, overview
dephosphorylated phospholamban exhibits an inhibitory effect on SERCA2a
-
?
phosphorylated lamban + H2O
lamban + phosphate
-
-
-
-
?
phosphorylated lamban + H2O
lamban + phosphate
-
the substrate enzyme regulates the activity of the Ca2+-ATPase pump on the sarcoplasmic reticulum and is a key regulator of both basal contractility and the heart's beta-agonist responses, overview
dephosphorylated phospholamban exhibits an inhibitory effect on SERCA2a
-
?
phosphorylated lamban + H2O
lamban + phosphate
-
the substrate enzyme regulates the activity of the Ca2+-ATPase pump on the sarcoplasmic reticulum and is a key regulator of both basal contractility and the heart's beta-agonist responses, overview
dephosphorylated phospholamban exhibits an inhibitory effect on SERCA2a
-
?
phosphorylated lamban + H2O
lamban + phosphate
-
the substrate enzyme regulates the activity of the Ca2+-ATPase pump on the sarcoplasmic reticulum and is a key regulator of both basal contractility and the heart's beta-agonist responses, overview
dephosphorylated phospholamban exhibits an inhibitory effect on SERCA2a
-
?
phosphorylated myosin light chain + H2O
myosin light chain + phosphate
-
dephosphorylation at Thr696
-
-
?
phosphorylated myosin light chain + H2O
myosin light chain + phosphate
-
isozyme PP1delta regulates smooth muscle relaxation
-
-
?
phosphorylated myosin light chain + H2O
myosin light chain + phosphate
-
isozyme PP1delta regulates smooth muscle relaxation
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
-
the B56-containing PP2A acts partly through p53 suppressing apoptosis
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
-
dephosphorylation of Ser15 by PP1, no activity with PP2A, PP1 inhibition leads to hyperphosphorylation of p53, PP1 has regulatory function
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
-
-
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
-
dephosphorylation of Ser15 by PP1, no activity with PP2A, PP1 inhibition leads to hyperphosphorylation of p53, PP1 has regulatory function
-
-
?
phosphorylated penicillin-binding protein + H2O
penicillin-binding protein + phosphate
-
-
-
-
?
phosphorylated penicillin-binding protein + H2O
penicillin-binding protein + phosphate
-
-
-
-
?
phosphorylated Raf-1 kinase + H2O
Raf 1 kinase + phosphate
-
phosphatase 2A dephosphorylates Raf-1 Ser259 in response to mitogens
-
-
?
phosphorylated Raf-1 kinase + H2O
Raf 1 kinase + phosphate
-
phosphatase 2A dephosphorylates Raf-1 Ser259 in response to mitogens
-
-
?
phosphorylated serine/threonine protein kinase + H2O
serine/threonine protein kinase + phosphate
-
-
-
-
?
phosphorylated serine/threonine protein kinase + H2O
serine/threonine protein kinase + phosphate
-
-
-
-
?
Rad53p + H2O
?
-
a complex of Pph3p and Psy2p may dephosphorylate Rad53p after it has been activated and phosphorylated in response to methylmethanesulfonate, but a cisplatin-induced activation and phosphorylation of Rad53p may require a complex of Pph3, Psy4p and Psy2p for dephosphorylation
-
-
?
Rad53p + H2O
?
-
a complex of Pph3p and Psy2p may dephosphorylate Rad53p after it has been activated and phosphorylated in response to methylmethanesulfonate, but a cisplatin-induced activation and phosphorylation of Rad53p may require a complex of Pph3, Psy4p and Psy2p for dephosphorylation
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
Streptococcus pneumoniae serotype 4
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
Streptococcus pneumoniae serotype 4 Rx1
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
[anti-anti-sigma factor SpoIIAA]-serine/threonine phosphate + H2O
[anti-anti-sigma factor SpoIIAA]-serine/threonine + phosphate
-
-
-
?
[anti-anti-sigma factor SpoIIAA]-serine/threonine phosphate + H2O
[anti-anti-sigma factor SpoIIAA]-serine/threonine + phosphate
-
-
-
?
[anti-sigma factor antagonist protein]-serine/threonine phosphate + H2O
[anti-sigma factor antagonist protein]-serine/threonine + phosphate
-
-
-
?
[anti-sigma factor antagonist protein]-serine/threonine phosphate + H2O
[anti-sigma factor antagonist protein]-serine/threonine + phosphate
-
-
-
?
[aquaporin-2]-serine/threonine phosphate + H2O
[aquaporin-2]-serine/threonine + phosphate
-
-
-
-
?
[aquaporin-2]-serine/threonine phosphate + H2O
[aquaporin-2]-serine/threonine + phosphate
-
-
-
-
?
[aquaporin-2]-serine/threonine phosphate + H2O
[aquaporin-2]-serine/threonine + phosphate
-
-
-
-
?
[CpG]-serine/threonine phosphate + H2O
[CpG]-serine/threonine + phosphate
substrate is a ribosome-associated GTPase
-
-
?
[CpG]-serine/threonine phosphate + H2O
[CpG]-serine/threonine + phosphate
substrate is a ribosome-associated GTPase
-
-
?
[EF-G translation factor]-serine/threonine phosphate + H2O
[EF-G translation factor]-serine/threonine + phosphate
-
-
-
?
[EF-G translation factor]-serine/threonine phosphate + H2O
[EF-G translation factor]-serine/threonine + phosphate
-
-
-
?
[EF-Tu translation factor]-serine/threonine phosphate + H2O
[EF-Tu translation factor]-serine/threonine + phosphate
-
-
-
?
[EF-Tu translation factor]-serine/threonine phosphate + H2O
[EF-Tu translation factor]-serine/threonine + phosphate
-
-
-
?
[EF-Tu translation factor]-serine/threonine phosphate + H2O
[EF-Tu translation factor]-serine/threonine + phosphate
-
-
-
?
[EF-Tu translation factor]-serine/threonine phosphate + H2O
[EF-Tu translation factor]-serine/threonine + phosphate
-
-
-
?
[EF-Tu translation factor]-serine/threonine phosphate + H2O
[EF-Tu translation factor]-serine/threonine + phosphate
-
-
-
?
[EmbR]-serine/threonine phosphate + H2O
[EmbR]-serine/threonine + phosphate
substrate is a transcriptional regulator of embCAB operon
-
-
?
[EmbR]-serine/threonine phosphate + H2O
[EmbR]-serine/threonine + phosphate
substrate is a transcriptional regulator of embCAB operon
-
-
?
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
the substrate is a FHA-domain-containing protein involved in hemolysin-coregulated protein 1 (Hcp1) secretion
-
-
?
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
the substrate is a FHA-domain-containing protein involved in hemolysin-coregulated protein 1 (Hcp1) secretion
-
-
?
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
the substrate is a FHA-domain-containing protein involved in hemolysin-coregulated protein 1 (Hcp1) secretion
-
-
?
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
the substrate is a FHA-domain-containing protein involved in hemolysin-coregulated protein 1 (Hcp1) secretion
-
-
?
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
the substrate is a FHA-domain-containing protein involved in hemolysin-coregulated protein 1 (Hcp1) secretion
-
-
?
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
the substrate is a FHA-domain-containing protein involved in hemolysin-coregulated protein 1 (Hcp1) secretion
-
-
?
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
the substrate is a FHA-domain-containing protein involved in hemolysin-coregulated protein 1 (Hcp1) secretion
-
-
?
[FHA-1]-serine/threonine phosphate + H2O
[FHA-1]-serine/threonine + phosphate
the substrate is a FHA-domain-containing protein involved in hemolysin-coregulated protein 1 (Hcp1) secretion
-
-
?
[HPr kinase]-serine/threonine phosphate + H2O
[HPr kinase]-serine/threonine + phosphate
-
-
-
?
[HPr kinase]-serine/threonine phosphate + H2O
[HPr kinase]-serine/threonine + phosphate
-
-
-
?
[HPr protein]-serine/threonine phosphate + H2O
[HPr protein]-serine/threonine + phosphate
substrate is a phosphocarrier protein involved in the phosphotransferase system
-
-
?
[HPr protein]-serine/threonine phosphate + H2O
[HPr protein]-serine/threonine + phosphate
substrate is a phosphocarrier protein involved in the phosphotransferase system
-
-
?
[HPr protein]-serine/threonine phosphate + H2O
[HPr protein]-serine/threonine + phosphate
substrate is a phosphocarrier protein involved in the phosphotransferase system
-
-
?
[HPr protein]-serine/threonine phosphate + H2O
[HPr protein]-serine/threonine + phosphate
substrate is a phosphocarrier protein involved in the phosphotransferase system
-
-
?
[HPr protein]-serine/threonine phosphate + H2O
[HPr protein]-serine/threonine + phosphate
substrate is a phosphocarrier protein involved in the phosphotransferase system
-
-
?
[HPr protein]-serine/threonine phosphate + H2O
[HPr protein]-serine/threonine + phosphate
substrate is a phosphocarrier protein involved in the phosphotransferase system
-
-
?
[MAP1B protein]-serine/threonine phosphate + H2O
[MAP1B protein]-serine/threonine + phosphate
enzyme calcineurin dephosphorylates mode I sites only of MAP1B phosphorylation
-
-
?
[MAP1B protein]-serine/threonine phosphate + H2O
[MAP1B protein]-serine/threonine + phosphate
enzyme PP1 dephosphorylates mode II sites only of MAP1B phosphorylation
-
-
?
[MAP1B protein]-serine/threonine phosphate + H2O
[MAP1B protein]-serine/threonine + phosphate
enzyme PP2A can dephosphorylate both modes of MAP1B phosphorylation
-
-
?
[P-HLP]-serine/threonine phosphate + H2O
[P-HLP]-serine/threonine + phosphate
substrate is a histone-like protein
-
-
?
[P-HLP]-serine/threonine phosphate + H2O
[P-HLP]-serine/threonine + phosphate
substrate is a histone-like protein
-
-
?
[PapA5]-serine/threonine phosphate + H2O
[PapA5]-serine/threonine + phosphate
-
-
-
?
[PapA5]-serine/threonine phosphate + H2O
[PapA5]-serine/threonine + phosphate
-
-
-
?
[PBPA]-serine/threonine phosphate + H2O
[PBPA]-serine/threonine + phosphate
substrate is a cell wall biosynthesis protein
-
-
?
[PBPA]-serine/threonine phosphate + H2O
[PBPA]-serine/threonine + phosphate
substrate is a cell wall biosynthesis protein
-
-
?
[Pkn5]-serine/threonine phosphate + H2O
[Pkn5]-serine/threonine + phosphate
substrate is a negative effector protein of development, vegetative growth and formation of fruiting bodies
-
-
?
[Pkn5]-serine/threonine phosphate + H2O
[Pkn5]-serine/threonine + phosphate
substrate is a negative effector protein of development, vegetative growth and formation of fruiting bodies
-
-
?
[PknA]-serine/threonine phosphate + H2O
[PknA]-serine/threonine + phosphate
-
-
-
?
[PknA]-serine/threonine phosphate + H2O
[PknA]-serine/threonine + phosphate
-
-
-
?
[PknB]-serine/threonine phosphate + H2O
[PknB]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling and cell growth
-
-
?
[PknB]-serine/threonine phosphate + H2O
[PknB]-serine/threonine + phosphate
-
substrate is a serine/threonine protein kinase involved in cell signaling
-
-
?
[PrkC]-serine/threonine phosphate + H2O
[PrkC]-serine/threonine + phosphate
substrate PrkC or BA-Stk1 is a serine/threonine protein kinase involved in cell signaling, survival within macrophages, and virulence
-
-
?
[PrkC]-serine/threonine phosphate + H2O
[PrkC]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling, biofilm formation, and sporulation
-
-
?
[PrkC]-serine/threonine phosphate + H2O
[PrkC]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling, biofilm formation, and sporulation
-
-
?
[protein]-L-serine phosphate + H2O
[protein]-L-serine + phosphate
-
-
-
?
[protein]-L-serine phosphate + H2O
[protein]-L-serine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[SP-STK kinase]-serine/threonine phosphate + H2O
[SP-STK kinase]-serine/threonine + phosphate
-
-
-
?
[SP-STK kinase]-serine/threonine phosphate + H2O
[SP-STK kinase]-serine/threonine + phosphate
-
-
-
?
[SP-STK]-serine/threonine phosphate + H2O
[SP-STK]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling
-
-
?
[SP-STK]-serine/threonine phosphate + H2O
[SP-STK]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling
-
-
?
[Stk1]-serine/threonine phosphate + H2O
[Stk1]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling, membrane integrity, cell division, and cell wall biosynthesis
-
-
?
[Stk1]-serine/threonine phosphate + H2O
[Stk1]-serine/threonine + phosphate
substrate is a serine/threonine protein kinase involved in cell signaling and cell aggregation
-
-
?
[superoxide dismutase]-serine/threonine phosphate + H2O
[superoxide dismutase]-serine/threonine + phosphate
-
-
-
?
[superoxide dismutase]-serine/threonine phosphate + H2O
[superoxide dismutase]-serine/threonine + phosphate
-
-
-
?
[superoxide dismutase]-serine/threonine phosphate + H2O
[superoxide dismutase]-serine/threonine + phosphate
-
-
-
?
[YegI kinase]-serine/threonine phosphate + H2O
[YegI kinase]-serine/threonine + phosphate
dephosphorylation of autophosphorylated Escherichia coli YegI. Gene yegI encodes the partner kinase YegI of PphC
-
-
?
[YegI kinase]-serine/threonine phosphate + H2O
[YegI kinase]-serine/threonine + phosphate
dephosphorylation of autophosphorylated Escherichia coli YegI. Gene yegI encodes the partner kinase YegI of PphC
-
-
?
additional information
?
-
different mutants: mutations in genes involved in the ethylene signal transduction pathway and a mutation at the start of exon 2
-
-
?
additional information
?
-
different mutants: mutations in genes involved in the ethylene signal transduction pathway and a mutation at the start of exon 2
-
-
?
additional information
?
-
-
different mutants: mutations in genes involved in the ethylene signal transduction pathway and a mutation at the start of exon 2
-
-
?
additional information
?
-
-
the holoenzyme plays a role in organelle assembly and is essential for maturation of the centrosome, overview, PP4 depletion results in disrupted centrosome maturation and a decreased number of chiasmata between homologous chromosomes during meiosis in oocytes
-
-
?
additional information
?
-
the minimal PP1-binding domains of regulators GADD34, PNUTS, and spinophilin bind PP1x02with strong affinities. The catalytic domain PPZ1cat binds GADD34 less effectively, as compared to the phosphatase PP1, largely due to an inability of GADD34552-567 to productively bind the PhiPhi motif binding pocket, pulldown assays, overview. The altered PhiPhi binding pocket and the presence of the Z1-helix negatively impact the binding of the regulators to PPZ1. PPZ1, compared to PP1alpha, does not effectively pull down either PNUTS or spinophilin (about 85% less binding)
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-
?
additional information
?
-
-
the minimal PP1-binding domains of regulators GADD34, PNUTS, and spinophilin bind PP1x02with strong affinities. The catalytic domain PPZ1cat binds GADD34 less effectively, as compared to the phosphatase PP1, largely due to an inability of GADD34552-567 to productively bind the PhiPhi motif binding pocket, pulldown assays, overview. The altered PhiPhi binding pocket and the presence of the Z1-helix negatively impact the binding of the regulators to PPZ1. PPZ1, compared to PP1alpha, does not effectively pull down either PNUTS or spinophilin (about 85% less binding)
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-
?
additional information
?
-
-
the enzyme is involved in regulation of diverse cellular processes and signaling pathways including embryonic development, cell proliferation, cell death, circadian rhythm and cancer, overview, knockout of the PP2A regulator alpha4 causes p53-regulated apoptosis correlated with increased phosphorylation of p53 and JNK, PP2A is involved in regulation of PERIOD degradation and de/phosphorylation important in cricadian rhythm, overview
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-
?
additional information
?
-
-
the holoenzyme plays a role in organelle assembly and is essential for maturation of the centrosome, phylogenetic tree and PPP phosphome, overviewe
-
-
?
additional information
?
-
the enzyme is involved in regulation of many biological processes, e.g. glycogen metabolism, cell-cycle progression, and muscle relaxation, regulatory mechanism involving myosin phosphatase targeting subunit MYPT1 in smooth muscle relaxation, overview
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-
?
additional information
?
-
-
PP1 contains a surface hydrophobic pocket on the catalytic subunit which is important in recognizing cellular regulators via their consensus RVxF motifs, regulation of the enzyme, overview
-
-
?
additional information
?
-
-
PP2A is involved in the maintenance of E-cadherin-mediated cell-cell adhesion through recruitment of IQGAP1, an effector of small GTPase Rac
-
-
?
additional information
?
-
-
PP2A regulates a wide variety of cellular signal transduction pathways, and performs positive regulation of Raf1-MEK1/2-ERK1/2 signaling at multiple steps of the pathway, overview
-
-
?
additional information
?
-
-
PP4 activates c-Jun N-terminal kinase JNK-1 and is required for JNK-1 stability in prostate cancer cells, PP4 is involved in the MAPK signaling pathway, overview
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-
?
additional information
?
-
-
PP4 is involved in TNFalpha signalling, PP4 down-regulates IRS-4 and mediates TNFalpha-induced IRS-4 degradation, overview
-
-
?
additional information
?
-
PP5 affects many signaling pathways regulating cell growth and cellular stress response
-
-
?
additional information
?
-
-
PP5 affects many signaling pathways regulating cell growth and cellular stress response
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-
?
additional information
?
-
-
PP5 is involved in MAPK signal pathways, PP5 suppresses the hypoxia-induced ASK-1/MKK-4/JNK signaling via two mechanisms, 1. by association to ASK-1, 2. by suppressing the phosphorylation of MKK-4, JNK, and c-Jun, overview
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-
?
additional information
?
-
-
Ppp5 is involved in signalling pathways that control cellular responses to stress, glucocorticoids, and DNA damage, molecular basis for N-terminal tetratricopeptide repeat domain TPR-mediated regulation of Ppp5
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-
?
additional information
?
-
-
regulation and function of the stably associated calcium/calmodulin-dependent protein kinase IV/protein serine/threonine phosphatase 2A signaling complex, PP2A is negatively regulating the kinase, interaction requires the Ca2+/CaM-binding autoinhibitory domain of CaMKIV
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?
additional information
?
-
-
the cystic fibrosis transmembrane conductance regulator, a cAMP-activated chloride channel at the apical surface of epithelia, is regulated by a direct interaction with the protein phosphatase 2A
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?
additional information
?
-
the enzyme is critical in many calcium-dependent signaling transduction pathways
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-
?
additional information
?
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-
the enzyme is critical in many calcium-dependent signaling transduction pathways
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?
additional information
?
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-
the enzyme is involved in regulation of diverse cellular processes and signaling pathways including embryonic development, cell proliferation, cell death, and cancer, overview, PP5 is involved in stress response negatively regulating ASK-1 dependent apoptosis and promoting tumor growth, PP2A is regulated by the small t antigen of SV40 and polyomavirus, and is involved in targeting of nuclear transcription factors, e.g. HAND1 and HAND2, overview
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-
?
additional information
?
-
-
the holoenzyme plays a role in organelle assembly and is essential for maturation of the centrosome and regulation of chromatin activities, it is involved in spliceosomal assembly via interaction with the survival of motor neuron complexes, PP4 regulates several cellular signalling routes, including the NF-kappaB and the target of rapamycin pathways, PP4 plays a role in DNA damage response and decrease histone deacetylase activity, phylogenetic tree and PPP phosphome, overview
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-
?
additional information
?
-
-
the Pro33 isoform of integrin beta3 enhances outside-in signaling in platelets by regulating the activation of serine/threonine phosphatases
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-
?
additional information
?
-
-
PP2A does not modify the activity of no receptor potential A-protein
-
-
?
additional information
?
-
-
PP2Ac associates with the integrin alphaIIbbeta3 complex in platelets, the alphaIIb membrane proximal region containing the KVGFFKR sequence can support the direct interaction of PP2Ac
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-
?
additional information
?
-
PP5 binds the A-subunit of the PP2A holoenzyme, which functions to tether the catalytic (PP2Ac) and substrate targeting B-subunits of PP2A
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-
?
additional information
?
-
-
PP5 binds the A-subunit of the PP2A holoenzyme, which functions to tether the catalytic (PP2Ac) and substrate targeting B-subunits of PP2A
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-
?
additional information
?
-
PP5 is a potentially important regulator of both hormone- and stress-induced signaling networks that enable a cell to respond appropriately to genomic stress
-
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?
additional information
?
-
-
PP5 is a potentially important regulator of both hormone- and stress-induced signaling networks that enable a cell to respond appropriately to genomic stress
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-
?
additional information
?
-
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physical and functional interaction of the phosphatase calcineurin with a group of modulators, the RCAN protein family, e.g. proteins Cabin1 and AKAP79, a valine-rich region within the RCAN carboxyl region is essential for binding to the docking site in calcineurin, overview. Competition by substrates and modulators for a common docking site appears to be an essential mechanism in the regulation of Ca2+-calcineurin signaling
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-
?
additional information
?
-
-
regulation of cellular PP1 by phosphorylation of the CPI-17 family, C-kinase-activated PP1 inhibitors, overview
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-
?
additional information
?
-
-
the enzyme is cleaved by caspase-3, PP1 inhibitor Inh3 harbors 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
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?
additional information
?
-
the PP2A/Balpha trimeric enzyme interacts with a domain encompassing the microtubule-binding repeats and upstream proline-rich region of the longest adult tau 2N/4R-Tau isoform containing 2 N-terminal inserts (2N) and four microtubule-binding repeats. PP2A is reported to be the only phosphatase mediating dephosphorylation of the neuronal phosphorylated betaIII tubulin isoform, which inhibits MAP2-stimulated microtubule assembly
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-
?
additional information
?
-
the PP2A/Balpha trimeric enzyme interacts with a domain encompassing the microtubule-binding repeats and upstream proline-rich region of the longest adult tau 2N/4R-Tau isoform containing 2 N-terminal inserts (2N) and four microtubule-binding repeats. PP2A is reported to be the only phosphatase mediating dephosphorylation of the neuronal phosphorylated betaIII tubulin isoform, which inhibits MAP2-stimulated microtubule assembly
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-
?
additional information
?
-
the PP2A/Balpha trimeric enzyme interacts with a domain encompassing the microtubule-binding repeats and upstream proline-rich region of the longest adult tau 2N/4R-Tau isoform containing 2 N-terminal inserts (2N) and four microtubule-binding repeats. PP2A is reported to be the only phosphatase mediating dephosphorylation of the neuronal phosphorylated betaIII tubulin isoform, which inhibits MAP2-stimulated microtubule assembly
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?
additional information
?
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-
the enzyme is involved in regulation of diverse cellular processes and signaling pathways including circadian rhythm and apoptosis, overview
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-
?
additional information
?
-
-
the enzyme is involved in regulation of diverse cellular processes and signaling pathways including embryonic development, cell proliferation, cell death, and cancer, overview, PP5 is involved in stress response negatively regulating ASK-1 dependent apoptosis and promoting tumor growth
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?
additional information
?
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the expression of wild type PP2A catalytic subunit suppresses the MAPK kinase 3 phosphorylation
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?
additional information
?
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calcineurin is a Ca2+/calmodulin-dependent protein phosphatase
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?
additional information
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the enzyme is involved in regulation of diverse cellular processes and signaling pathways including circadian rhythm, moluating the circadian transcription factor FRQ, and apoptosis, overview
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-
?
additional information
?
-
in vivo expression and response pattern of PP2A gene to environmental stress
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additional information
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in vivo expression and response pattern of PP2A gene to environmental stress
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?
additional information
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in vivo expression and response pattern of PP2A gene to environmental stress
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?
additional information
?
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in vivo expression and response pattern of PP2A gene to environmental stress
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?
additional information
?
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the enzyme is involved in bacterial swarming activity and biofilm formation, PA3346 is the only of seven orphan response regulators inthe organism that is trans-phosphorylated by HptB
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?
additional information
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ceramide-induced cell survival mechanism, overview
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additional information
?
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PP2A is involved in central sensitization, PP2A negatively regulates the phosphorylation of N-methyl-D-aspartate, NMDA, receptors in response to capsaicin induction in the spinal cord
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?
additional information
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PP2A modulates Akt activity, role of PP2A holoenzyme and subunits in MAPK signaling pathways, overview
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?
additional information
?
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PP5 acts as an effector in Rac GTPase signalling via interaction of its N-terminal TPR domain with Rac-GTP, PP5 inhibition results in blockage of KCNH2 channel stimulation by thyroid hormone and by Rac in pituitary cells, overview
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?
additional information
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PP2A is a multifunctional enzyme, direct interaction with the adenovirus E4orf4 protein via the regulatory subunit initiation virus-induced growth arrest in yeast cells, signal transduction is mediated by Cdc55 interacting with both PP2A catalytic subunit in absence of the Tpd3 subunit and E4orf4, mechanism involving the Tpd3 yeast subunit, overview
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?
additional information
?
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the holoenzyme plays a role in organelle assembly and is essential for maturation of the centrosome, PP4 homologues participate in the nutrient sensing pathway, pathway modeling overview, and confers resistance to the anticancer DNA-binding agents cisplatin and oxaliplatin, phylogenetic tree and PPP phosphome, overview
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?
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1,3-bis(4-amino-2-methylquinolin-6-yl)urea
-
1-(3-bromophenyl)-6-undecyl-1,3,5-triazinane-2,4-diimine
-
1-[(ethylcarbamoyl)amino]-1-oxopropan-2-yl (3E)-3-(3,4-dimethoxybenzylidene)-2,3-dihydro-1H-cyclopenta[b]quinoline-9-carboxylate
-
-
2-amino-4-methyl-N-naphthalen-2-ylpentanamide
-
2-mercaptoethanol
-
phosphatase activity is decreased by 5 mM
3-hydroxy-3-methylglutaryl CoA
3-iodo-7-[(8-iodo-10-phenyl-5,10-dihydrophenazin-2-yl)amino]-5-phenylphenazin-5-ium
-
4,4'-dipyridyl disulfide
-
-
4-nitrophenyl phosphate
-
10 mM, 89% inhibition
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
-
5,5'-dithiobis(2-nitrobenzoic acid)
5,5'-methylene disalicylic acid
13% inhibition at 0.1 mM
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
A23187
-
reduces the Ca2+ level and thereby inhibits Ca2+-dependent calcineurin
alpha 4 protein
-
rapamycin has no effect on PP2A-C association with the inhibitor alpha 4 protein
-
Aurin tricarboxylic acid
48% inhibition at 0.1 mM
bovine serum albumin
-
1 mg/ml 30°C, pH 7.5, 95% remaining activity with glycogen synthase D and 92% with phosphorylase, in presence of 10 mg/ml 79% remaining activity with phosphorylase a as substrate
-
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
-
CaCl2
-
14 mM, 30°C, pH 7.5, with phosphorylase a as substrate, 50% remaining activity
caffeic acid phenethyl ester
-
down-regulation of expression of PP2A catalytic subunit in cells treated with caffeic acid phenethyl ester at 48 h
cAMP
-
1 mM, 30°C, pH 7.5, 83% remaining activity with histone as substrate and 83% with phosphorylase a
cantheridin
-
strong inhibition at 0.005 mM
caspase-3-inhibitor
-
0.1 mM completely inhibits activity
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
-
Cr2+
Lambdavirus lambda
-
-
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
-
cyclosporin A-cyclophilin complex
-
-
-
D-glucose 6-phosphate
-
-
deltamethrin
-
a calcineurin inhibitor
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
-
dithiothreitol
-
phosphatase activity is decreased by 5 mM
docetaxel
-
docetaxel induces the decrease in the activity of protein phosphatase 1
Drosophila melanogaster protein phosphatase inhibitor-2
-
IC50: 0.5-1 nM
-
Fe3+
-
1 mM: 2% of enzyme activity
FK506-FK506-binding protein
-
-
-
FR225659
-
synthesizes by Helicomyces sp. strain 19353, inhibits PP1 and PP2A, inhibition of gluconeogenese in vivo in hepatocytes
FR253761
-
synthetic derivative of FR225659, inhibits PP1 and PP2A, inhibition of gluconeogenese in vivo in hepatocytes
FR259383
-
synthetic derivative of FR225659, inhibits PP1 and PP2A, inhibition of gluconeogenese in vivo in hepatocytes
gelatin
-
1 mg/ml, 30°C, pH 7.5, 92% remaining activity with histone as substrate, and 31% withe phosphorylase a, in presence of 10 mg/ml 10% remaining activity with phohsphorylase a
-
ginsenoside Rg1
from Panax ginseng roots, Rg1 alleviates left ventricular hypertrophy induced by abdominal aorta coarctation, and the protection appears to be due, at least in part, to its inhibitory effects on calcineurin and MAP kinase signaling pathways, overview
glutathione disulfide
-
-
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
guanosine 5'-(beta,gamma-imido)triphosphate
-
-
Hg2+
Lambdavirus lambda
-
-
histone
-
competitive when glycogen synthase D is the substrate, increases the Km-value for glycogen synthase D 4fold, but shows mixed type inhibition when phosphorylase a acts as substrate with an 1.4fold increase of Km
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
-
I-2
inhibitor-2, an inhibitory regulator from rabbit skeletal muscle. I-2 is a much less potent inhibitor against PPZ1FL, which includes the about 160-amino-acid N-terminal IDP domain, as compared to the catalytic domain. The N-terminal domain likely masks one or more binding sites for I-2 but not the active site, as the PPZ1FL protein is fully susceptible to microcystin-LR inhibition and prevents PPZ1 inhibition by this protein inhibitor
I-2 protein
-
PP1-specific inhibitor
-
Inhibitor protein
-
MW 33000-36000, heat and acid stable, specific for BCKDH phosphatase
-
Inhibitor-1
-
inhibitor of isozyme PP1
-
mesalazine
-
1 mg/ml efficiently inhibits PP2A
MgCl2
-
14 mM, 30°C, pH 7.5, with phosphorylase a as substrate, 60% remaining activity
MnCl2
-
14 mM, 30°C, pH 7.5, with phosphorylase a as substrate, 51% remaining activity
molybdate
-
1 mM, 70% inhibition
myosin light chain hydroxy peptide
-
competitive inhibition
-
N-methyl-N'-phenanthren-9-ylimidodicarbonimidic diamide
-
Na2HPO4
-
14 mM, 30°C, pH 7.5, no activity with glycogen synthase D as substrate, remaining activity 79% with histone as substrate, and 64% with phosphorylase a as substrate
Na2P2O7
-
14 mM, 30°C, pH 7.5, remaining activity 6% with glycogen synthase D as substrate, 15% with histone as substrate, and 8% with phosphorylase a as substrate
Na2SO4
-
14 mM, 30°C, pH 7.5, remaining activity 53% with glycogen synthase D as substrate and 32% with phosphorylase a as substrate
NaCl
-
14 mM, 30°C, pH 7.5, with phosphorylase a as substrate, 83% remaining activity
NaHCO3
-
14 mM, 30°C, pH 7.5, remaining activity 49% with glycogen synthase D as substrate, 79% with histone as substrate, and 64% with phosphorylase a as substrate
NaNO3
-
14 mM, 30°C, pH 7.5, remaining activity 70% with glycogen synthase D as substrate, 83% with histone as substrate, and 78% with phosphorylase a as substrate
neurabin-I
-
IC50 for the wild-type catalytic subunit PP1alpha is 1.75 nM
-
nuclear inhibitor of protein phosphatase 1
-
-
-
Nucleoside mono-, di-, and triphosphates
-
orthovanadate
-
specific inhibition of activity for the ENDpYINASL substrate by 0.01 mM
p-bromotetramisole
-
PTP-1B
p-chloromercuribenzoate
-
-
paclitaxel
-
paclitaxel induces decrease in activity of protein phosphatase 2 subgroups
Pd2+
Lambdavirus lambda
-
-
Phenylarsine oxide
-
potent dithiothreitol-reversible inhibition of PP2A
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
phosphorylase a
-
mixed type inhibitor with glycogen synthase d as substrate, increases Km 2fold with only small decearse in vmax
polylysine
-
inhibition with substrate myelin basic protein, activation with substrate p-nitrophenyl phosphate
protamine
-
inhibition of phosphatase PP3
protein phosphatase inhibitor II
-
Protein phosphatase inhibitor-1
-
protein phosphatase inhibitor-2
-
protein phosphatase-1 inhibitor-1
-
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
-
rabbit liver glycogen
-
1 mg/ml 30°C, pH 7.5, 88% remaining activity with glycogen synthase D and 37% remaining activity with 10 mg/ml inhibitor
-
RCAN proteins
-
RCAN inhibition of CN phosphatase activity is mediated by the extreme C-terminal region
-
Rcn1
-
inhibits calcineurin signaling when expressed at high levels
-
regucalcin
-
has regulatory function in heart cytosol; the protein inhibits the enzyme in presence of EGTA or ethylene glycol and has a regulatory function for the enzyme independently of Ca2+
-
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
Sc3+
Lambdavirus lambda
-
-
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 orthovanadate
-
1 mM completely inhibits activity
sodium potassium tartrate
-
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
-
Tartrate
-
moderate inhibition of P11 at 2 mM; strong inhibition
tetramisole
-
strong inhibition at 2 mM
trifluoperazin
-
cocmplete inhibition at 0.001-0.002 mM
Trifluoperazine
inhibition of phosphatase PfPP2B
Trifluorperazine
-
moderate inhibition; strong inhibition; strong inhibition at 0.1 mM
tris(2-carboxyethyl)-phosphine hydrochloride
-
phosphatase activity is decreased by 5 mM
UDP
-
1.4 mM, 30°C, pH 7.5, 52% remaining activity with glycogen synthase D as substrate and 20% with phosphorylase a
UMP
-
1.4 mM, 30°C, pH 7.5, 58% remaining activity with glycogen synthase D as substrate and 16% with phosphorylase a
UTP
-
1.4 mM, 30°C, pH 7.5, 44% remaining activity with glycogen synthase D as substrate and 21% with phosphorylase a
V3+
Lambdavirus lambda
-
-
Yb3+
Lambdavirus lambda
-
-
ZnSO4
-
1 mM, 91% inhibition
3-hydroxy-3-methylglutaryl CoA
-
-
3-hydroxy-3-methylglutaryl CoA
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
ADP
-
1.4 mM, 30°C, pH 7.5, 55% remaining activity with glycogen synthase D as substrate and 12% with phosphorylase a
AMP
-
1.4 mM, 30°C, pH 7.5, 55% remaining activity with glycogen synthase D as substrate and 10% with phosphorylase a
AMP
Lambdavirus lambda
-
-
ATP
-
-
ATP
-
1.4 mM, 30°C, pH 7.5, 47% remaining activity with glycogen synthase D as substrate and 15% with phosphorylase a
ATP
-
phosphatases SMP-I and SMP-II
Ca2+
-
degree of inhibition depends on concentration of Mg2+
Ca2+
-
high concentrations
calyculin
-
IC50: 0.09 nM
calyculin
-
moderate inhibition at 0.00001 mM
calyculin A
-
calyculin A
-
inhibits isozymes PP1, PP4, PP5, and PP2A
calyculin A
-
inhibitor of isozymes PP1 and PP2A
calyculin A
-
inhibits PP1, PP4, PP5, and PP2A
cantharidin
-
IC50: 60 nM
cantharidin
-
antitumor agent from the chinese blister beetle, strong inhibition of PP4
cantharidin
-
IC50: 0.13 mM
citrate
-
1.4 mM, 30°C, pH 7.5, 68% remaining activity with glycogen synthase D as substrate
Co2+
-
-
Co2+
Lambdavirus lambda
-
-
Co2+
-
Mn2+-stimulated form
Co2+
-
1 mM: 8% of enzyme activity
Cu2+
Lambdavirus lambda
-
-
cyclin-dependent kinase 2
-
-
-
cyclin-dependent kinase 2
-
-
-
cyclosporin
-
PP-2B
cyclosporin
-
a calcineurin inhibitor, CNI, with potent impact on the success of organ transplantation. The compound is nephrotoxic and can cause renal dysfunction, which is an independent risk factor for graft loss and mortality after kidney transplantation, mechanisms and involved factors, detailed overview
cyclosporin A
-
cyclosporin A
-
in vivo inhibition in cell culture, 40% inhibition at 0.002 mM in vitro
cyclosporin A
-
specific inhibitor of calcineurin
cyclosporin A
-
a specific pharmacological inhibitor of calcineurin. Cyclosporin A modulates cell shape and actin organization of melanoma cells
cyclosporin A
-
the calcineurin inhibitor can block T-cell activation and is used as immunosuppressiv drug to prevent graft-versus-host reactions and autoimmune diseases
cyclosporin A
-
an immunosuppressive drug. 25% inhibition in keratinocytes at 831 nM, 49% in melanocytes
cyclosporin A
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
cyclosporin A
-
a specific calcineurin inhibitor, time course of inhibition in vivo, overview
cyclosporin A
inhibition of phosphatase PfPP2B
cyclosporin A
-
specific inhibitor of calcineurin
diethyldicarbonate
0.5%. No inhibition at 0.05% and 0.1%
diphosphate
-
IC50: 0.07 mM
diphosphate
-
10 mM, complete inhibition
diphosphate
-
10 mM, 93% inhibition
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
-
DSCR1
-
a calcineurin inhibitor, encoded by gene Dscr1 on chromosome 21, is elevated in Down syndrome model mice
-
EDTA
-
14 mM, 30°C, pH 7.5, 23% remaining activity with glycogen synthase D as substrate and 35% with phosphorylase a
EDTA
62% inhibition at 2 mM
EDTA
-
isozyme PP1 has low activity after depletion of Mn2+ with EDTA
EDTA
Lambdavirus lambda
-
-
EDTA
-
type PP2C phosphatase
EDTA
-
0.1 mM, complete inactivation
EDTA
-
10 mM, 93% inhibition
EDTA
-
0.1 mM decreases specific and total activities by about 40%
EGTA
-
14 mM, 30°C, pH 7.5, 55% remaining activity with glycogen synthase D as substrate and 83% with phosphorylase a
EGTA
-
reduces the Ca2+ level and thereby inhibits Ca2+-dependent calcineurin
EGTA
-
moderate inhibition
endothall
-
specific inhibitor of isozyme PP2A
endothall
-
specific inhibitor of isozyme PP2A
endothall
-
IC50: 0.21 mM
F-
-
-
F-
Lambdavirus lambda
-
-
Fe2+
Lambdavirus lambda
-
-
Fe2+
-
Mn2+-stimulated form
Fe2+
-
1 mM: 7% of enzyme activity
FK506
-
FK506
-
selective PPP3 inhibitor
FK506
-
the calcineurin inhibitor can block T-cell activation and is used as immunosuppressive drug to prevent graft-versus-host reactions and autoimmune diseases
FK506
-
a specific calcineurin inhibitor, time course of inhibition in vivo, overview
FK506
-
a calcineurin inhibitor
fostriecin
-
IC50: 0.022 mM
fostriecin
-
inhibits isozymes PP2A and PP4
fostriecin
-
antitumor agent from Streptomyces pulveraceus ssp. fostreus, strong inhibition of PP4
fostriecin
-
more selective inhibitor of PP2A
fostriecin
-
inhibits PP2A and PP4
fostriecin
-
potent specific inhibition of PP2A
fostriecin
inhibits at 400-1000 nM
fostriecin
-
inhibits PP2A at 3.2 nM
glutamate
-
inhibitor of isozyme PP2A
glutamate
-
inhibitor of isozyme PP2A
Inhibitor-2
-
-
-
Inhibitor-2
-
inhibitor of isozyme PP1
-
Inhibitor-2
inhibits at 100-500 nM
-
Inhibitor-2
-
marginally inhibited by 200 nM
-
microcystin
-
-
microcystin
-
inhibits isozymes PP1, PP4, PP5, and PP2A
-
microcystin
-
inhibits PP1, PP4, PP5, and PP2A
-
microcystin
-
potent inhibitor
-
microcystin
-
inhibits by binding tightly to the phosphatase catalytic domain of PP5
-
microcystin-LR
-
IC50: 0.01 nM
microcystin-LR
-
inhibition of phosphatase PP3
microcystin-LR
i.e. MC, the marine toxin microcystin-LR is a potent cyclic peptide inhibitor of PP1, it binds the active site of PPZ1cat, binding structure analysis, overview. The bulk of the MC binds the PPZ1cat hydrophobic binding pocket, while the remainder covers and, as a consequence, blocks the active site
microcystin-LR
-
specific PP2A inhibitor
microcystin-LR
-
inhibitor of isozymes PP1 and PP2A
NaF
-
IC50: 2.1 mM
NaF
-
14 mM, 30°C, pH 7.5, remaining activity 31% with glycogen synthase D as substrate, 67% with histone as substrate, and 37% with phosphorylase a as substrate
NaF
-
specific inhibition of activity for the RRApTVA substrate by 50 mM
NaF
-
50 mM, 47% inhibition
NaF
-
moderate inhibition; strong inhibition
NaF
-
type PP2C phosphatase
NaF
-
50 mM, 78% inhibition
NaF
-
specific inhibition of activity for the RRApTVA substrate by 50 mM
Ni2+
-
-
Ni2+
-
1 mM: 4% of enzyme activity
nodularin
-
IC50: 0.04 nM
nodularin
-
inhibits isozymes PP2A, PP5, and PP4
nodularin
-
inhibits PP2A, PP5, and PP4
nodularin
-
IC50: 0.0005 mM
Nucleoside mono-, di-, and triphosphates
-
e.g. GTP, GDP, ATP, ADP
-
Nucleoside mono-, di-, and triphosphates
-
e.g. GTP, GDP, ATP, ADP
-
Nucleoside mono-, di-, and triphosphates
-
e.g. GTP, GDP, ATP, ADP
-
Nucleoside mono-, di-, and triphosphates
-
e.g. GTP, GDP, ATP, ADP
-
okadaic acid
-
IC50: 20 nM
okadaic acid
-
inhibition of phosphatase PP3
okadaic acid
-
no inhibition of phosphatase PP2C
okadaic acid
-
IC50: 40 nM
okadaic acid
12% inhibition at 0.001 mM
okadaic acid
-
no inhibition of phosphatase PP2Calpha
okadaic acid
-
no inhibition of phosphatase PP7
okadaic acid
-
IC50: 0.66 nM
okadaic acid
-
inhibits isozymes PP1, PP4, PP5, and PP2A
okadaic acid
-
IC50 for the wild-type catalytic subunit PP1alpha is 157 nM
okadaic acid
-
PP2A inhibition induces the dissociation of IQGAP1 from the E-cadheri-catenins complex
okadaic acid
-
unspecific protein phosphatase inhibitor
okadaic acid
-
specific inhibitor of PP2A
okadaic acid
-
50-100 nM efficiently inhibits PP2A
okadaic acid
-
inhibition at 100 nM
okadaic acid
-
inhibitor of isozyme PP2A
okadaic acid
-
inhibitor of isozymes PP1 and PP2A
okadaic acid
-
a polyether derivative of a C38 fatty acid produced by toxigenic dinoflagellates, Dynophysis and Prorocentrum, strong inhibition by okadaic acid and derivatives
okadaic acid
-
specific inhibitor of PP2A
okadaic acid
PP2A activity is also regulated by many cellular regulators and natural inhibitors, such as okadaic acid. The commonly used inhibitor not only inhibits all PP2A isoforms, but also other Ser/Thr phosphatases, including PP1 and other PPP family members, at the concentrations needed to completely abrogate cellular PP2A activity; the commonly used inhibitor not only inhibit Ser/Thr phosphatases, including PP1 and other PPP family members, but also all PP2A isoforms
okadaic acid
-
inhibits PP1, PP4, PP5, and PP2A
okadaic acid
no inhibition
okadaic acid
-
IC50: 4 nM
okadaic acid
-
type PP2C phosphatase is not inhibited
okadaic acid
-
0.00125 mM. 50% inhibition
okadaic acid
inhibition is greater at 40°C than at 90°C
okadaic acid
-
inhibition of heterotrimeric phosphatase 2A catalyzing the dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase
okadaic acid
-
two enzyme forms in parotid gland, one is sensitive, the other not inhibited
okadaic acid
inhibition of wild-type PP5, no inhibition of PP5 mutant 451A
okadaic acid
-
inhibits PP2A at 100 nM
okadaic acid
-
91% inhibition of the total phosphatase activity
okadaic acid
-
inhibitory at 10 nM
okadaic acid
-
inhibitor of isozyme PP2A
okadaic acid
-
PP2A activity is dose-dependently decreased with okadaic acid with 15% inhibition at 0.05 nM, 55% inhibition at 0.5 nM, and 69% inhibition at 5 nM
okadaic acid
-
complete inhibition at 250 nM
okadaic acid
-
IC50: 0.0002 mM
okadaic acid
IC50: 0.0081 mM
okadaic acid
-
complete inhibition at 50 nM
okadaic acid
56% activity in presence of 10 nM okadaic acid
okadaic acid
-
inhibition at 1 nM
okadaic acid
-
inhibits PP2A at 10 nM
okadaic acid
-
IC50: 0.18 nM; IC50: 0.1 nM
okadaic acid
-
IC50: 0.03 nM
phosphate
-
-
phosphate
-
competitive inhibition to C-subunit and AC-dimer, noncompetitive inhibition to AC-R2
phosphate
-
50 mM, complete inhibition
phosphate
Lambdavirus lambda
-
-
phosphate
-
10 mM, 76% inhibition
phosphoenolpyruvate
Lambdavirus lambda
-
-
phosphonothioic acid
-
pimecrolimus
-
a topical calcineurin inhibitor, treatement might bear high risk for skin cancer and lymphoma, overview
pimecrolimus
-
an immunosuppressive drug
protein phosphatase inhibitor II
-
specific inhibitor of isozyme PP1
-
protein phosphatase inhibitor II
-
specific inhibitor of isozyme PP1
-
Protein phosphatase inhibitor-1
-
-
-
Protein phosphatase inhibitor-1
-
inhibits isozyme PP1
-
Protein phosphatase inhibitor-1
-
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
-
Protein phosphatase inhibitor-1
-
PPI-1, the effect of activated inhibitor-1 on regulation of protein phosphorylation is critical in the stimulatory effects of beta-agonists in the heart. The mutant G147D inhibitor-1 decreases PLN phosphorylation in response to beta-adrenergic activation. The G147D polymorphism in PPI-1 occurs exclusively in Afro-American populations, quantitation of the expressional levels of wild-type inhibitor-1 and G147D inhibitor-1, also in white subjects. Overexpression of inhibitor-1 or its variant does not alter the levels of the major regulatory proteins related to cardiac calcium homeostasis
-
Protein phosphatase inhibitor-1
-
inhibits PP1
-
protein phosphatase inhibitor-2
-
IC50: 0.65 nM
-
protein phosphatase inhibitor-2
-
-
-
protein phosphatase inhibitor-2
-
inhibits isozyme PP1
-
protein phosphatase inhibitor-2
-
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
-
protein phosphatase inhibitor-2
-
inhibits PP1
-
protein phosphatase inhibitor-2
-
i.e. I-2, specific for PP1
-
protein phosphatase-1 inhibitor-1
-
plays a role in cardiac physiology and pathophysiology, overview
-
protein phosphatase-1 inhibitor-1
-
plays a role in cardiac physiology and pathophysiology, overview
-
protein phosphatase-1 inhibitor-1
-
the inhibitor-1 contains an RVXF motif sequence, which facilitates its interaction with PP1. On stimulation of the beta-adrenergic axis, protein kinase A phosphorylates Thr35 in inhibitor-1, resulting in PP1 inhibition and amplification of the contractile response
-
protein phosphatase-1 inhibitor-1
-
plays a role in cardiac physiology and pathophysiology, overview
-
protein phosphatase-1 inhibitor-1
-
plays a role in cardiac physiology and pathophysiology, overview
-
sanguinarine
-
Sodium fluoride
30% inhibition at 100 mM, 18% at 10 mM
Sodium phosphate
87% inhibition at 5 mM, 96% at 10 mM
Sodium vanadate
-
-
Sodium vanadate
a PTP inhibitor targeting the catalytic site pocket. Vanadate is anchored in the active site of Tk-PTP(form II), stabilized by electrostatic interaction with the guanidinium group of Arg109 and by its oxygen atom-mediated hydrogen bonds with the main chain amides of Met94, Gly95, Leu97, Gly98, and Arg99. The Tk-PTP(form II) P-loop is structurally similar to those of catalytically active DUSP proteins
tacrolimus
-
a topical calcineurin inhibitor, treatment might bear high risk for skin cancer and lymphoma, overview
tacrolimus
-
an immunosuppressive drug. 89% inhibition in keratinocytes at 124 nM, 74% in fibroblasts, and 75% in melanocytes
tacrolimus
-
27-30% inhibition at 5 ng/ml, females and males
tacrolimus
-
a calcineurin inhibitor, CN, with potent impact on the success of organ transplantation. The compound is nephrotoxic and can cause renal dysfunction, which is an independent risk factor for graft loss and mortality after kidney transplantation, mechanisms and involved factors, detailed overview
tacrolimus
i.e. FK506; i.e. FK506
tacrolimus
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
tautomycin
-
IC50: 0.06 nM
tautomycin
tautomycin preferentially binds PP1 over PP2A
tautomycin
-
inhibitor of isozymes PP1 and PP2A
tautomycin
-
inhibits PP1 at 1 nM and PP2A at 10 nM
tungstate
Lambdavirus lambda
-
-
vanadate
-
1 mM, complete inhibition
vanadate
-
at 1 mM inhibition to 60% of its activity
vanadate
Lambdavirus lambda
-
-
Zn2+
-
-
Zn2+
-
5 mM, complete inhibition
Zn2+
Lambdavirus lambda
-
-
Zn2+
strong inhibition, the inhibition of PrpC activity by Zn2+ ions may be attributed to the destabilization of the native fold of the protein
Zn2+
-
Mn2+-stimulated form
Zn2+
-
1 mM: 0% of enzyme activity
additional information
about 2.4fold reduced expression in Arabidopsis thaliana mutants etr1 with altered gene expression of the ethylene signal transduction pathway; about 3fold reduced expression in Arabidopsis thaliana mutant aba2 with a mutation at the start of exon 2
-
additional information
about 2.4fold reduced expression in Arabidopsis thaliana mutants etr1 with altered gene expression of the ethylene signal transduction pathway; about 3fold reduced expression in Arabidopsis thaliana mutant aba2 with a mutation at the start of exon 2
-
additional information
-
about 2.4fold reduced expression in Arabidopsis thaliana mutants etr1 with altered gene expression of the ethylene signal transduction pathway; about 3fold reduced expression in Arabidopsis thaliana mutant aba2 with a mutation at the start of exon 2
-
additional information
-
study of effects of D-glucose 6-phosphate on inhibitory compounds; study of effects of MgCl2 in presence of AMP, ADP, ATP, UMP, UDP, UTP, or citrate
-
additional information
the residues at 407-456 also have an inhibitory effect on CaN A phosphatase activity in addition to the previously known autoinhibitory domain at 457-480
-
additional information
-
the residues at 407-456 also have an inhibitory effect on CaN A phosphatase activity in addition to the previously known autoinhibitory domain at 457-480
-
additional information
-
SCPL-1 is not inhibited by the typical phosphatase inhibitors NaF, BeCl2, AlCl3, and Na3VO4
-
additional information
no inhibition by sanguinarine chloride at 0.05 mM. Poor inhibition by orthovanadate at 0.005-0.05 mM
-
additional information
-
no inhibition by sanguinarine chloride at 0.05 mM. Poor inhibition by orthovanadate at 0.005-0.05 mM
-
additional information
-
activity is unaffected by other potential inhibitors or activators such as polyamines, heparin, cyclic nucleotides, Ca2+/calmodulin, tartrate, tetramisole, okadaic acid, microcystin LR, or sulfhydryl-modifying agents
-
additional information
-
no inhibition by okadaic acid
-
additional information
-
isozyme PP5 contains an extended N-terminal domain with three tetratricopeptide repeat, TPR, motifs which possesses autoinhibitory function and are important for interaction with other proteins
-
additional information
-
Ppp5 is inhibited by an autoinhitory conformation formed by the N-terminal TPR domain and a C-terminal subdomain, structure and mechanism overview
-
additional information
-
IC50 of inhibitors for mutant PP1alpha catalytic subunits, overview
-
additional information
-
phosphoserine-containing diphosphorylated peptides with the sequence pSXpY inhibit Wip1 phosphatase activity; PP2A and PP2Calpha are not significantly inhibited by the cyclic phosphopeptides c(MpSIpYVA) and c(M-L-2-amino-4-phosphono-4,4-difluorobutanoate-IpYVA)
-
additional information
the recombinant Trx-His-tagged enzyme is not affected by 0.001 mM okadaic acid
-
additional information
-
the recombinant Trx-His-tagged enzyme is not affected by 0.001 mM okadaic acid
-
additional information
-
not inhibited by tautomycin or cyclosporin
-
additional information
-
20 and 40 nM PPP3CA siRNA decreases PPP3CA protein levels by about 97% but not PPP2CA potein expression, knockdown of PPP3CA protein expression enhances vascular endothelial growth factor-beta, but not fibroblast growth factor 2-stimulated cell proliferation, knockdown of PPP3CA protein expression does not significantly affect vascular endothelial growth factor-induced mitogen-activated protein kinase 3/1 and phosphoinositide 3-kinase/v-akt murine thymoma viral oncogen homolog 1 phosphorylation, while attenuates fibroblast growth factor 2-induced mitogen-activated protein kinase 3/1 and phosphoinositide 3-kinase/v-akt murine thymoma viral oncogen homolog 1 phosphorylation
-
additional information
-
protein phosphatase inhibitor II and cyclosporin A have no inhibitory effect on isozyme PP2A
-
additional information
-
protein phosphatase 2B is highly resistant to inhibition by okadaic acid
-
additional information
-
fibrinogen binding to alphaIIbbeta3 during platelet adhesion decreases integrin-associated PP2A activity
-
additional information
-
PP5 protein expression is more than 90% inhibited by PP5 siRNA transfection
-
additional information
-
isozyme PP2 is insensitive to inhibitor-1 and inhibitor-2
-
additional information
-
the hypothetic mechanisms of carcinogenesis include a direct effect of calcineurin inhibitors on keratinocytes, because topical calcineurin inhibits DNA repair and reduces apoptosis in epidermal keratinocytes
-
additional information
-
phosphorylation by cyclin-dependent kinases lower PP1 activity in vitro and vivo
-
additional information
-
regulation of cellular PP1 by phosphorylation of the CPI-17 family, C-kinase-activated PP1 inhibitors. Mechanisms underlying PP1 inhibition and the kinase/PP1 cross-talk mediated by CPI-17 and its related proteins, PHI, KEPI, and GBPI, overview
-
additional information
-
knockout of Ste20-like kinase, Mst2, reduces the expression of the catalytic subunit of PP2A, RNAi silencing of Mst2 triggers a striking proteasome-dependent decrease in the levels of the catalytic subunit of PP2A. Treatment with the specific proteasome inhibitor lactacystin completely reverses the loss of HEI-193 cell PP2A-C incurred upon Mst2 RNAi. Mst2-dependent stabilization of PP2A-C is a posttranslational process likely involving a reduction in proteasome-dependent PP2A-C degradation
-
additional information
-
calcineurin inhibition in fibroblasts and keratinocytes may be of influence on the overall functioning of the skin immune system. No inhibition of calcineurin by okadaic acid
-
additional information
-
calcineurin inhibitor treatment optimization in patients treated with mixed immunosuppressive protocols, overview
-
additional information
toxins that bind and block the PP1 active site are lethal, thus, potential drugs that target PP1 must interact outside the PP1 active site. The REG1:PP1 holoenzyme (REG1 represents a PP1 regulatory protein that contains an RVxF-PhiPhi-Arg motif, such as PNUTS) is preferentially populated compared to the REG2:PP1 holoenzyme (REG2 is a PP1 regulatory protein with only an RVxF motif), because the affinity of REG1 for PP1 is much higher than REG2 for PP1. A drug that targets only the PhiPhi-Arg binding grooves will selectively displace the motifs in REG1 that bind at these sites, thereby reducing the affinity of REG1 for PP1 and, consequently, increase the likelihood of forming REG2:PP1 holoenzymes. In this way, dephosphorylation of REG1:PP1 substrates will decrease while REG2:PP1 holoenzymes will increase
-
additional information
toxins that bind and block the PP1 active site are lethal, thus, potential drugs that target PP1 must interact outside the PP1 active site. The REG1:PP1 holoenzyme (REG1 represents a PP1 regulatory protein that contains an RVxF-PhiPhi-Arg motif, such as PNUTS) is preferentially populated compared to the REG2:PP1 holoenzyme (REG2 is a PP1 regulatory protein with only an RVxF motif), because the affinity of REG1 for PP1 is much higher than REG2 for PP1. A drug that targets only the PhiPhi-Arg binding grooves will selectively displace the motifs in REG1 that bind at these sites, thereby reducing the affinity of REG1 for PP1 and, consequently, increase the likelihood of forming REG2:PP1 holoenzymes. In this way, dephosphorylation of REG1:PP1 substrates will decrease while REG2:PP1 holoenzymes will increase
-
additional information
phosphorylation of PTPN12 at Ser19 changes its substrate interface, and by doing so, selectively decreases its activity toward the human epidermal growth factor receptor 2 (HER2)-pY1196 site, but not other HER2 phosphorylation sites or other known PTPN12 substrates, such as SRC, paxillin, PAK1,VAV2, p130Cas, FAK, and p190RhoGAP
-
additional information
calcineurin shows low sensitivity to inhibitory toxins such as okadaic acid and microcystin-LR, due to a divergent amino acid sequence in the beta12-beta33 loop of phosphatase PP1c
-
additional information
calcineurin shows low sensitivity to inhibitory toxins such as okadaic acid and microcystin-LR, due to a divergent amino acid sequence in the beta12-beta33 loop of phosphatase PP1c
-
additional information
calcineurin shows low sensitivity to inhibitory toxins such as okadaic acid and microcystin-LR, due to a divergent amino acid sequence in the beta12-beta33 loop of phosphatase PP1c
-
additional information
Lambdavirus lambda
-
not inhibitory are okadaic acid, phosphoserine, phosphothreonine, phoshotyrosine
-
additional information
-
insensitive to inhibitor-2
-
additional information
-
DNA damage 34, i.e. gADD34, and growth arrest disturb the binding of PP1 to p53
-
additional information
-
Par-3 does not inhibit the enzymatic activity of PP1alpha
-
additional information
-
knockout of Ste20-like kinase, Mst2, reduces the expression of the catalytic subunit of PP2A, RNAi silencing of Mst2 triggers a striking proteasome-dependent decrease in the levels of the catalytic subunit of PP2A. Mst2-dependent stabilization of PP2A-C is a posttranslational process likely involving a reduction in proteasome-dependent PP2A-C degradation
-
additional information
-
not inhibited by NIPP-1 and inhibitor 2
-
additional information
-
not inhibited by NIPP-1
-
additional information
-
no inhibition by okadaic acid
-
additional information
-
protein phosphatase inhibitor II and cyclosporin A have no inhibitory effect on isozyme PP2A
-
additional information
-
no inhibition by okadaic acid
-
additional information
-
addition of EGTA and vanadate to the assay does not affect the enzyme activity
-
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evolution
analysis of mechanisms controlling the phosphorylation of these proteins and focus on the role of altered dephosphorylation via local type-1, type-2A and type-2B phosphatases (PP1, PP2A, and PP2B, also known as calcineurin, respectively)
evolution
analysis of mechanisms controlling the phosphorylation of these proteins and focus on the role of altered dephosphorylation via local type-1, type-2A and type-2B phosphatases (PP1, PP2A, and PP2B, also known as calcineurin, respectively). Three different CnA isoforms (CnAalpha/PPP3CA, CnAbeta/PPP3CB, and CnAgamma/PPP3CC) have been identified, of which CnAalpha and CnAbeta are ubiquitously expressed. CnB is expressed by two genes (CnBalpha/PPP3R1 and CnBbeta/PPP3R2)
evolution
-
clustering analyses of PP2As in sweet potato, overview
evolution
enzyme DhSIT4 is a member of PPP6 class of serine threonine phosphatases from the halotolerant yeast Debaryomyces hansenii
evolution
enzyme PphC belongs to the eukaryote-like Ser/Thr phosphatases (eSTPs) in Escherichia coli, that have extensive sequence and structural homology to eukaryotic Ser/Thr protein phosphatase 2C (PP2C) phosphatases. But YegK is an atypical PP2C-like phosphatase. Unlike other bacterial PP2C homologues, YegK contains only six of the eight absolutely conserved residues that are involved in metal binding, coordination, and catalysis, instead of eleven. In particular, the amino acid sequence alignment clearly shows that YegK lacks the conserved glycine residue in motif VI and the aspartic acid residue in motif VIII
evolution
group A Streptococcus (GAS) Streptococcus pyogenes is a human pathogen that causes high morbidity and mortality. GAS lacks a gene encoding tyrosine kinase but contains one encoding tyrosine phosphatase (SP-PTP). SP-PTP falls into the category of low-molecular weight PTPases (LMW PTPases)
evolution
group A Streptococcus (GAS) Streptococcus pyogenes is a human pathogen that causes high morbidity and mortality. GAS lacks a gene encoding tyrosine kinase but contains one encoding tyrosine phosphatase (SP-PTP). SP-PTP falls into the category of low-molecular weight PTPases (LMW PTPases)
evolution
the enzyme belongs to the protein phosphatase 2C (PP2C) subfamily. Comparison of PrpC with typical PP2C phosphatases, overview
evolution
the enzyme is a member of the PTP superfamily, but VHR is a dual-specific enzyme (a DSP)
evolution
compared to kinetoplastid-specific phospho-protein phosphatase (PPP) in the sequence of locus Tb927.6.640 reveals two changes in the conserved PPP signature motif GDXXDRG: the second aspartate is replaced by asparagine and arginine is replaced by lysine. These changes are characteristic for an ApaH-like phosphatase (Alph), a subgroup of the PPP family that is closely related to the bacterial enzyme ApaH. Tb927.6.640 is referred to as TbALPH1. There are two further ApaH-like phosphatases in the Trypanosoma brucei genome: Tb927.4.4330 (TbALPH2) and Tb927.8.8040 (TbALPH3), but neither was identified as stress granule component or as involved in mRNA binding
evolution
-
enzyme DhSIT4 is a member of PPP6 class of serine threonine phosphatases from the halotolerant yeast Debaryomyces hansenii
-
evolution
-
enzyme DhSIT4 is a member of PPP6 class of serine threonine phosphatases from the halotolerant yeast Debaryomyces hansenii
-
evolution
-
enzyme DhSIT4 is a member of PPP6 class of serine threonine phosphatases from the halotolerant yeast Debaryomyces hansenii
-
evolution
-
enzyme PphC belongs to the eukaryote-like Ser/Thr phosphatases (eSTPs) in Escherichia coli, that have extensive sequence and structural homology to eukaryotic Ser/Thr protein phosphatase 2C (PP2C) phosphatases. But YegK is an atypical PP2C-like phosphatase. Unlike other bacterial PP2C homologues, YegK contains only six of the eight absolutely conserved residues that are involved in metal binding, coordination, and catalysis, instead of eleven. In particular, the amino acid sequence alignment clearly shows that YegK lacks the conserved glycine residue in motif VI and the aspartic acid residue in motif VIII
-
evolution
-
enzyme DhSIT4 is a member of PPP6 class of serine threonine phosphatases from the halotolerant yeast Debaryomyces hansenii
-
evolution
-
the enzyme belongs to the protein phosphatase 2C (PP2C) subfamily. Comparison of PrpC with typical PP2C phosphatases, overview
-
evolution
-
enzyme DhSIT4 is a member of PPP6 class of serine threonine phosphatases from the halotolerant yeast Debaryomyces hansenii
-
evolution
-
enzyme DhSIT4 is a member of PPP6 class of serine threonine phosphatases from the halotolerant yeast Debaryomyces hansenii
-
evolution
-
compared to kinetoplastid-specific phospho-protein phosphatase (PPP) in the sequence of locus Tb927.6.640 reveals two changes in the conserved PPP signature motif GDXXDRG: the second aspartate is replaced by asparagine and arginine is replaced by lysine. These changes are characteristic for an ApaH-like phosphatase (Alph), a subgroup of the PPP family that is closely related to the bacterial enzyme ApaH. Tb927.6.640 is referred to as TbALPH1. There are two further ApaH-like phosphatases in the Trypanosoma brucei genome: Tb927.4.4330 (TbALPH2) and Tb927.8.8040 (TbALPH3), but neither was identified as stress granule component or as involved in mRNA binding
-
malfunction
-
calcineurin inhibition by FK506 significantly enhances the phosphorylation of protein tau at Ser262, Ser198, Ser199, and/or Ser202 and Ser396, and/or Ser404, overview
malfunction
-
calcineurin inhibition in fibroblasts and keratinocytes may be of influence on the overall functioning of the skin immune system
malfunction
-
calcineurin is involved in and a therapeutic target in myasthenia gravis, clinical parameters, overview
malfunction
-
calcineurin participates in neuronal apoptosis, protection of neurons from apoptosis by apolipoprotein E-containing lipoproteins does not require lipoprotein uptake and involves activation of phospholipase Cgamma1 and inhibition of calcineurin
malfunction
-
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
malfunction
-
malfunctions of C-kinase-activated PP1 inhibitor proteins are linked to a variety of diseases, including cardiovascular disease and cancer
malfunction
-
modest elevation in expression afforded by a single extra transgenic copy of Dscr1 is sufficient to confer significant suppression of tumor growth in mice and that such resistance is a consequence of a deficit in tumor angiogenesis arising from suppression of the calcineurin pathway. Attenuation of calcineurin activity by DSCR1 together with another chromosome 21 gene DYRK1A, may be sufficient to dramatically diminish angiogenesis
malfunction
-
partly malignancy-dependent role of calcineurin in melanoma cell lines, overview. Calcineurin-inhibiting compounds are applied for local treatment of psoriasis or atopic dermatitis
malfunction
-
perturbations in the regulation of PP1 by inhibitor-1 have been implicated in the pathogenesis of heart failure, role of PP1 and protein phosphatase-1 inhibitor-1 in the failing heart, overview
malfunction
-
perturbations in the regulation of PP1 by inhibitor-1 have been implicated in the pathogenesis of heart failure, role of PP1 and protein phosphatase-1 inhibitor-1 in the failing heart, overview
malfunction
-
perturbations in the regulation of PP1 by inhibitor-1 have been implicated in the pathogenesis of heart failure, role of PP1 and protein phosphatase-1 inhibitor-1 in the failing heart, overview
malfunction
-
perturbations in the regulation of PP1 by inhibitor-1 have been implicated in the pathogenesis of heart failure, role of PP1 and protein phosphatase-1 inhibitor-1 in the failing heart, overview
malfunction
-
a decrease in alpha-isoform of PP2A catalytic subunit accelerates osteoblast differentiation through the expression of bone-related genes
malfunction
-
inhibition of protein phosphatase 2A results in changes in the organization of endothelial cell cytoskeleton as microtubule dissolution and actin re-arrangement are detected. Depletion of Balpha regulatory subunit of protein phosphatase 2A has similar effect on the cytoskeleton structure of the cells
malfunction
-
knockdown of protein phosphatase PP1-3 leads to a coordinated rearrangement of cellular organelles and compartments in the procyclic trypanosome
malfunction
absence of SP-PTP and SP-PTP enzymatic activity adversely affects GAS cell morphology, the slow growth of M1T1DELTAPTP is associated with defective cell divisiony. The GAS mutant lacking SP-PTP poorly adheres to and invades human respiratory cells and affects in vivo phosphorylation events in human respiratory cells, phenotype
malfunction
absence of SP-PTP and SP-PTP enzymatic activity adversely affects GAS cell morphology, the slow growth of M1T1DELTAPTP is associated with defective cell divisiony. The GAS mutant lacking SP-PTP poorly adheres to and invades human respiratory cells and affects in vivo phosphorylation events in human respiratory cells, phenotype
malfunction
Streptococcus pneumoniae serotype 4
catalytic inactivation or absence of PhpP results in the hyperphosphorylation of Ser/Thr protein kinase (StkP) substrates and specific phenotypic changes, including sensitivity to environmental stresses and competence deficiency. The morphology of the DELTAphpP cells resembles the StkP overexpression phenotype and conversely, overexpression of PhpP results in cell elongation mimicking the stkP null phenotype. Proteomic analysis of the phpP knockout strain permits identification of a StkP/PhpP substrate, Spr1851, a putative RNA-binding protein homologous to Jag. Pneumococcal protein Jag is phosphorylated on Thr89. Inactivation of jag confers a phenotype similar to the phpP mutant strain. The unencapsulated Rx1 phpP knockout strain is viable. The morphology of both, the unencapsulated phpP null mutant and the phpP overexpression strain, clearly demonstrated that PhpP participates in the regulation of cell division and has an opposite regulatory effect to that of Ser/Thr protein kinase, StkP. The phpP knockout strain is sensitive to elevated temperature and oxidative stress
malfunction
-
decreased PP2A activity promotes cellular transformation, and numerous studies have highlighted a tumor suppressor role for PP2A. PP2A loss-of-function occurs by molecular mechanisms such as mutations of the PP2A subunits, phosphorylation and methylation of PP2A-C, deregulation of the expression of the regulatory subunits or endogenous PP2A inhibitors. PP2A inhibition impairs double strand break (DSB) repair by homologous recombination
malfunction
deletion of DhSIT4 in Debaryomyces hansenii is not lethal but the mutant exhibits reduced growth due to its effect on the cell cycle. The knockout mutant Dhsit4DELTA shows sensitivity towards Li+, Na+ and cell wall damaging agents. Growth pattern of Dhsit4DELTA knockout mutant in the presence of toxic cations and oxidative agents, overview. The expression of DhSit4p rescues salt, caffeine and calcofluor white sensitivity of Dhmpk1DELTA strain and thereby indicating a genetic interaction of this phosphatase with the cell wall integrity pathway in this species. Antagonistic roles of DhSit4p and DhPpz1p in maintaining the cell cycle and ion homeostasis in Debaryomyces hansenii. Mutant phenotype, overview
malfunction
depletion of PPP5C via RNAi remarkably inhibits glioma cell proliferation and colony formation, and arrests cell cycle in the G0/G1 phase. Moreover, knockdown of PP5 markedly suppresses glioma cell migration
malfunction
dysfunction of the regulation of cardiac proteins by serine/threonine protein phosphatases can contribute to the initiation, maintenance and progression of cardiac arrhythmias. Atrial fibrillation (AF) is the most common heart rhythm disorder and is characterized by electrical, autonomic, calcium-handling, contractile, and structural remodeling, which include, among other things, changes in the phosphorylation status of a wide range of proteins. AF-associated alterations in the phosphorylation of atrial ion channels, calcium-handling and contractile proteins, and their role in atrial fibrillation-pathophysiology, overview. AF significantly affects morbidity and mortality as a risk factor for worsening heart failure and stroke. 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. The regulatory subunit I-1 (PPP1R1A) of phosphatase PP1 is dephosphorylated at Thr35 by phosphatase PP2A deactivating I-1 and thus activating enzyme PP1. PKCalpha phosphorylates I-1 on Ser67, decreasing I-1 activity and substrate phosphorylation, but Ser67 phosphorylation levels are unchanged in AF patients. AF-related changes in I-1-mediated regulation (inhibition) of PP1 are unlikely to explain the increase in global PP1 activity. Altered regulation of cardiac electrophysiology and contraction by protein phosphatases in AF, AF-related modulation of Ca2+-handling by protein phosphatases, overview. Increased phosphatase activity in heart failure decreases gap-junction coupling through multiple mechanisms. Loss of PP1beta increases phosphorylation of myosin light chain 2 and cMyBP-C
malfunction
dysfunction of the regulation of cardiac proteins by serine/threonine protein phosphatases can contribute to the initiation, maintenance and progression of cardiac arrhythmias. Atrial fibrillation (AF) is the most common heart rhythm disorder and is characterized by electrical, autonomic, calcium-handling, contractile, and structural remodeling, which include, among other things, changes in the phosphorylation status of a wide range of proteins. Atrial fibrillation-associated alterations in the phosphorylation of atrial ion channels, calcium-handling and contractile proteins, and their role in atrial fibrillation-pathophysiology, overview. Atrial fibrillation significantly affects morbidity and mortality as a risk factor for worsening heart failure and stroke. Altered regulation of cardiac electrophysiology and contraction by protein phosphatases in AF, AF-related modulation of Ca2+-handling by protein phosphatases, overview. Increased phosphatase activity in heart failure decreases gap-junction coupling through multiple mechanisms
malfunction
dysfunction of the regulation of cardiac proteins by serine/threonine protein phosphatases can contribute to the initiation, maintenance and progression of cardiac arrhythmias. Atrial fibrillation (AF) is the most common heart rhythm disorder and is characterized by electrical, autonomic, calcium-handling, contractile, and structural remodeling, which include, among other things, changes in the phosphorylation status of a wide range of proteins. Atrial fibrillation-associated alterations in the phosphorylation of atrial ion channels, calcium-handling and contractile proteins, and their role in atrial fibrillation-pathophysiology, overview. Atrial fibrillation significantly affects morbidity and mortality as a risk factor for worsening heart failure and stroke. Both expression and activity of calcineurin A subunit are increased in paroxysmal atrial fibrillation and chronic atrial fibrillation patients. Altered regulation of cardiac electrophysiology and contraction by protein phosphatases in AF, AF-related modulation of Ca2+-handling by protein phosphatases, overview
malfunction
-
overexpression of PstP leads to elongated cells and partially compromised survival. Depletion of PstP in Mycobacterium smegmatis leads to cell death
malfunction
overexpression of PstP leads to elongated cells and partially compromised survival. Depletion of PstP is detrimental to cell survival, eventually leading to cell death. PstP depletion results in elongated multiseptate cells, suggesting a role for PstP in regulating cell division events. Depletion of PstP decreases the bacillary load even in an established infection. Marginally compromised survival in complementation experiments. All of the domains, including the extracellular domain, are necessary for complete rescue. Depletion of PstP from established infections causes pathogen clearance, indicating that the continued presence of PstP is necessary for pathogen survival
malfunction
phosphorylation of PTPN12 at Ser19 by CDK2 impairs recruitment of the serine/threonine-protein kinase 1 (PAK1) to HER2, resulting in the blockade of the HER2-pY1196-PAK1-T423 signaling pathway, thus increases tumor cell motility. Decreased PTPN12 protein level is associated with poor prognosis of several types of cancers. Phosphorylation of Ser19 by CDK2 specifically increases EGF-induced HER2-pY1196 and PAK1-pT423 phosphorylation
malfunction
specific inhibition of calcineurin prevents axonal elongation, affects tau phosphorylation state and interferes with the establishment of cell polarity. Inhibition of PP2A, and to a lesser extent of calcineurin, enhances MAP1B phosphorylation and inhibit its microtubule binding activity
malfunction
specific inhibition of PP2A/Balpha is associated with enhanced tau phosphorylation, and subsequent inability of tau to bind to and stabilize microtubules. Deregulation of the microtubule cytoskeleton can in turn contribute to the inhibition of neurite outgrowth observed following silencing of PP2A/Balpha. Inhibition of PP2A, and to a lesser extent of calcineurin, enhances MAP1B phosphorylation and inhibit its microtubule binding activity
malfunction
toxins that bind and block the PP1 active site are lethal, thus, potential drugs that target PP1 must interact outside the PP1 active site
malfunction
triple knockdown of Sj-pp1c genes by RNA interference causes stunted growth and decreased pairing stability of worm pairs, as well as a remarkable reduction in cell proliferation activity and defects in reproductive maturation and fecundity, phenotypes, overview
malfunction
ALPH1 depletion is lethal and results in a massive, global increase in mRNAs, that are deadenylated but have not yet started degradation. ALPH1 RNAi depletion causes growth arrest and increase in mRNA levels. RNAi depletion of ALPH1 causes a significant increase in mRNA levels for all mRNAs analysed. Total mRNA levels increase 1.7/2.2fold after 48/72 hours of ALPH1 RNAi induction. Concerning the two developmentally regulated mRNAs, GPI-PLC mRNA increases 4.2/4-6fold and PGKC mRNA increases 16/22fold after 48/72 hours of RNAi induction. RNAi phenotype of ALPH1 includes cell growth stop, total mRNA levels increase about 2fold and a particular pronounced effect on unstable, developmentally regulated mRNAs. The mRNAs that accumulate after ALPH1 RNAi depletion are deadenylated, overview. ALPH1 RNAi depletion causes an increase in intact mRNA molecules, but no increase in decay intermediates
malfunction
-
deletion of DhSIT4 in Debaryomyces hansenii is not lethal but the mutant exhibits reduced growth due to its effect on the cell cycle. The knockout mutant Dhsit4DELTA shows sensitivity towards Li+, Na+ and cell wall damaging agents. Growth pattern of Dhsit4DELTA knockout mutant in the presence of toxic cations and oxidative agents, overview. The expression of DhSit4p rescues salt, caffeine and calcofluor white sensitivity of Dhmpk1DELTA strain and thereby indicating a genetic interaction of this phosphatase with the cell wall integrity pathway in this species. Antagonistic roles of DhSit4p and DhPpz1p in maintaining the cell cycle and ion homeostasis in Debaryomyces hansenii. Mutant phenotype, overview
-
malfunction
-
deletion of DhSIT4 in Debaryomyces hansenii is not lethal but the mutant exhibits reduced growth due to its effect on the cell cycle. The knockout mutant Dhsit4DELTA shows sensitivity towards Li+, Na+ and cell wall damaging agents. Growth pattern of Dhsit4DELTA knockout mutant in the presence of toxic cations and oxidative agents, overview. The expression of DhSit4p rescues salt, caffeine and calcofluor white sensitivity of Dhmpk1DELTA strain and thereby indicating a genetic interaction of this phosphatase with the cell wall integrity pathway in this species. Antagonistic roles of DhSit4p and DhPpz1p in maintaining the cell cycle and ion homeostasis in Debaryomyces hansenii. Mutant phenotype, overview
-
malfunction
-
catalytic inactivation or absence of PhpP results in the hyperphosphorylation of Ser/Thr protein kinase (StkP) substrates and specific phenotypic changes, including sensitivity to environmental stresses and competence deficiency. The morphology of the DELTAphpP cells resembles the StkP overexpression phenotype and conversely, overexpression of PhpP results in cell elongation mimicking the stkP null phenotype. Proteomic analysis of the phpP knockout strain permits identification of a StkP/PhpP substrate, Spr1851, a putative RNA-binding protein homologous to Jag. Pneumococcal protein Jag is phosphorylated on Thr89. Inactivation of jag confers a phenotype similar to the phpP mutant strain. The unencapsulated Rx1 phpP knockout strain is viable. The morphology of both, the unencapsulated phpP null mutant and the phpP overexpression strain, clearly demonstrated that PhpP participates in the regulation of cell division and has an opposite regulatory effect to that of Ser/Thr protein kinase, StkP. The phpP knockout strain is sensitive to elevated temperature and oxidative stress
-
malfunction
-
deletion of DhSIT4 in Debaryomyces hansenii is not lethal but the mutant exhibits reduced growth due to its effect on the cell cycle. The knockout mutant Dhsit4DELTA shows sensitivity towards Li+, Na+ and cell wall damaging agents. Growth pattern of Dhsit4DELTA knockout mutant in the presence of toxic cations and oxidative agents, overview. The expression of DhSit4p rescues salt, caffeine and calcofluor white sensitivity of Dhmpk1DELTA strain and thereby indicating a genetic interaction of this phosphatase with the cell wall integrity pathway in this species. Antagonistic roles of DhSit4p and DhPpz1p in maintaining the cell cycle and ion homeostasis in Debaryomyces hansenii. Mutant phenotype, overview
-
malfunction
-
overexpression of PstP leads to elongated cells and partially compromised survival. Depletion of PstP is detrimental to cell survival, eventually leading to cell death. PstP depletion results in elongated multiseptate cells, suggesting a role for PstP in regulating cell division events. Depletion of PstP decreases the bacillary load even in an established infection. Marginally compromised survival in complementation experiments. All of the domains, including the extracellular domain, are necessary for complete rescue. Depletion of PstP from established infections causes pathogen clearance, indicating that the continued presence of PstP is necessary for pathogen survival
-
malfunction
-
absence of SP-PTP and SP-PTP enzymatic activity adversely affects GAS cell morphology, the slow growth of M1T1DELTAPTP is associated with defective cell divisiony. The GAS mutant lacking SP-PTP poorly adheres to and invades human respiratory cells and affects in vivo phosphorylation events in human respiratory cells, phenotype
-
malfunction
-
deletion of DhSIT4 in Debaryomyces hansenii is not lethal but the mutant exhibits reduced growth due to its effect on the cell cycle. The knockout mutant Dhsit4DELTA shows sensitivity towards Li+, Na+ and cell wall damaging agents. Growth pattern of Dhsit4DELTA knockout mutant in the presence of toxic cations and oxidative agents, overview. The expression of DhSit4p rescues salt, caffeine and calcofluor white sensitivity of Dhmpk1DELTA strain and thereby indicating a genetic interaction of this phosphatase with the cell wall integrity pathway in this species. Antagonistic roles of DhSit4p and DhPpz1p in maintaining the cell cycle and ion homeostasis in Debaryomyces hansenii. Mutant phenotype, overview
-
malfunction
Streptococcus pneumoniae serotype 4 Rx1
-
catalytic inactivation or absence of PhpP results in the hyperphosphorylation of Ser/Thr protein kinase (StkP) substrates and specific phenotypic changes, including sensitivity to environmental stresses and competence deficiency. The morphology of the DELTAphpP cells resembles the StkP overexpression phenotype and conversely, overexpression of PhpP results in cell elongation mimicking the stkP null phenotype. Proteomic analysis of the phpP knockout strain permits identification of a StkP/PhpP substrate, Spr1851, a putative RNA-binding protein homologous to Jag. Pneumococcal protein Jag is phosphorylated on Thr89. Inactivation of jag confers a phenotype similar to the phpP mutant strain. The unencapsulated Rx1 phpP knockout strain is viable. The morphology of both, the unencapsulated phpP null mutant and the phpP overexpression strain, clearly demonstrated that PhpP participates in the regulation of cell division and has an opposite regulatory effect to that of Ser/Thr protein kinase, StkP. The phpP knockout strain is sensitive to elevated temperature and oxidative stress
-
malfunction
-
deletion of DhSIT4 in Debaryomyces hansenii is not lethal but the mutant exhibits reduced growth due to its effect on the cell cycle. The knockout mutant Dhsit4DELTA shows sensitivity towards Li+, Na+ and cell wall damaging agents. Growth pattern of Dhsit4DELTA knockout mutant in the presence of toxic cations and oxidative agents, overview. The expression of DhSit4p rescues salt, caffeine and calcofluor white sensitivity of Dhmpk1DELTA strain and thereby indicating a genetic interaction of this phosphatase with the cell wall integrity pathway in this species. Antagonistic roles of DhSit4p and DhPpz1p in maintaining the cell cycle and ion homeostasis in Debaryomyces hansenii. Mutant phenotype, overview
-
malfunction
-
catalytic inactivation or absence of PhpP results in the hyperphosphorylation of Ser/Thr protein kinase (StkP) substrates and specific phenotypic changes, including sensitivity to environmental stresses and competence deficiency. The morphology of the DELTAphpP cells resembles the StkP overexpression phenotype and conversely, overexpression of PhpP results in cell elongation mimicking the stkP null phenotype. Proteomic analysis of the phpP knockout strain permits identification of a StkP/PhpP substrate, Spr1851, a putative RNA-binding protein homologous to Jag. Pneumococcal protein Jag is phosphorylated on Thr89. Inactivation of jag confers a phenotype similar to the phpP mutant strain. The unencapsulated Rx1 phpP knockout strain is viable. The morphology of both, the unencapsulated phpP null mutant and the phpP overexpression strain, clearly demonstrated that PhpP participates in the regulation of cell division and has an opposite regulatory effect to that of Ser/Thr protein kinase, StkP. The phpP knockout strain is sensitive to elevated temperature and oxidative stress
-
malfunction
-
deletion of DhSIT4 in Debaryomyces hansenii is not lethal but the mutant exhibits reduced growth due to its effect on the cell cycle. The knockout mutant Dhsit4DELTA shows sensitivity towards Li+, Na+ and cell wall damaging agents. Growth pattern of Dhsit4DELTA knockout mutant in the presence of toxic cations and oxidative agents, overview. The expression of DhSit4p rescues salt, caffeine and calcofluor white sensitivity of Dhmpk1DELTA strain and thereby indicating a genetic interaction of this phosphatase with the cell wall integrity pathway in this species. Antagonistic roles of DhSit4p and DhPpz1p in maintaining the cell cycle and ion homeostasis in Debaryomyces hansenii. Mutant phenotype, overview
-
malfunction
-
ALPH1 depletion is lethal and results in a massive, global increase in mRNAs, that are deadenylated but have not yet started degradation. ALPH1 RNAi depletion causes growth arrest and increase in mRNA levels. RNAi depletion of ALPH1 causes a significant increase in mRNA levels for all mRNAs analysed. Total mRNA levels increase 1.7/2.2fold after 48/72 hours of ALPH1 RNAi induction. Concerning the two developmentally regulated mRNAs, GPI-PLC mRNA increases 4.2/4-6fold and PGKC mRNA increases 16/22fold after 48/72 hours of RNAi induction. RNAi phenotype of ALPH1 includes cell growth stop, total mRNA levels increase about 2fold and a particular pronounced effect on unstable, developmentally regulated mRNAs. The mRNAs that accumulate after ALPH1 RNAi depletion are deadenylated, overview. ALPH1 RNAi depletion causes an increase in intact mRNA molecules, but no increase in decay intermediates
-
metabolism
-
the enzyme is involved in the Raf-1/ERK pathway, overview
metabolism
-
the enzyme is involved in the Raf-1/ERK pathway, overview
metabolism
-
Ser/Thr phosphatase Ppq1 down-regulates mating signaling by targeting at or upstream of the terminal MAP kinase Fus3 in the cascade
metabolism
a CDK2-mediated phosphorylation-based substrate recognition mechanism of PTPN12 orchestrated signaling crosstalk between the oncogenic CDK2 and HER2 pathways
metabolism
-
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
-
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
-
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
metabolism
multi-protein cytoskeletal scaffolds can also influence the regulation of these phosphatases, with important implications for neuronal signalling and homeostasis. Deregulation of the cytoskeletal scaffolds and phosphatase dysfunction are associated with many neurological diseases. PP2A- and PP1-dependent regulation of neurofilament architecture and regulation of the neuronal actin cytoskeleton by PP2A, PP1 and calcineurin, overview
metabolism
multi-protein cytoskeletal scaffolds can also influence the regulation of these phosphatases, with important implications for neuronal signalling and homeostasis. Deregulation of the cytoskeletal scaffolds and phosphatase dysfunction are associated with many neurological diseases. PP2A- and PP1-dependent regulation of neurofilament architecture, and regulation of the neuronal actin cytoskeleton by PP2A, PP1 and calcineurin, overview
metabolism
multi-protein cytoskeletal scaffolds can also influence the regulation of these phosphatases, with important implications for neuronal signalling and homeostasis. Deregulation of the cytoskeletal scaffolds and phosphatase dysfunction are associated with many neurological diseases. PP2A- and PP1-dependent regulation of neurofilament architecture, and regulation of the neuronal actin cytoskeleton by PP2A, PP1 and calcineurin, overview. Regulation of neurofilaments by PP2A, PP1 and calcineurin, functional significance of neurofilament (de)phosphorylation in neuronal homeostasis
metabolism
role of DhSIT4 in cell wall integrity (CWI) signaling pathway in Debaryomyces hansenii
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
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metabolism
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role of DhSIT4 in cell wall integrity (CWI) signaling pathway in Debaryomyces hansenii
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metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
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metabolism
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role of DhSIT4 in cell wall integrity (CWI) signaling pathway in Debaryomyces hansenii
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metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
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metabolism
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role of DhSIT4 in cell wall integrity (CWI) signaling pathway in Debaryomyces hansenii
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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role of DhSIT4 in cell wall integrity (CWI) signaling pathway in Debaryomyces hansenii
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
-
metabolism
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Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
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metabolism
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role of DhSIT4 in cell wall integrity (CWI) signaling pathway in Debaryomyces hansenii
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metabolism
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role of DhSIT4 in cell wall integrity (CWI) signaling pathway in Debaryomyces hansenii
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physiological function
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PGAM5 is an evolutionarily conserved activator of apoptosis signal-regulating kinase 1
physiological function
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PGAM5 is an evolutionarily conserved activator of apoptosis signal-regulating kinase 1
physiological function
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Ca2+-calcineurin signaling
physiological function
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calcineurin is one of the target molecules regulated by the changes of intracellular Ca2+ level, it has a regulatory role in Ca2+ cytosolic concentration and signaling in chondrogenic cells, Ca2+ plays an important role in chondrogenesis, cartilage formation and cartilage differentiation, overview
physiological function
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calcineurin play roles in various signaling pathways such as fertility, movement, body size regulation and serotonin-mediated egg laying
physiological function
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calcineurin plays an important role in brain function and in regulation of tau phosphorylation
physiological function
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opposing the protein kinase A axis are protein phosphatases that dephosphorylate regulatory proteins, e.g. ryanodine receptor and phospholamban in sarcoplasmic reticulum, troponin I and C-protein in the myofilaments, and the plasma membrane L-type calcium channel, and play an essential role in maintaining biochemical and functional phosphorylation homeostasis, overview
physiological function
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PP1 phosphorylation is essential for proper cell cycle progression. NIPP1-associated PP1 regulates Sap155 phosphorylation, overview
physiological function
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the Ca2+/calmodulin-dependent protein phosphatase calcineurin is a key mediator in antigen-specific T-cell activation
physiological function
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the enzyme is involved in regulation of diverse enzyme functions via de-/activation of phosphoproteins through dephosphorylation, in the same way its inhibitor protein phosphatase-1 inhibitor-1, phosphoproteomic analysis, overview
physiological function
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topical calcineurin inhibits DNA repair and reduces apoptosis in epidermal keratinocytes
physiological function
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type 1 protein phosphatase is a critical negative regulator of Ca2+ cycling and contractility in the cardiomyocyte. In particular, it mediates restoration of cardiac function to basal levels, after beta-adrenergic stimulation, by dephosphorylating key phospho-proteins, role of PP1 in the heart and its critical regulation by the endogenous phospho-protein I-1, overview
physiological function
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type 1 protein phosphatase is a critical negative regulator of Ca2+ cycling and contractility in the cardiomyocyte. In particular, it mediates restoration of cardiac function to basal levels, after beta-adrenergic stimulation, by dephosphorylating key phospho-proteins, role of PP1 in the heart and its critical regulation by the endogenous phospho-protein I-1, overview
physiological function
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type 1 protein phosphatase is a critical negative regulator of Ca2+ cycling and contractility in the cardiomyocyte. In particular, it mediates restoration of cardiac function to basal levels, after beta-adrenergic stimulation, by dephosphorylating key phospho-proteins, role of PP1 in the heart and its critical regulation by the endogenous phospho-protein I-1, overview
physiological function
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type 1 protein phosphatase is a critical negative regulator of Ca2+ cycling and contractility in the cardiomyocyte. In particular, it mediates restoration of cardiac function to basal levels, after beta-adrenergic stimulation, by dephosphorylating key phospho-proteins, role of PP1 in the heart and its critical regulation by the endogenous phospho-protein I-1, overview
physiological function
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cytoplasmic accumulation of the enzyme induces Ebola virus transcription
physiological function
isofom PPP1CC1 participates in actin-related function, mitosis, brain function, vesicular trafficking, and other functions
physiological function
isoform PP1 plays critical roles in an enormous variety of cellular processes such as cell cycle progression, protein synthesis, carbohydrate metabolism and apoptosis
physiological function
isoform PPP1CA participates in nuclear function, androgen receptor signaling, TGFbeta signaling, protein synthesis, cell cylcle/apoptosis, brain function, actin-related function, centrosomal and other functions
physiological function
isoform PPP1CB participates in muscle function, glycogen metabolism, nuclear function, cell shortening and spreading, and cellular homeostasis
physiological function
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overexpression of subunit PP2A Calpha reduces alkaline phosphatase activity. Osteoblast differentiation and mineralization are decreased in subunit PP2A Calpha-overexpressing cells, with reduction of bone-related genes including osterix, bone sialoprotein, and osteocalcin
physiological function
PP1 regulates diverse, essential cellular processes such as cell cycle progression, protein synthesis, muscle contraction, carbohydrate metabolism, transcription and neuronal signaling
physiological function
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PP5 enhances thermotolerance via forming multi-chaperone complexes with heat shock protein 90.2 under heat shock conditions (42°C) in Arabidopsis
physiological function
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protein phosphatase 1 participates in cell cycle regulation, salinity tolerance, cytokinin production, embryo development, blue-light signaling, cell differentiation, cell patterning, cell division, and gene silencing. Protein phosphatase 2A is intimately involved in regulating intracellular responses to brassinosteroids. Functions of PP5 include roles in disease resistance, thermotolerance, and light detection, while PP7 is implicated in several sensory functions, in particular, light sensing through the regulation of cryptochrome and phytochrome
physiological function
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protein phosphatase PP1-3 is essential in conserving the intracellular organisation of the procyclic trypanosome cell
physiological function
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the enzyme is essential for asexual development and plant infection
physiological function
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the enzyme plays a significant role in the maintenance of endothelial cell cytoskeleton and barrier function with special focus on the Balpha (regulatory) subunit of protein phosphatase 2A. The PP2A Balpha regulatory subunit associates with adherent junction proteins
physiological function
calcineurin (PP2B) is a Ca2+-dependent phosphatase consisting of catalytic (CnA) and regulatory (CnB) subunits that link Ca2+- and phosphorylation-dependent signaling pathways. Serine/threonine protein phosphatases control dephosphorylation of numerous cardiac proteins, including a variety of ion channels and calcium-handling proteins, thereby providing precise post-translational regulation of cardiac electrophysiology and function
physiological function
Streptococcus pneumoniae serotype 4
enzyme PhpP and StkP cooperatively regulate cell division of Streptococcus pneumoniae and phosphorylate putative RNA binding protein Jag
physiological function
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phosphorylation of the aquaporin-2 (AQP2) water channel at four COOH-terminal serines plays a central role in the regulation of water permeability of the renal collecting duct. The level of phosphorylation at these sites is determined by a balance between phosphorylation by protein kinases and dephosphorylation by phosphatases. Serine/threonine phosphatases and aquaporin-2 regulation in renal collecting duct, overview
physiological function
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phosphorylation of the aquaporin-2 (AQP2) water channel at four COOH-terminal serines plays a central role in the regulation of water permeability of the renal collecting duct. The level of phosphorylation at these sites is determined by a balance between phosphorylation by protein kinases and dephosphorylation by phosphatases. Serine/threonine phosphatases and aquaporin-2 regulation in renal collecting duct, overview
physiological function
protein phosphatase 1 (PP1) is an enzyme essential to cell viability in the malaria parasite Plasmodium falciparum. The activity of PP1 is regulated by the binding of regulatory subunits, of which there are 3 reported for the parasite to date
physiological function
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protein phosphatase 2A (PP2A) is a major intracellular protein phosphatase that plays crucial roles in hormone signal transduction and abiotic stress response. IbPP2A1 is an abiotic stress-responsive gene, but it cannot work alone in vitro
physiological function
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protein phosphatase PP2A controls a variety of cellular functions through a broad spectrum of substrates, including cell cycle regulation, apoptosis, mitosis and DNA damage repair, and controls major signaling pathways including the MAPK and AKT pathways. The RAS-related small GTPase RHOB positively regulates PP2A, one of the major cellular serine-threonine phosphatases, by recruiting its regulatory subunit B55. Role of the RHOB/PP2A/AKT1/RAC1 pathway in relation to mesenchymal migration and invasion in lung cancer, overview. RHOB binds and activates the tumor suppressor PP2A, RHOB binds to the catalytic subunit of PP2A. PP2A is known to play a prevalent role in dephosphorylating histone 2A (gH2AX) after treatment with the selective topoisomerase I inhibitor camptothecin
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme All1758 is a PP2C phosphatase involved in diazotrophic growth, cell morphology, and glycolipid synthesis
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme IcfG is a PP2C phosphatase
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme PphA is a PPM phosphatase
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme PrpA is a PPP phosphatase
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme PrpC is a PP2C phosphatase
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme PrpC is a PP2C phosphatase
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme PssZ is a PP2C phosphatase involved in cell envelope biogenesis, stress response, and motility
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme SpoIIE is a PPM phosphatase
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme Stp1 is a PP2C phosphatase
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme MG_207 is kinase MG_109. Enzyme MG_207 is a PPM phosphatase involved in cell signaling and virulence
physiological function
-
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme PhpP is kinase StkP. Enzyme PhpP is a PP2C phosphatase
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme Pph1 is kinase Pkn5. Enzyme Pph1 is a PP2C phosphatase
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme PppA is kinase PpkA. Enzyme PppA is a PP2C phosphatase
physiological function
-
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme PppL is kinase PknB. Enzyme PppL is a PP2C phosphatase
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme PrpC is kinase BA-Stk1. Enzyme PrpC is a PP2C phosphatase
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme PrpC is kinase PrkC. Enzyme PrpC is a PP2C phosphatase
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme PstP is kinase PknB. Enzyme PstP is a PPM phosphatase
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme SP-STP is kinase SP-STK. The enzyme is a PP2C phosphatase
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme Stp1 is kinase Stk1. Enzyme Stp1 is a PP2C phosphatase
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme Stp1 is kinase Stk1. Enzyme Stp1 is a PP2C phosphatase
physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme StpA is kinase Stk. Enzyme StpA is a PP2C phosphatase
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The enzyme is a PP2C phosphatase
physiological function
role of enzyme PPP5C in glioma cell migration, overview. PPP5C is essential for glioma cell growth and serve as a promising therapeutic target in human gliomas
physiological function
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serine/threonine protein phosphatase PstP of Mycobacterium tuberculosis is necessary for accurate cell division and survival of pathogen, role for PstP in regulating cell division events. The activity of PstP is essential for mycobacterial growth. All of the enzyme domains, including the extracellular domain, are necessary for enzyme activity in vivo. The catalytic activity of PstP is absolutely essential for the in vitro growth
physiological function
serine/threonine protein phosphatase PstP of Mycobacterium tuberculosis is necessary for accurate cell division and survival of pathogen, role for PstP in regulating cell division events. The activity of PstP is essential for mycobacterial growth. All of the enzyme domains, including the extracellular domain, are necessary for enzyme activity in vivo. The catalytic activity of PstP is absolutely essential for the in vitro growth
physiological function
serine/threonine protein phosphatases control dephosphorylation of numerous cardiac proteins, including a variety of ion channels and calcium-handling proteins, thereby providing precise post-translational regulation of cardiac electrophysiology and function. Dephosphorylation of I-1, the regulatory subunit I-1 (PPP1R1A) of phosphatase PP1, by PP2A deactivates I-1 and thus activates enzyme PP1. PP2A-A (PPP2R1) expression is unchanged in cAF patients, but the expression of PP2A-C (PPP2C) is increased, potentially explaining the increased enzymatic activity. By contrast, PP2A-C expression is unchanged in pAF patients. Functional regulation by PP2A is spatially-heterogeneous. Regulatory subunits may also play a critical inhibitory role in the regulation of PP2A activity in the heart. For example, B56alpha (PPP2R5A) overexpression decreases phosphatase activity and increases RyR2 phosphorylation, whereas loss of B56alpha results in PP2A-mediated RyR2 dephosphorylation. Atrial contractility is also regulated by phosphorylation of contractile proteins, including the inhibitory troponin subunit (TnI), which influences Ca2+-sensitivity of the myofilaments and cMyBP-C, which determines Ca2+-sensitivity and kinetics of cross-bridge cycling. PP1 and PP2A are the major phosphatases controlling dephosphorylation of myofilament proteins. PP1 preferentially dephosphorylates Ser23/24 on TnI, whereas PP2A induces a more uniform dephosphorylation
physiological function
serine/threonine protein phosphatases control dephosphorylation of numerous cardiac proteins, including a variety of ion channels and calcium-handling proteins, thereby providing precise post-translational regulation of cardiac electrophysiology and function. The PP2A-catalytic subunit can bind directly to the poreforming L-type Ca2+-channel alpha1C-subunit, in close proximity to the PKA phosphorylation site Ser1928, but this interaction can be further modulated by multiple regulatory subunits and other phosphatases. Disruption of PP2A binding using inhibitory peptides increase the L-type Ca2+-current, suggesting an important inhibitory role for channel-bound PP2A. PP1 and PP2A are the major phosphatases controlling dephosphorylation of myofilament proteins. PP1 preferentially dephosphorylates Ser23/24 on TnI, whereas PP2A induces a more uniform dephosphorylation
physiological function
SP-PTP is a secretory protein tyrosine phosphatase and plays a crucial role in group A Streptococcus (GAS) growth. As a group A Streptococcus, Streptococcus pyogenes is a human pathogen that causes high morbidity and mortality. It lacks a gene encoding tyrosine kinase but contains one encoding tyrosine phosphatase (SP-PTP). Enzymatically active SP-PTP plays a crucial role in cell division, the function of SP-PTP is physiologically relevant for GAS growth and cell division. SP-PTP is essential for GAS virulence
physiological function
SP-PTP is a secretory protein tyrosine phosphatase and plays a crucial role in group A Streptococcus (GAS) growth. As a group A Streptococcus, Streptococcus pyogenes is a human pathogen that causes high morbidity and mortality. It lacks a gene encoding tyrosine kinase but contains one encoding tyrosine phosphatase (SP-PTP). Enzymatically active SP-PTP plays a crucial role in cell division, the function of SP-PTP is physiologically relevant for GAS growth and cell division. SP-PTP is essential for GAS virulence
physiological function
the Escherichia coli eSTP acts to dephosphorylate another Ser/Thr kinase that is encoded in the same operon. Regulatory reversible protein phosphorylation is a conserved mechanism of signaling in all biological systems
physiological function
the protein tyrosine phosphatase nonreceptor type 12 (PTPN12) is a multifunctional protein. A CDK2-mediated phosphorylation-based substrate recognition mechanism of PTPN12 orchestrated signaling crosstalk between the oncogenic CDK2 and HER2 pathways
physiological function
the serine/threonine phosphatase DhSIT4 modulates cell cycle, salt tolerance and cell wall integrity in halotolerant yeast Debaryomyces hansenii, role of DhSIT4 in cell wall integrity (CWI) signaling pathway in Debaryomyces hansenii
physiological function
the Sj-pp1c genes are involved in controlling worm development and maturation mainly by regulating cell proliferation, eggshell synthesis, nutritional metabolism, cytoskeleton organization, and neural process. Fundamental contribution of Sj-PP1c to molecular mechanisms underlying the reproductive biology of schistosomes
physiological function
the Sj-pp1c genes are involved in controlling wormdevelopment and maturation mainly by regulating cell proliferation, eggshell synthesis, nutritional metabolism, cytoskeleton organization, and neural process. Fundamental contribution of Sj-PP1c to molecular mechanisms underlying the reproductive biology of schistosomes
physiological function
the stable and dynamic subsets of microtubules are differentially regulated by protein phosphorylation-dependent mechanism. Calcineurin is a major neuronal Ser/Thr protein phosphatase playing a role in the homeostasis of the neuronal cytoskeleton. The enzyme interacts with and dephosphorylates a variety of cytoskeletal proteins, resulting in major regulation of neuronal cytoskeletal dynamics. Calcineurin is the most abundant calmodulin-binding protein in adult brain, where it plays an important role in memory and plasticity. Calcineurin is responsible for alterations in the microtubule cytoskeleton during changes in synaptic function. It also binds to tau and co-localises with tau on microtubules. Calcineurin is especially well positioned to mediate interactions between microtubule and actin cytoskeletal systems during neuritogenesis. The MAP2 protein is differentially dephosphorylated by protein phosphatases PP2A, PP1 and calcineurin. PP2A, PP1 and calcineurin dephosphorylate MAPs, thereby affecting microtubule assembly. Regulation of neurofilaments by PP2A, PP1 and calcineurin, significance of neurofilament (de)phosphorylation in neuronal homeostasis
physiological function
the stable and dynamic subsets of microtubules are differentially regulated by protein phosphorylation-dependent mechanism. PP1 is a major neuronal Ser/Thr protein phosphatase playing a role in the homeostasis of the neuronal cytoskeleton. The enzyme interacts with and dephosphorylates a variety of cytoskeletal proteins, resulting in major regulation of neuronal cytoskeletal dynamics. The MAP2 protein is differentially dephosphorylated by protein phosphatases PP2A, PP1 and calcineurin. PP2A, PP1 and calcineurin dephosphorylate MAPs, thereby affecting microtubule assembly. Regulation of neurofilaments by PP2A, PP1, and calcineurin, significance of neurofilament (de)phosphorylation in neuronal homeostasis
physiological function
the stable and dynamic subsets of microtubules are differentially regulated by protein phosphorylation-dependent mechanism. PPA2 is a major neuronal Ser/Thr protein phosphatase playing a role in the homeostasis of the neuronal cytoskeleton. The enzyme interacts with and dephosphorylates a variety of cytoskeletal proteins, resulting in major regulation of neuronal cytoskeletal dynamics. PP2A is a major tau and MAP2 phosphatase, but it can only dephosphorylate these phospho-MAPs when they are not bound to microtubules. Microtubule depolymerisation releases enzyme PP2A (and MAPs), resulting in enhanced dephosphorylation of cytosolic tubulin, tau and other MAPs like MAP2 and MAP1B. The MAP2 protein is differentially dephosphorylated by protein phosphatases PP2A, PP1 and calcineurin. PP2A, PP1 and calcineurin dephosphorylate MAPs, thereby affecting microtubule assembly
physiological function
TbALPH1 has all features required of an mRNA decapping enzyme. In vitro experiments confirm that ALPH1 can sensitise a capped RNA to Xrn1 in the presence of an RNA 5' polyphosphatase. ALPH1 has an essential role in trypanosome mRNA metabolism. The trypanosome ApaH-like phosphatase ALPH1 has all characteristics of an mRNA decapping enzyme. The enzyme is essential and localises to P-bodies
physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme PppA is kinase PpkA. Enzyme PppA is a PP2C phosphatase
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physiological function
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the serine/threonine phosphatase DhSIT4 modulates cell cycle, salt tolerance and cell wall integrity in halotolerant yeast Debaryomyces hansenii, role of DhSIT4 in cell wall integrity (CWI) signaling pathway in Debaryomyces hansenii
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physiological function
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phosphorylation of the aquaporin-2 (AQP2) water channel at four COOH-terminal serines plays a central role in the regulation of water permeability of the renal collecting duct. The level of phosphorylation at these sites is determined by a balance between phosphorylation by protein kinases and dephosphorylation by phosphatases. Serine/threonine phosphatases and aquaporin-2 regulation in renal collecting duct, overview
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme PrpC is kinase PrkC. Enzyme PrpC is a PP2C phosphatase
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme SpoIIE is a PPM phosphatase
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physiological function
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the serine/threonine phosphatase DhSIT4 modulates cell cycle, salt tolerance and cell wall integrity in halotolerant yeast Debaryomyces hansenii, role of DhSIT4 in cell wall integrity (CWI) signaling pathway in Debaryomyces hansenii
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme PrpC is a PP2C phosphatase
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme Pph1 is kinase Pkn5. Enzyme Pph1 is a PP2C phosphatase
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme MG_207 is kinase MG_109. Enzyme MG_207 is a PPM phosphatase involved in cell signaling and virulence
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme PrpC is a PP2C phosphatase
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme PppA is kinase PpkA. Enzyme PppA is a PP2C phosphatase
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme IcfG is a PP2C phosphatase
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme MG_207 is kinase MG_109. Enzyme MG_207 is a PPM phosphatase involved in cell signaling and virulence
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physiological function
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the enzyme is essential for asexual development and plant infection
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme PrpC is a PP2C phosphatase
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physiological function
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enzyme PhpP and StkP cooperatively regulate cell division of Streptococcus pneumoniae and phosphorylate putative RNA binding protein Jag
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme PppA is kinase PpkA. Enzyme PppA is a PP2C phosphatase
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme PrpC is a PP2C phosphatase
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The enzyme is a PP2C phosphatase
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme PppA is kinase PpkA. Enzyme PppA is a PP2C phosphatase
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physiological function
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the serine/threonine phosphatase DhSIT4 modulates cell cycle, salt tolerance and cell wall integrity in halotolerant yeast Debaryomyces hansenii, role of DhSIT4 in cell wall integrity (CWI) signaling pathway in Debaryomyces hansenii
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme All1758 is a PP2C phosphatase involved in diazotrophic growth, cell morphology, and glycolipid synthesis
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme PppA is kinase PpkA. Enzyme PppA is a PP2C phosphatase
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme PppA is kinase PpkA. Enzyme PppA is a PP2C phosphatase
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme PstP is kinase PknB. Enzyme PstP is a PPM phosphatase
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physiological function
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serine/threonine protein phosphatase PstP of Mycobacterium tuberculosis is necessary for accurate cell division and survival of pathogen, role for PstP in regulating cell division events. The activity of PstP is essential for mycobacterial growth. All of the enzyme domains, including the extracellular domain, are necessary for enzyme activity in vivo. The catalytic activity of PstP is absolutely essential for the in vitro growth
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme All1758 is a PP2C phosphatase involved in diazotrophic growth, cell morphology, and glycolipid synthesis
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physiological function
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SP-PTP is a secretory protein tyrosine phosphatase and plays a crucial role in group A Streptococcus (GAS) growth. As a group A Streptococcus, Streptococcus pyogenes is a human pathogen that causes high morbidity and mortality. It lacks a gene encoding tyrosine kinase but contains one encoding tyrosine phosphatase (SP-PTP). Enzymatically active SP-PTP plays a crucial role in cell division, the function of SP-PTP is physiologically relevant for GAS growth and cell division. SP-PTP is essential for GAS virulence
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physiological function
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the Escherichia coli eSTP acts to dephosphorylate another Ser/Thr kinase that is encoded in the same operon. Regulatory reversible protein phosphorylation is a conserved mechanism of signaling in all biological systems
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme SP-STP is kinase SP-STK. The enzyme is a PP2C phosphatase
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physiological function
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the serine/threonine phosphatase DhSIT4 modulates cell cycle, salt tolerance and cell wall integrity in halotolerant yeast Debaryomyces hansenii, role of DhSIT4 in cell wall integrity (CWI) signaling pathway in Debaryomyces hansenii
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme PrpC is a PP2C phosphatase
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme MG_207 is kinase MG_109. Enzyme MG_207 is a PPM phosphatase involved in cell signaling and virulence
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The enzyme is a PP2C phosphatase
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physiological function
Streptococcus pneumoniae serotype 4 Rx1
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enzyme PhpP and StkP cooperatively regulate cell division of Streptococcus pneumoniae and phosphorylate putative RNA binding protein Jag
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme PppA is kinase PpkA. Enzyme PppA is a PP2C phosphatase
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physiological function
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reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme PrpC is a PP2C phosphatase
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physiological function
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the serine/threonine phosphatase DhSIT4 modulates cell cycle, salt tolerance and cell wall integrity in halotolerant yeast Debaryomyces hansenii, role of DhSIT4 in cell wall integrity (CWI) signaling pathway in Debaryomyces hansenii
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physiological function
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enzyme PhpP and StkP cooperatively regulate cell division of Streptococcus pneumoniae and phosphorylate putative RNA binding protein Jag
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physiological function
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the serine/threonine phosphatase DhSIT4 modulates cell cycle, salt tolerance and cell wall integrity in halotolerant yeast Debaryomyces hansenii, role of DhSIT4 in cell wall integrity (CWI) signaling pathway in Debaryomyces hansenii
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physiological function
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TbALPH1 has all features required of an mRNA decapping enzyme. In vitro experiments confirm that ALPH1 can sensitise a capped RNA to Xrn1 in the presence of an RNA 5' polyphosphatase. ALPH1 has an essential role in trypanosome mRNA metabolism. The trypanosome ApaH-like phosphatase ALPH1 has all characteristics of an mRNA decapping enzyme. The enzyme is essential and localises to P-bodies
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additional information
calcineurin comprises a catalytic A or CNA subunit (PPP3C A/B/C isoforms), which interacts with calmodulin in a calcium-dependent fashion, and a regulatory B or CNB subunit (PPP3R 1/2 isoforms), which contains four calcium-binding domains. The subunits act in concert to regulate calcineurin activity
additional information
calcineurin comprises a catalytic A or CNA subunit (PPP3C A/B/C isoforms), which interacts with calmodulin in a calcium-dependent fashion, and a regulatory B or CNB subunit (PPP3R 1/2 isoforms), which contains four calcium-binding domains. The subunits act in concert to regulate calcineurin activity
additional information
calcineurin comprises a catalytic A or CNA subunit (PPP3C A/B/C isoforms), which interacts with calmodulin in a calcium-dependent fashion, and a regulatory B or CNB subunit (PPP3R 1/2 isoforms), which contains four calcium-binding domains. The subunits act in concert to regulate calcineurin activity
additional information
Streptococcus pneumoniae serotype 4
conserved residues D192 and D231 are essential for PhpP activity in vivo
additional information
detection of the PfPP1 interactome and PP1 interacting proteins (Pips) by mass spectrometry, yeast two-hybrid screening, and in silico analysis of the Plasmodium falciparum predicted proteome. The Pips include a large range of proteins, overview
additional information
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detection of the PfPP1 interactome and PP1 interacting proteins (Pips) by mass spectrometry, yeast two-hybrid screening, and in silico analysis of the Plasmodium falciparum predicted proteome. The Pips include a large range of proteins, overview
additional information
functional PP1 enzymes classically consist of a complex between the catalytic C subunit (PP1c or PPP1C, four isoforms) and one or more regulators (R or PPP1R). PP1-binding domains allow a single PP1c subunit to recruit more than one regulator, using what is described as a molecular-lego strategy. There is especially an incredible diversity of PP1-interacting proteins in the brain. The nearly 200 vertebrate PP1-interacting proteins identified so far show preferential docking to individual PP1 isoforms, thereby supporting PP1 functional specificity and diversity
additional information
functional PP1 enzymes classically consist of a complex between the catalytic C subunit (PP1c or PPP1C, four isoforms) and one or more regulators (R or PPP1R). PP1-binding domains allow a single PP1c subunit to recruit more than one regulator, using what is described as a molecular-lego strategy. There is especially an incredible diversity of PP1-interacting proteins in the brain. The nearly 200 vertebrate PP1-interacting proteins identified so far show preferential docking to individual PP1 isoforms, thereby supporting PP1 functional specificity and diversity
additional information
functional PP1 enzymes classically consist of a complex between the catalytic C subunit (PP1c or PPP1C, four isoforms) and one or more regulators (R or PPP1R). PP1-binding domains allow a single PP1c subunit to recruit more than one regulator, using what is described as a molecular-lego strategy. There is especially an incredible diversity of PP1-interacting proteins in the brain. The nearly 200 vertebrate PP1-interacting proteins identified so far show preferential docking to individual PP1 isoforms, thereby supporting PP1 functional specificity and diversity
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heterogeneous expression of regulatory subunit IbPP2A1 does not enhance abiotic stress tolerance in recombinant Saccharomyces cerevisiae
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phosphatases do not alter the transition state for phosphoryl transfer
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PP2A is a trimeric holoenzyme containing a scaffold subunit (PP2A-A), a catalytic subunit (PP2A-C), and a regulatory B subunit. Four B subunit families have been described: B (B55/PR55), B0 (B56/PR61), B00 (PR48/72/ 130) and B000 (PR93/110). The type of B subunit bound to the PP2A dimer determines both the substrate specificity and the cellular localization of the PP2A holoenzyme complex
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structure of the catalytic domain of Mycobacterium tuberculosis STP PstP, overview
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the conserved residues involved in PP2C third metal ion-binding site are also involved in PrpC catalysis, and the metal binding also contributes to the protein overall structural stability. Homology modeling and analysis of the three-dimensional structure of PrpC using the structure of Streptococcus agalactiae serine/threonine phosphatase as template, PDB ID 2PK0, overview
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the conserved residues involved in PP2C third metal ion-binding site are also involved in PrpC catalysis, and the metal binding also contributes to the protein overall structural stability. Homology modeling and analysis of the three-dimensional structure of PrpC using the structure of Streptococcus agalactiae serine/threonine phosphatase as template, PDB ID 2PK0, overview
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the typical mammalian PP2A enzyme exists as a heterotrimer of a scaffolding A subunit (PPP2R1 A/B isoforms), a catalytic C subunit (PP2Ac or PPP2C A/B isoforms) and one of 23 regulatory B-type subunits belonging to one of 4 distinct families: B (PPP2R), B' (PPP2R5), B'' (PPP2R3) or B'''/striatins (PPP2R4). B, B' and B'' families each comprise several isoforms (named A, B, C etc. or alpha, beta, gamma etc.). Other atypical regulatory subunits, such as alpha4, can also associate with PP2Ac. PP2A activity is also regulated by many cellular regulators and natural inhibitors, such as okadaic acid. These commonly used inhibitors not only inhibit all PP2A isoforms, but also other Ser/Thr phosphatases, including PP1 and other PPP family members, at the concentrations needed to completely abrogate cellular PP2A activity
additional information
the typical mammalian PP2A enzyme exists as a heterotrimer of a scaffolding A subunit (PPP2R1 A/B isoforms), a catalytic C subunit (PP2Ac or PPP2C A/B isoforms) and one of 23 regulatory B-type subunits belonging to one of 4 distinct families: B (PPP2R), B' (PPP2R5), B'' (PPP2R3) or B'''/striatins (PPP2R4). B, B' and B'' families each comprise several isoforms (named A, B, C etc. or alpha, beta, gamma etc.). Other atypical regulatory subunits, such as alpha4, can also associate with PP2Ac. PP2A activity is also regulated by many cellular regulators and natural inhibitors, such as okadaic acid. These commonly used inhibitors not only inhibit all PP2A isoforms, but also other Ser/Thr phosphatases, including PP1 and other PPP family members, at the concentrations needed to completely abrogate cellular PP2A activity
additional information
the typical mammalian PP2A enzyme exists as a heterotrimer of a scaffolding A subunit (PPP2R1 A/B isoforms), a catalytic C subunit (PP2Ac or PPP2C A/B isoforms) and one of 23 regulatory B-type subunits belonging to one of 4 distinct families: B (PPP2R), B' (PPP2R5), B'' (PPP2R3) or B'''/striatins (PPP2R4). B, B' and B'' families each comprise several isoforms (named A, B, C etc. or alpha, beta, gamma etc.). Other atypical regulatory subunits, such as alpha4, can also associate with PP2Ac. PP2A activity is also regulated by many cellular regulators and natural inhibitors, such as okadaic acid. These commonly used inhibitors not only inhibit all PP2A isoforms, but also other Ser/Thr phosphatases, including PP1 and other PPP family members, at the concentrations needed to completely abrogate cellular PP2A activity
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the widened Z1-helix binding pocket results in the second significant structural difference between PPZ1cat and PP1alpha: the C-terminal residues of PPZ1cat are not disordered like they are in PP1alpha, but instead form an alpha-helix that nestles into this widened Z1-helix binding pocket. This interaction is stabilized by hydrophobic interactions between the C-terminal helix and residues from helices A' and B, with the interaction centered on PPZ1 C-terminal helix residue Met473PPZ1. This residue is completely buried from solvent via interactions with Leu464PPZ1, Leu469PPZ1, and Val472PPZ1 from the C-terminal helix as well as by interactions with Phe185PPZ1 from helix A' and His235PPZ1, Ile238PPZ1, and Arg239PPZ1 from helix B. The PPZ1-specific helix is dynamic. PPZ1 binds only a subset of PP1 regulatory proteins
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the widened Z1-helix binding pocket results in the second significant structural difference between PPZ1cat and PP1alpha: the C-terminal residues of PPZ1cat are not disordered like they are in PP1alpha, but instead form an alpha-helix that nestles into this widened Z1-helix binding pocket. This interaction is stabilized by hydrophobic interactions between the C-terminal helix and residues from helices A' and B, with the interaction centered on PPZ1 C-terminal helix residue Met473PPZ1. This residue is completely buried from solvent via interactions with Leu464PPZ1, Leu469PPZ1, and Val472PPZ1 from the C-terminal helix as well as by interactions with Phe185PPZ1 from helix A' and His235PPZ1, Ile238PPZ1, and Arg239PPZ1 from helix B. The PPZ1-specific helix is dynamic. PPZ1 binds only a subset of PP1 regulatory proteins
additional information
Tk-PTP adopts a common dual-specificity phosphatase (DUSP) fold, but it undergoes an atypical temperature-dependent conformational change in its P-loop and alpha4-alpha5 loop regions, switching between the inactive and active forms. Tk-PTP contains a PTP signature motif HCxxGxxR, HC93MGGLGR99 in Tk-PTP constituting the phosphate binding loop (or simply called P-loop), contains the catalytic cysteine residue (Cys93) that functions as a nucleophile for dephosphorylation and the conserved arginine residue (Arg99) that anchors the phosphate group of the substrate during the enzyme reaction. Tk-PTP contains dual general acid/base residues, Asp63 or Glu132. Structural analysis of the conformation of the P-loop in of Tk-PTP(form I), structure comparisons of PTPs, structure-function analysis of the two enzyme forms, overview. Molecular dynamics simulations
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transcriptomic analysis
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transcriptomic analysis
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transcriptomic analysis
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transcriptomic analysis
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Tk-PTP adopts a common dual-specificity phosphatase (DUSP) fold, but it undergoes an atypical temperature-dependent conformational change in its P-loop and alpha4-alpha5 loop regions, switching between the inactive and active forms. Tk-PTP contains a PTP signature motif HCxxGxxR, HC93MGGLGR99 in Tk-PTP constituting the phosphate binding loop (or simply called P-loop), contains the catalytic cysteine residue (Cys93) that functions as a nucleophile for dephosphorylation and the conserved arginine residue (Arg99) that anchors the phosphate group of the substrate during the enzyme reaction. Tk-PTP contains dual general acid/base residues, Asp63 or Glu132. Structural analysis of the conformation of the P-loop in of Tk-PTP(form I), structure comparisons of PTPs, structure-function analysis of the two enzyme forms, overview. Molecular dynamics simulations
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conserved residues D192 and D231 are essential for PhpP activity in vivo
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structure of the catalytic domain of Mycobacterium tuberculosis STP PstP, overview
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additional information
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Tk-PTP adopts a common dual-specificity phosphatase (DUSP) fold, but it undergoes an atypical temperature-dependent conformational change in its P-loop and alpha4-alpha5 loop regions, switching between the inactive and active forms. Tk-PTP contains a PTP signature motif HCxxGxxR, HC93MGGLGR99 in Tk-PTP constituting the phosphate binding loop (or simply called P-loop), contains the catalytic cysteine residue (Cys93) that functions as a nucleophile for dephosphorylation and the conserved arginine residue (Arg99) that anchors the phosphate group of the substrate during the enzyme reaction. Tk-PTP contains dual general acid/base residues, Asp63 or Glu132. Structural analysis of the conformation of the P-loop in of Tk-PTP(form I), structure comparisons of PTPs, structure-function analysis of the two enzyme forms, overview. Molecular dynamics simulations
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additional information
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the conserved residues involved in PP2C third metal ion-binding site are also involved in PrpC catalysis, and the metal binding also contributes to the protein overall structural stability. Homology modeling and analysis of the three-dimensional structure of PrpC using the structure of Streptococcus agalactiae serine/threonine phosphatase as template, PDB ID 2PK0, overview
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additional information
Streptococcus pneumoniae serotype 4 Rx1
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conserved residues D192 and D231 are essential for PhpP activity in vivo
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additional information
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conserved residues D192 and D231 are essential for PhpP activity in vivo
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