| + |
PPP1CC | down-regulates activity 
dephosphorylation
|
TP53 |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248499 |
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-248500 |
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 |
| + |
PPP1CC | up-regulates activity 
dephosphorylation
|
CASP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248503 |
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 |
| + |
PPP1CC | up-regulates
dephosphorylation
|
CDK9 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173450 |
Ser175 |
FGLARAFsLAKNSQP |
Homo sapiens |
|
| pmid |
sentence |
| 21533037 |
Protein phosphatase-1 activates cdk9 by dephosphorylating ser175 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173454 |
Thr186 |
NSQPNRYtNRVVTLW |
Homo sapiens |
|
| pmid |
sentence |
| 21533037 |
Pp1 is an activator of cdk9. Pp1 dephosphorylates cdk9 thr186. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PPP1CC | down-regulates activity
dephosphorylation
|
AXIN1 |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248496 |
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-248497 |
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-248494 |
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-248495 |
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 |
| + |
PPP1CC | up-regulates quantity by stabilization
dephosphorylation
|
MDM2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248504 |
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 |
| + |
PPP1CC | down-regulates activity
dephosphorylation
|
AKT |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248502 |
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 |
| Pathways: | COVID-19 Causal Network |
| + |
PPP1CC | down-regulates activity
dephosphorylation
|
AKT1 |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252605 |
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 |
| + |
PPP1CC |
dephosphorylation
|
AHCYL1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248498 |
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 |
| + |
PPP1CC | up-regulates activity
dephosphorylation
|
DDX58 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264580 |
Ser8 |
MTTEQRRsLQAFQDY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23499489 |
We identified PP1alpha and PP1gamma as primary phosphatases responsible for MDA5 and RIG-I dephosphorylation, leading to their activation.|endogenous RIG-I and MDA5 that interacted with PP1 exhibited markedly decreased phosphorylation levels at S8 and S88, respectively |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network |
| + |
PPP1CC | up-regulates activity
dephosphorylation
|
IFIH1 |
0.249 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264578 |
Ser88 |
EALRRTGsPLAARYM |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25865883 |
A recent study has revealed that PP1alpha and PP1gamma phosphatases are responsible for dephosphorylating MDA5 and are essential for its activation. |PP1gamma mediates dephosphorylation of MDA5 not only at Ser-88 but also at other Ser/Thr residues. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264579 |
Ser88 |
EALRRTGsPLAARYM |
Homo sapiens |
|
| pmid |
sentence |
| 23499489 |
Exogenous PP1alpha or PP1gamma substantially decreased the S88 phosphorylation of Flag-MDA5|we identified PP1alpha and PP1gamma as primary phosphatases responsible for MDA5 and RIG-I dephosphorylation, leading to their activation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network |
| + |
NEK2 | down-regulates
phosphorylation
|
PPP1CC |
0.502 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78306 |
Thr307 |
EKKKPNAtRPVTPPR |
Homo sapiens |
|
| pmid |
sentence |
| 10880350 |
Pp1 is a substrate for nek2 and phosphorylation of pp1gamma(1) on two c-terminal sites reduces its phosphatase activity. / threonine-307 and -318 appear to be equally well phosphorylated by nek2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78603 |
Thr318 |
TPPRGMItKQAKK |
Homo sapiens |
|
| pmid |
sentence |
| 10880350 |
Pp1 is a substrate for nek2 and phosphorylation of pp1gamma(1) on two c-terminal sites reduces its phosphatase activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PPP1CC | up-regulates activity
dephosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248501 |
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 |
| + |
PPP1CC | up-regulates activity
dephosphorylation
|
EIF2S1 |
0.422 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254119 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27629041 |
Dephosphorylation of eIF2α is central to ISR signal termination to restore protein synthesis and normal cell functioning. It is mediated by protein phosphatase 1 (PP1) complex that recruits a PP1 catalytic subunit (PP1c) and one of the two regulatory subunits. In mammals, phosphatase activity is regulated by either PPP1R15A (also known as growth arrest and DNA damageâ€inducible protein, GADD34), which is induced as part of the ISR. the GADD34–PP1 complex acts as an important negative feedback loop to restore protein synthesis once the ER stress has been resolved, and as such aids in cell survival |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ER STRESS |
| + |
ANKRD28 | up-regulates activity
binding
|
PPP1CC |
0.456 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264794 |
|
|
in vitro |
|
| pmid |
sentence |
| 17023142 |
Phosphatase Interactor Targeting K protein (PITK) was previously identified as a novel PP1 targeting subunit implicated in modulating the phosphorylation of the transcriptional regulator heterogeneous nuclear ribonucleoprotein K (hnRNP K) |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PPP1R15A | up-regulates
relocalization, binding
|
PPP1CC |
0.686 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120734 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14718519 |
We found smad7 interacts with growth arrest and dna damage protein, gadd34, a regulatory subunit of the protein phosphatase 1 (pp1) holoenzyme, which subsequently recruits catalytic subunit of pp1 (pp1c) to dephosphorylate t?RI. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120471 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14718519 |
We found smad7 interacts with growth arrest and dna damage protein, gadd34, a regulatory subunit of the protein phosphatase 1 (pp1) holoenzyme, which subsequently recruits catalytic subunit of pp1 (pp1c) to dephosphorylate tbetari. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ER STRESS |
| + |
PPP1R15A | up-regulates activity
binding
|
PPP1CC |
0.686 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260174 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27629041 |
Dephosphorylation of eIF2α is central to ISR signal termination to restore protein synthesis and normal cell functioning 15. It is mediated by protein phosphatase 1 (PP1) complex that recruits a PP1 catalytic subunit (PP1c) and one of the two regulatory subunits. In mammals, phosphatase activity is regulated by either PPP1R15A (also known as growth arrest and DNA damage‐inducible protein, GADD34), which is induced as part of the ISR. the GADD34–PP1 complex acts as an important negative feedback loop to restore protein synthesis once the ER stress has been resolved, and as such aids in cell survival |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ER STRESS |
| + |
PPP1R1B | down-regulates activity
binding
|
PPP1CC |
0.579 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264958 |
|
|
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 |
| + |
CDCA2 | up-regulates activity
binding
|
PPP1CC |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274003 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 32938714 |
This result demonstrates that the three sites of Repo-Man (Ser-543, Ser-977, and Ser-981) are phosphorylated by Aurora B in early mitosis. We uncover that PP1γ is recruited to mitotic chromosomes by its regulatory subunit Repo-Man in the absence of Aurora B activity and that Aurora B regulates dissociation of PP1γ by phosphorylating and disrupting PP1γ-Repo-Man interactions on chromatin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1CC | up-regulates
dephosphorylation
|
IKZF1 |
0.336 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174865 |
|
|
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 |
| + |
PPP1CC | down-regulates
dephosphorylation
|
TGFBR1 |
0.445 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121277 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14718519 |
We found smad7 interacts with growth arrest and dna damage protein, gadd34, a regulatory subunit of the protein phosphatase 1 (pp1) holoenzyme, which subsequently recruits catalytic subunit of pp1 (pp1c) to dephosphorylate t?RI. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network |
3.0
PPP1CC
- 
- 