| + |
PPME1 | down-regulates activity 
demethylation
|
PPP2CB |
0.724 |
| 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 |
0.676 |
| 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 |
0.271 |
| 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 |
0.256 |
| 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 |
0.285 |
| 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 |
0.266 |
| 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 |
0.263 |
| 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 |
0.46 |
| 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 |
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4.0
PPP2CB
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