| + |
PPME1 | down-regulates activity 
demethylation
|
PPP2CB |
0.698 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265750 |
Leu309 |
RRTPDYFl |
in vitro |
|
| pmid |
sentence |
| 18394995 |
Methylation of the carboxy-terminal Leu309 in a conserved TPDYFL309 motif of the C subunit has been shown to enhance the affinity of the PP2A core enzyme for some, but not all, regulatory subunits |Demethylation and negative regulation of PP2A is mediated by a PP2A-specific methylesterase PME-1, which is conserved from yeast to humans. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
LCMT1 | up-regulates activity 
methylation
|
PPP2CB |
0.645 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265751 |
Leu309 |
RRTPDYFl |
in vitro |
|
| pmid |
sentence |
| 18394995 |
Methylation of the carboxy-terminal Leu309 in a conserved TPDYFL309 motif of the C subunit has been shown to enhance the affinity of the PP2A core enzyme for some, but not all, regulatory subunits |The PP2A core enzyme was methylated by a PP2A-specific leucine carboxyl methyltransferase (LCMT1) |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
SNCA |
0.278 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248592 |
Ser129 |
NEAYEMPsEEGYQDY |
Homo sapiens |
|
| pmid |
sentence |
| 21562258 |
α-Synuclein (α-Syn) is a key protein that accumulates as hyperphosphorylated aggregates in pathologic hallmark features of Parkinson's disease (PD) and other neurodegenerative disorders. Phosphorylation of this protein at serine 129 is believed to promote its aggregation and neurotoxicity, suggesting that this post-translational modification could be a therapeutic target. Here, we demonstrate that phosphoprotein phosphatase 2A (PP2A) dephosphorylates α-Syn at serine 129 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | up-regulates activity
dephosphorylation
|
HDAC7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248603 |
Ser155 |
FPLRKTVsEPNLKLR |
Homo sapiens |
|
| pmid |
sentence |
| 18339811 |
Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. |Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248604 |
Ser181 |
NPLLRKEsAPPSLRR |
Homo sapiens |
|
| pmid |
sentence |
| 18339811 |
Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. |Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248605 |
Ser358 |
WPLSRTRsEPLPPSA |
Homo sapiens |
|
| pmid |
sentence |
| 18339811 |
Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. |Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248606 |
Ser486 |
RPLSRAQsSPAAPAS |
Homo sapiens |
|
| pmid |
sentence |
| 18339811 |
Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. |Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
IKBKB |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248581 |
Ser177 |
AKELDQGsLCTSFVG |
Homo sapiens |
Carcinoma Cell |
| pmid |
sentence |
| 19607706 |
Permanent activation of the upstream kinase IKK beta results from UVB-induced inhibition of the catalytic subunit of Ser-Thr phosphatase PP2A (PP2Ac), leading to immediate phosphorylation and degradation of newly synthesized I kappaB alpha|Chronic Ser 177/181 phosphorylation of IKKβ was due to UVB-induced inhibition of the catalytic subunit of the Ser-Thr phosphatase PP2A (PP2Ac) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248580 |
Ser181 |
DQGSLCTsFVGTLQY |
Homo sapiens |
|
| pmid |
sentence |
| 19607706 |
Permanent activation of the upstream kinase IKK beta results from UVB-induced inhibition of the catalytic subunit of Ser-Thr phosphatase PP2A (PP2Ac), leading to immediate phosphorylation and degradation of newly synthesized I kappaB alpha|Chronic Ser 177/181 phosphorylation of IKKβ was due to UVB-induced inhibition of the catalytic subunit of the Ser-Thr phosphatase PP2A (PP2Ac) |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | down-regulates
dephosphorylation
|
RALA |
0.294 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-155349 |
Ser183 |
RARKMEDsKEKNGKK |
Homo sapiens |
|
| pmid |
sentence |
| 17540176 |
Pp2a abeta-containing complexes dephosphorylate rala at ser183 and ser194, inactivating rala and abolishing its transforming function |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-155353 |
Ser194 |
NGKKKRKsLAKRIRE |
Homo sapiens |
|
| pmid |
sentence |
| 17540176 |
Pp2a abeta-containing complexes dephosphorylate rala at ser183 and ser194, inactivating rala and abolishing its transforming function |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
ATM |
0.273 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248601 |
Ser1981 |
SLAFEEGsQSTTISS |
Homo sapiens |
|
| pmid |
sentence |
| 15510216 |
Ionizing radiation induces autophosphorylation of the ataxia-telangiectasia mutated (ATM) protein kinase on serine 1981; however, the precise mechanisms that regulate ATM activation are not fully understood. Here, we show that the protein phosphatase inhibitor okadaic acid (OA) induces autophosphorylation of ATM on serine 1981 in unirradiated cells at concentrations that inhibit protein phosphatase 2A-like activity in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
PAK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248599 |
Ser199 |
PRPEHTKsVYTRSVI |
Rattus norvegicus |
|
| pmid |
sentence |
| 18586681 |
Both sites were dephosphorylated with the same kinetics; the anti-Ser(P)198 antibody was subsequently used as it exhibited lower background staining. Direct comparison of PP2Cα with purified PP1 and PP2A lead us to conclude that at the same molar ratio PP2Cα was the most efficient in dephosphorylating PAK1 (Fig. 1D). In this case we monitored two autophosphorylation sites in the Pak1 N-terminal regulatory region (Ser57 and Ser198/203) using phosphospecific antibodies: both sites showed the same kinetics of inactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248598 |
Ser57 |
KKDRFYRsILPGDKT |
Rattus norvegicus |
|
| pmid |
sentence |
| 18586681 |
Both sites were dephosphorylated with the same kinetics; the anti-Ser(P)198 antibody was subsequently used as it exhibited lower background staining. Direct comparison of PP2Cα with purified PP1 and PP2A lead us to conclude that at the same molar ratio PP2Cα was the most efficient in dephosphorylating PAK1 (Fig. 1D). In this case we monitored two autophosphorylation sites in the Pak1 N-terminal regulatory region (Ser57 and Ser198/203) using phosphospecific antibodies: both sites showed the same kinetics of inactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248600 |
Thr423 |
PEQSKRStMVGTPYW |
Rattus norvegicus |
|
| pmid |
sentence |
| 18586681 |
Both sites were dephosphorylated with the same kinetics; the anti-Ser(P)198 antibody was subsequently used as it exhibited lower background staining. Direct comparison of PP2Cα with purified PP1 and PP2A lead us to conclude that at the same molar ratio PP2Cα was the most efficient in dephosphorylating PAK1 (Fig. 1D). In this case we monitored two autophosphorylation sites in the Pak1 N-terminal regulatory region (Ser57 and Ser198/203) using phosphospecific antibodies: both sites showed the same kinetics of inactivation. |
|
| Publications: |
3 |
Organism: |
Rattus Norvegicus |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
CHEK1 |
0.269 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248579 |
Ser317 |
ENVKYSSsQPEPRTG |
Homo sapiens |
|
| pmid |
sentence |
| 17015476 |
Phosphorylation of Chk1 by ATR is antagonized by a Chk1-regulated protein phosphatase 2A circuit|In response to genotoxic stress, Chk1 is phosphorylated on serines 317 (S317) and 345 (S345) by the ataxia-telangiectasia-related (ATR) protein kinase. Phosphorylation of Chk1 on these C-terminal serine residues is used as an indicator of Chk1 activation in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248578 |
Ser345 |
LVQGISFsQPTCPDH |
Homo sapiens |
|
| pmid |
sentence |
| 17015476 |
Phosphorylation of Chk1 by ATR is antagonized by a Chk1-regulated protein phosphatase 2A circuit|In response to genotoxic stress, Chk1 is phosphorylated on serines 317 (S317) and 345 (S345) by the ataxia-telangiectasia-related (ATR) protein kinase. Phosphorylation of Chk1 on these C-terminal serine residues is used as an indicator of Chk1 activation in vivo. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | up-regulates quantity by stabilization
dephosphorylation
|
TP53 |
0.407 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248584 |
Ser37 |
NVLSPLPsQAMDDLM |
Homo sapiens |
|
| pmid |
sentence |
| 14712210 |
Phosphorylation of p53 at serine 37 is important for transcriptional activity and regulation in response to DNA damage| Furthermore, in vitro phosphatase assays show that PP2A dephosphorylates p53 at S37. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248583 |
Thr55 |
DDIEQWFtEDPGPDE |
Homo sapiens |
|
| pmid |
sentence |
| 17245430 |
A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-induced dephosphorylation of p53 at Thr55| In this study, we reported that the specific B regulatory subunits of PP2A B56gamma1 and B56gamma3 mediate dephosphorylation of p53 at Thr55. Ablation of the B56gamma protein by RNAi, which abolishes the Thr55 dephosphorylation in response to DNA damage, reduces p53 stabilization, Bax expression and cell apoptosis |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PPP2CB |
dephosphorylation
|
KRT8 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248588 |
Ser432 |
SAYGGLTsPGLSYSL |
Homo sapiens |
HT-29 Cell |
| pmid |
sentence |
| 16554440 |
K8 Ser431-P is a physiologic substrate to PP2A during hyposmotic conditions and possibly other biologic contexts. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
AKT3 |
0.468 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248610 |
Ser472 |
RPHFPQFsYSASGRE |
Homo sapiens |
|
| pmid |
sentence |
| 18160256 |
Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248609 |
Ser474 |
HFPQFSYsASGRE |
Homo sapiens |
|
| pmid |
sentence |
| 18160256 |
Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248611 |
Thr305 |
TDAATMKtFCGTPEY |
Homo sapiens |
|
| pmid |
sentence |
| 18160256 |
Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248612 |
Thr309 |
TMKTFCGtPEYLAPE |
Homo sapiens |
|
| pmid |
sentence |
| 18160256 |
Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | down-regulates
dephosphorylation
|
MYC |
0.281 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149726 |
Ser62 |
LLPTPPLsPSRRSGL |
Homo sapiens |
|
| pmid |
sentence |
| 16987807 |
Phosphorylation at ser-62 by pro-directed kinases (p-k) is a prerequisite for gsk3-dependent phosphorylation of thr-58. This triggers binding of pin1, subsequently protein phosphatase 2a (pp2a)-dependent dephosphorylation of ser-62, and then recruitment of scf-fbw7 to the thr-58-phosphorylated myc. Scf-fbw7 polyubiquitinylates myc (branching through lys-48), leading to its proteasomal degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
CARD11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248607 |
Ser644 |
NLMFRKFsLERPFRP |
Homo sapiens |
|
| pmid |
sentence |
| 21157432 |
NF-kappaB activation is triggered by PKCtheta-dependent phosphorylation of Carma1 after TCR/CD28 co-stimulation. PKCtheta-phosphorylated Carma1 was suggested to function as a molecular scaffold that recruits preassembled Bcl10-Malt1 complexes to the membrane|we demonstrate that PP2A removes PKCtheta-dependent phosphorylation of Ser645 in Carma1, and show that maintenance of this phosphorylation is correlated with increased T-cell activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
PRKCD |
0.305 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248595 |
Ser645 |
LNEKARLsYSDKNLI |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 11959144 |
PP2A(c) displayed the highest specific activity towards PKCdelta. The role of PP2A(c) in the dephosphorylation of PKCdelta in cells was supported by the demonstration that these proteins could be co-immunoprecipitated from NIH3T3 cells.|In conclusion, the evidence here indicates that PKCdelta de-phosphorylation and hence inactivation is effected by PP2A with which it forms a complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248596 |
Ser664 |
QSAFAGFsFVNPKFE |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 11959144 |
PP2A(c) displayed the highest specific activity towards PKCdelta. The role of PP2A(c) in the dephosphorylation of PKCdelta in cells was supported by the demonstration that these proteins could be co-immunoprecipitated from NIH3T3 cells.|In conclusion, the evidence here indicates that PKCdelta de-phosphorylation and hence inactivation is effected by PP2A with which it forms a complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248594 |
Thr507 |
FGESRAStFCGTPDY |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 11959144 |
PP2A(c) displayed the highest specific activity towards PKCdelta. The role of PP2A(c) in the dephosphorylation of PKCdelta in cells was supported by the demonstration that these proteins could be co-immunoprecipitated from NIH3T3 cells.|In conclusion, the evidence here indicates that PKCdelta de-phosphorylation and hence inactivation is effected by PP2A with which it forms a complex |
|
| Publications: |
3 |
Organism: |
Mus Musculus |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
PRKCB (isoform 2) |
0.452 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248586 |
Ser660 |
QSEFEGFsFVNSEFL |
Rattus norvegicus |
|
| pmid |
sentence |
| 15880462 |
Inhibition of PP2A increased phosphorylation at Ser660 that determines calcium sensitivity and activity of PKCbetaII isoform |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248587 |
Thr641 |
TRHPPVLtPPDQEVI |
Rattus norvegicus |
|
| pmid |
sentence |
| 8749392 |
Specifically, the threonine at position 500 (T500) on the activation loop, and T641 and S660 on the carboxyl terminus of protein kinase C beta II are phosphorylated in vivo. T500 and S660 are selectively dephosphorylated in vitro by protein phosphatase 2A to yield an enzyme that is still capable of lipid-dependent activation, whereas all three residues are dephosphorylated by protein phosphatase 1 to yield an inactive enzyme. |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
PPP2CB |
dephosphorylation
|
PPP1R1A |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248602 |
Ser67 |
LKSTLAMsPRQRKKM |
Rattus norvegicus |
|
| pmid |
sentence |
| 11278334 |
In vitro and in vivo studies indicated that phospho-Ser-67 inhibitor-1 was dephosphorylated by protein phosphatases-2A and -2B. | However, inhibitor-1 phosphorylated at Ser-67 was a less efficient substrate for cAMP-dependent protein kinase. These results demonstrate regulation of a Cdk5-dependent phosphorylation site in inhibitor-1 and suggest a role for this site in modulating the amplitude of signal transduction events that involve cAMP-dependent protein kinase activation. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PPP2CB | up-regulates activity
dephosphorylation
|
BCL2 |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248589 |
Ser87 |
AAAGPALsPVPPVVH |
Homo sapiens |
|
| pmid |
sentence |
| 15225643 |
The phosphorylation of Bcl-2 resulted in a reduction in anti-apoptotic function, implying that dephosphorylation promoted the anti-apoptotic activity of Bcl-2 protein in human tumor cell lines. Thus, the present findings suggest that ERK and PP2A are physiological regulators of Bcl-2 phosphorylation, and these enzymes exert an influence on the anti-apoptotic function of Bcl-2.phosphorylation of Bcl2 at Ser70 is proposed to be a dynamic process regulated by the sequential action of an agonist-activated Bcl2 kinase and PP2A. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
TRAF2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248597 |
Thr117 |
DGCTWKGtLKEYESC |
Mus musculus |
|
| pmid |
sentence |
| 17188031 |
We show that the Thr117 residue in TRAF2 is phosphorylated following TNFalpha stimulation. This phosphorylation process is modulated by PP2A and is required for TRAF2 functional activity. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
MAPK1 |
0.451 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248590 |
Thr185 |
HDHTGFLtEYVATRW |
Rattus norvegicus |
|
| pmid |
sentence |
| 7780739 |
Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100, in various cell lines|Protein phosphatase-2A was the only vanadate-insensitive phosphatase acting on Thr 183 of p42mapk or on MAPKK to be detected in PC12 cell extracts. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PPP2CB | up-regulates
dephosphorylation
|
MDM2 |
0.369 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-86736 |
Thr216 |
RSSSSEStGTPSNPD |
Homo sapiens |
|
| pmid |
sentence |
| 11983168 |
Cyclin g also binds in vivo and in vitro to mdm2 and markedly stimulates the ability of pp2a to dephosphorylate mdm2 at t216. Our data imply that the function of cyclin g is to serve as a negative regulator of p53 by activating mdm2 through dephosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | up-regulates activity
dephosphorylation
|
MDM2 |
0.369 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248593 |
Thr216 |
RSSSSEStGTPSNPD |
Mus musculus |
|
| pmid |
sentence |
| 11983168 |
cyclin G also binds in vivo and in vitro to Mdm2 and markedly stimulates the ability of PP2A to dephosphorylate Mdm2 at T216. Consistent with these data, cyclin G null cells have both Mdm2 that is hyperphosphorylated at T216 and markedly higher levels of p53 protein when compared to wild-type cells |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
ELF1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248591 |
Thr231 |
CPKYIKWtQREKGIF |
Homo sapiens |
|
| pmid |
sentence |
| 18714041 |
Elf-1 enhances the expression of CD3zeta, whereas it suppresses the expression of FcRgamma gene and lupus T cells have decreased amounts of DNA-binding 98 kDa form of Elf-1. We show that the aberrantly increased PP2A in lupus T cells dephosphorylates Elf-1 at Thr-231. Dephosphorylation results in limited expression and binding of the 98 kDa Elf-1 form to the CD3zeta and FcRgamma promoters. Suppression of the expression of the PP2A leads to increased expression of CD3zeta and decreased expression of FcRgamma genes and correction of the early signaling response |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
PRKCB |
0.452 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248585 |
Thr500 |
WDGVTTKtFCGTPDY |
Rattus norvegicus |
|
| pmid |
sentence |
| 8749392 |
Specifically, the threonine at position 500 (T500) on the activation loop, and T641 and S660 on the carboxyl terminus of protein kinase C beta II are phosphorylated in vivo. T500 and S660 are selectively dephosphorylated in vitro by protein phosphatase 2A to yield an enzyme that is still capable of lipid-dependent activation, whereas all three residues are dephosphorylated by protein phosphatase 1 to yield an inactive enzyme. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PPP2CB | up-regulates activity
dephosphorylation
|
CHEK2 |
0.314 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248582 |
Thr68 |
SSLETVStQELYSIP |
Homo sapiens |
|
| pmid |
sentence |
| 16596250 |
Protein phosphatase 2A interacts with Chk2 and regulates phosphorylation at Thr-68 after cisplatin treatment of human ovarian cancer cells|In response to DNA damage, Chk2 is initially phosphorylated at Thr-68, which leads to its full activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2R1A | up-regulates
binding
|
PPP2CB |
0.884 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138886 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16039140 |
Pr65/a acts as a scaffold protein for binding pp2ac and regulatory b subunits in a heterotrimeric holoenzyme |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
AKT |
0.483 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248614 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18160256 |
Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | down-regulates
dephosphorylation
|
AKT |
0.483 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-42050 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8650155 |
These results confirm that the activity changes observed are achieved by a reversible phosphorylation mechanism, and also argue that pp2a may negatively regulate rac-pk activity in vivo. Dephosphorylation of the activated rac-pk in itro by pp2ac resulted in an 87% reduction of kinase activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AMBRA1 | up-regulates activity
binding
|
PPP2CB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272964 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25438055 |
We found that AMBRA1 favours the interaction between c-Myc and its phosphatase PP2A and that, when mTOR is inhibited, it enhances PP2A activity on this specific target, thereby reducing the cell division rate. As expected, such a de-regulation of c-Myc correlates with increased tumorigenesis in AMBRA1-defective systems, thus supporting a role for AMBRA1 as a haploinsufficient tumour suppressor gene. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STRN4 | up-regulates activity
binding
|
PPP2CB |
0.607 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261699 |
|
|
Mus musculus |
Neuron |
| pmid |
sentence |
| 29802198 |
The striatin family proteins interact with the structural (A) and catalytic (C) subunits of the protein phosphatase, PP2A, and are also termed the B‴ family of PP2A subunits (4). Within heterotrimeric PP2A complexes, striatins function as one of many regulatory B subunits thought to be responsible for substrate selection and localization of PP2A isoforms |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SET | down-regulates
binding
|
PPP2CB |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-175722 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21806989 |
Here we report that both the amino terminal fragment (i(2ntf);aa 1-175) and the carboxy terminal fragment (i(2ctf);aa 176-277) of i(2)(pp2a) inhibit pp2a by binding to its catalytic subunit pp2ac |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STRN | up-regulates activity
binding
|
PPP2CB |
0.614 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261700 |
|
|
Mus musculus |
Neuron |
| pmid |
sentence |
| 29802198 |
The striatin family proteins interact with the structural (A) and catalytic (C) subunits of the protein phosphatase, PP2A, and are also termed the B‴ family of PP2A subunits (4). Within heterotrimeric PP2A complexes, striatins function as one of many regulatory B subunits thought to be responsible for substrate selection and localization of PP2A isoforms |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PPP2CB | down-regulates
dephosphorylation
|
AKT1 |
0.483 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252636 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8650155 |
These results confirm that the activity changes observed are achieved by a reversible phosphorylation mechanism, and also argue that pp2a may negatively regulate rac-pk activity in vivo. Dephosphorylation of the activated rac-pk in itro by pp2ac resulted in an 87% reduction of kinase activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | down-regulates
dephosphorylation
|
AKT2 |
0.453 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-42123 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8650155 |
These results confirm that the activity changes observed are achieved by a reversible phosphorylation mechanism, and also argue that pp2a may negatively regulate rac-pk activity in vivo. Dephosphorylation of the activated rac-pk in itro by pp2ac resulted in an 87% reduction of kinase activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLAAT3 | down-regulates 
|
PPP2CB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153775 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17374643 |
The alpha-isoform of the regulatory subunit a of protein phosphatase 2a (pr65alpha) as a new interaction partner of hrsl3 / we demonstrate that hrsl3 binds to the endogenous pr65alpha, thereby partially sequestering the catalytic subunit pr36 from the pr65 protein complex, and inhibiting pp2a catalytic activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TLX1 | down-regulates activity
binding
|
PPP2CB |
0.304 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240722 |
|
|
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 15897879 |
HOX11 also inhibited PP2A serine/threonine phosphatase activity concomitant with stimulation of the AKT/PKB signaling cascade. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PPP2CB
- 
- 