| + |
PP1 | down-regulates activity
dephosphorylation
|
CAD |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264653 |
Ser1406 |
GAGGRRLsSFVTKGY |
in vitro |
|
| pmid |
sentence |
| 4092695 |
Cyclic AMP-dependent protein kinase phosphorylates two serine residues on the protein termed sites 1 and 2| Site 1: Arg-Leu-Ser(P)-Ser-Phe-Val-Thr-Lys Site 2: Ile-His-Arg-Ala-Ser(P)-Asp-Pro-Gly-Leu-Pro-Ala-Glu-Glu-Pro-Lys | Both phosphorylation and activation can be reversed using purified preparations of the catalytic subunits of protein phosphatases 1- and -2A, and inactivation also correlates better with dephosphorylation of site 1 rather than site 2. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PP1 | down-regulates activity
dephosphorylation
|
TP53 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264670 |
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. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PP1 | down-regulates activity
dephosphorylation
|
PYGM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267402 |
Ser15 |
QEKRKQIsVRGLAGV |
Homo sapiens |
Chang Cell |
| pmid |
sentence |
| 22225877 |
GP is the first protein whose function was discovered to be regulated by reversible protein phosphorylation, which is controlled by phosphorylase kinase (PhK) and protein phosphatase 1 (PP1). Here we report that lysine acetylation negatively regulates GP activity by both inhibiting enzyme activity directly and promoting dephosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PP1 | down-regulates activity
dephosphorylation
|
PYGL |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267403 |
Ser15 |
QEKRRQIsIRGIVGV |
Homo sapiens |
|
| pmid |
sentence |
| 22225877 |
GP is the first protein whose function was discovered to be regulated by reversible protein phosphorylation, which is controlled by phosphorylase kinase (PhK) and protein phosphatase 1 (PP1). Here we report that lysine acetylation negatively regulates GP activity by both inhibiting enzyme activity directly and promoting dephosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PP1 | up-regulates activity
dephosphorylation
|
CASP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264661 |
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 |
| + |
PP1 | up-regulates
dephosphorylation
|
CDK9 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264671 |
Ser175 |
FGLARAFsLAKNSQP |
Homo sapiens |
|
| pmid |
sentence |
| 21533037 |
Protein phosphatase-1 activates cdk9 by dephosphorylating ser175 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PP1 | down-regulates activity
dephosphorylation
|
AXIN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264660 |
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 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PP1 | up-regulates quantity by stabilization
dephosphorylation
|
MDM2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264666 |
Ser370 |
KKTIVNDsRESCVEE |
Homo sapiens |
U2-OS Cell |
| 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 |
| + |
PP1 | down-regulates activity
dephosphorylation
|
AKT1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264658 |
Ser473 |
RPHFPQFsYSASGTA |
Homo sapiens |
SK-BR-3 Cell |
| 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 |
| + |
PP1 |
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