| + |
PPP1CB | down-regulates activity 
dephosphorylation
|
TP53 |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248572 |
Ser15 |
PSVEPPLsQETFSDL |
Homo sapiens |
|
| pmid |
sentence |
| 16501611 |
Protein serine/threonine phosphatase-1 dephosphorylates p53 at Ser-15 and Ser-37 to modulate its transcriptional and apoptotic activities|In addition, our results reveal that one of the molecular mechanisms by which PP-1 promotes cell survival is to dephosphorylate p53, and thus negatively regulate p53-dependent death pathway. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248573 |
Ser37 |
NVLSPLPsQAMDDLM |
Homo sapiens |
|
| pmid |
sentence |
| 16501611 |
Protein serine/threonine phosphatase-1 dephosphorylates p53 at Ser-15 and Ser-37 to modulate its transcriptional and apoptotic activities|In addition, our results reveal that one of the molecular mechanisms by which PP-1 promotes cell survival is to dephosphorylate p53, and thus negatively regulate p53-dependent death pathway. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PPP1CB | up-regulates activity 
dephosphorylation
|
CASP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248576 |
Ser164 |
STDTVEHsLDNKDGP |
in vitro |
|
| pmid |
sentence |
| 19531356 |
Nutrient-replete oocytes inhibit C2 via S135 phosphorylation catalyzed by calcium/calmodulin-dependent protein kinase II. We now show that C2 phosphorylated at S135 binds 14-3-3zeta, thus preventing C2 dephosphorylation. Moreover, we determined that S135 dephosphorylation is catalyzed by protein phosphatase-1 (PP1), which directly binds C2. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PPP1CB | down-regulates activity
dephosphorylation
|
AXIN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248569 |
Ser217 |
YTRTGSEsPKVCSDQ |
Homo sapiens |
|
| pmid |
sentence |
| 17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248570 |
Ser469 |
AHEENPEsILDEHVQ |
Homo sapiens |
|
| pmid |
sentence |
| 17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248567 |
Ser75 |
LGYEPEGsASPTPPY |
Homo sapiens |
|
| pmid |
sentence |
| 17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248568 |
Ser77 |
YEPEGSAsPTPPYLK |
Homo sapiens |
|
| pmid |
sentence |
| 17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PPP1CB | up-regulates quantity by stabilization
dephosphorylation
|
MDM2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248577 |
Ser370 |
KKTIVNDsRESCVEE |
Homo sapiens |
|
| pmid |
sentence |
| 23277204 |
Three phosphorylation sites identified are Ser342, Ser367, and Ser403. In the present study, we identify protein phosphatase 1 (PP1) as a negative regulator in the p53 signaling pathway. PP1 directly interacts with Mdmx and specifically dephosphorylates Mdmx at Ser367. The dephosphorylation of Mdmx increases its stability and thereby inhibits p53 activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1CB | down-regulates activity
dephosphorylation
|
AKT |
0.395 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248575 |
Ser473 |
RPHFPQFsYSASGTA |
Homo sapiens |
|
| pmid |
sentence |
| 14633703 |
Here, we identify PP1 as a serine/threonine phosphatase that associates with and dephosphorylates AKT in breast cancer cells|The heat shock protein 90 inhibitor geldanamycin and the ErbB inhibitor ZD1839 promote rapid PP1 phosphatase-dependent inactivation of AKT in ErbB2 overexpressing breast cancer cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1CB | down-regulates activity
dephosphorylation
|
AKT1 |
0.395 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252604 |
Ser473 |
RPHFPQFsYSASGTA |
Homo sapiens |
|
| pmid |
sentence |
| 14633703 |
Here, we identify PP1 as a serine/threonine phosphatase that associates with and dephosphorylates AKT in breast cancer cells|The heat shock protein 90 inhibitor geldanamycin and the ErbB inhibitor ZD1839 promote rapid PP1 phosphatase-dependent inactivation of AKT in ErbB2 overexpressing breast cancer cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1CB | up-regulates
dephosphorylation
|
NF2 |
0.387 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159836 |
Ser518 |
DTDMKRLsMEIEKEK |
Homo sapiens |
|
| pmid |
sentence |
| 18071304 |
When serine 518 is dephosphorylated by the myosin phosphatase mypt-1-pp1?, The tumor suppressor function of merlin is activated, inhibiting the ras signaling pathway and leading to growth arrest |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1CB |
dephosphorylation
|
AHCYL1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248571 |
Ser68 |
RSLSRSIsQSSTDSY |
Mus musculus |
|
| pmid |
sentence |
| 17635105 |
Moreover, IRBIT-associated PP1 specifically dephosphorylated Ser68 of IRBIT. Phosphorylation of Ser68 was required for subsequent phosphorylation of Ser71 and Ser74, but the latter two sites were not targeted by PP1. We found that phosphorylation of Ser71 and Ser74 were sufficient to enable inhibition of IP3 binding to the IP3R|Given the importance of phosphorylation for the function of IRBIT in suppressing IP3R activity [7,10], in the present study, we searched for a protein phosphatase involved in the dephosphorylation and, hence, inactivation of IRBIT. We found that IRBIT contains a specific well-conserved binding site for PP1. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PPP1CB | down-regulates
dephosphorylation
|
AKT1 |
0.395 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163965 |
Thr450 |
TAQMITItPPDQDDS |
Homo sapiens |
|
| pmid |
sentence |
| 20186153 |
Akt activation is achieved through a series of phosphorylation steps, the first being akt phosphorylation at thr-450 by jnk kinases. Pp-1 acts as a major phosphatase to dephosphorylate akt at thr-450 and thus modulate its functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1CB | up-regulates activity
dephosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248574 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
Endothelial Cell |
| pmid |
sentence |
| 19036824 |
The increase in eNOS activity coincided with specific dephosphorylation of eNOS-Thr495, known to enhance eNOS activity. Inhibition of protein phosphatase 1 (PP1) by calyculin A, tautomycetin, or siRNA against PP1 reversed NF-induced eNOS-Thr495 dephosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1CB | up-regulates
dephosphorylation
|
IKZF1 |
0.269 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174862 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21750978 |
Ikarosis dephosphorylated by protein phosphatase 1 (pp1) via interaction at a consensus pp1-binding motif/ hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1R1B | down-regulates activity
binding
|
PPP1CB |
0.422 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264959 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 10604473 |
DARPP-32 (dopamine and cyclic AMP-regulated phospho-protein, relative molecular mass 32,000) is converted into an inhibitor of protein phosphatase 1 when it is phosphorylated by protein kinase A (PKA) at threonine 34.‚ |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1R14A | down-regulates activity
binding
|
PPP1CB |
0.482 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265742 |
|
|
in vitro |
|
| pmid |
sentence |
| 12144526 |
We conclude that ILK may activate smooth-muscle contraction both directly, via phosphorylation of myosin, and indirectly, via phosphorylation and activation of CPI-17 and PHI-1, leading to inhibition of MLCP.|CPI-17 and PHI-1 thiophosphorylated by ILK at Thr(38) or Thr(57) respectively inhibited myosin light-chain phosphatase (MLCP) activity bound to myosin |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PPP1R14B | down-regulates activity
binding
|
PPP1CB |
0.293 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265743 |
|
|
in vitro |
|
| pmid |
sentence |
| 12144526 |
We conclude that ILK may activate smooth-muscle contraction both directly, via phosphorylation of myosin, and indirectly, via phosphorylation and activation of CPI-17 and PHI-1, leading to inhibition of MLCP.|CPI-17 and PHI-1 thiophosphorylated by ILK at Thr(38) or Thr(57) respectively inhibited myosin light-chain phosphatase (MLCP) activity bound to myosin |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
PPP1CB
- 
- 