+ |
PPP1CA | up-regulates activity
dephosphorylation
|
PREX1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277024 |
Ser1001 |
IRFGRKPsLIGLDPE |
Homo sapiens |
|
pmid |
sentence |
22242915 |
MS analysis of wild-type P-Rex1 and a PP1\u03b1-binding-deficient mutant revealed that endogenous PP1\u03b1 dephosphorylates P-Rex1 on at least three residues, Ser834, Ser1001 and Ser1165.|The phosphatase activity of PP1\u03b1 is required for P-Rex1 activation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277023 |
Ser1165 |
DSGHDTMsYRDSYSE |
Homo sapiens |
|
pmid |
sentence |
22242915 |
MS analysis of wild-type P-Rex1 and a PP1\u03b1-binding-deficient mutant revealed that endogenous PP1\u03b1 dephosphorylates P-Rex1 on at least three residues, Ser834, Ser1001 and Ser1165.|The phosphatase activity of PP1\u03b1 is required for P-Rex1 activation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277022 |
Ser834 |
LSLGPRLsLCEDSPM |
Homo sapiens |
|
pmid |
sentence |
22242915 |
MS analysis of wild-type P-Rex1 and a PP1\u03b1-binding-deficient mutant revealed that endogenous PP1\u03b1 dephosphorylates P-Rex1 on at least three residues, Ser834, Ser1001 and Ser1165.|The phosphatase activity of PP1\u03b1 is required for P-Rex1 activation. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | down-regulates activity
dephosphorylation
|
MECOM |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273429 |
Ser1037 |
IGNSNHGsQSPRNVE |
|
|
pmid |
sentence |
23858473 |
We also identified EVI1 phosphorylation sites by MS analysis and showed that Ser538 and Ser858 can be phosphorylated and dephosphorylated by two EVI1 interactome proteins, casein kinase II and protein phosphatase-1α. Finally, mutations that impair EVI1 phosphorylation at these sites reduced EVI1 DNA binding through its C-terminal zinc finger domain and induced cancer cell proliferation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273430 |
Ser726 |
PLKMEPQsPGEVKKL |
|
|
pmid |
sentence |
23858473 |
We also identified EVI1 phosphorylation sites by MS analysis and showed that Ser538 and Ser858 can be phosphorylated and dephosphorylated by two EVI1 interactome proteins, casein kinase II and protein phosphatase-1α. Finally, mutations that impair EVI1 phosphorylation at these sites reduced EVI1 DNA binding through its C-terminal zinc finger domain and induced cancer cell proliferation. |
|
Publications: |
2 |
+ |
PPP1CA | up-regulates activity
dephosphorylation
|
PREX2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277183 |
Ser1107 |
DTISNRDsYSDCNSN |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
26438819 |
PREX2 is dephosphorylated by PP1α and PP2A.PAK-mediated phosphorylation of PREX2 reduced GEF activity toward Rac1 by inhibiting PREX2 binding to PIP3 and Gβγ. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | up-regulates activity
dephosphorylation
|
YAP1 |
0.658 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276999 |
Ser127 |
PQHVRAHsSPASLQL |
Homo sapiens |
|
pmid |
sentence |
21909427 |
In the present study, we demonstrate that PP1A (catalytic subunit of protein phosphatase-1) interacts with and dephosphorylates YAP2 in vitro and in vivo, and PP1A-mediated dephosphorylation induces the nuclear accumulation and transcriptional activation of YAP2.|PP1A dephosphorylates endogenous YAP2 at serine 127. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | up-regulates
dephosphorylation
|
PFN1 |
0.248 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-196816 |
Ser138 |
MASHLRRsQY |
Homo sapiens |
|
pmid |
sentence |
22479341 |
Knockdown of the catalytic subunit of pp1 (pp1c_), but not pp2a (pp2ac_), increased ps137-pfn1 levels. Pp1c_ binds pfn1 in cultured cells, and this interaction was increased by a phosphomimetic mutation of pfn1 at ser-137 (s137d). Together, these data define pp1 as the principal phosphatase for ser-137 of pfn1 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | down-regulates activity
dephosphorylation
|
CAD |
0.337 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263741 |
Ser1406 |
CSGAGGRrLSSFVTK |
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 |
+ |
PPP1CA | down-regulates activity
dephosphorylation
|
BRCA1 |
0.384 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248561 |
Ser1423 |
AVLEQHGsQPSNSYP |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
17603999 |
Protein kinases involved in the DNA damage checkpoint control, such as ATM, ATR, and hCds1/Chk2, have been shown to phosphorylate and activate BRCA1 upon DNA damage. |Altogether, these results indicate that PP1α specifically dephosphorylates BRCA1 at multiple serine sites, including S988 [12], S1423, and S1524. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248562 |
Ser1524 |
LQNRNYPsQEELIKV |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
17603999 |
Protein kinases involved in the DNA damage checkpoint control, such as ATM, ATR, and hCds1/Chk2, have been shown to phosphorylate and activate BRCA1 upon DNA damage. |Altogether, these results indicate that PP1α specifically dephosphorylates BRCA1 at multiple serine sites, including S988 [12], S1423, and S1524. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248560 |
Ser988 |
PPLFPIKsFVKTKCK |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
17603999 |
Protein kinases involved in the DNA damage checkpoint control, such as ATM, ATR, and hCds1/Chk2, have been shown to phosphorylate and activate BRCA1 upon DNA damage. |Altogether, these results indicate that PP1α specifically dephosphorylates BRCA1 at multiple serine sites, including S988 [12], S1423, and S1524. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | down-regulates activity
dephosphorylation
|
TP53 |
0.32 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248556 |
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-248557 |
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 |
+ |
PPP1CA | up-regulates activity
dephosphorylation
|
CASP2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248564 |
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 |
+ |
PPP1CA | down-regulates activity
dephosphorylation
|
AXIN1 |
0.338 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248553 |
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-248554 |
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-248551 |
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-248552 |
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 |
+ |
PPP1CA | up-regulates activity
dephosphorylation
|
RAF1 |
0.274 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251649 |
Ser259 |
SQRQRSTsTPNVHMV |
Homo sapiens |
|
pmid |
sentence |
16630891 |
We have identified a complex comprised of Shoc2/Sur-8 and the catalytic subunit of protein phosphatase 1 (PP1c) as a highly specific M-Ras effector. M-Ras targets Shoc2-PP1c to stimulate Raf activity by dephosphorylating the S259 inhibitory site of Raf proteins |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Noonan syndrome |
+ |
PPP1CA | up-regulates activity
dephosphorylation
|
WWTR1 |
0.526 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277115 |
Ser311 |
PYHSREQsTDSGLGL |
Homo sapiens |
|
pmid |
sentence |
21189257 |
PP1A dephosphorylates TAZ at Ser-89 and Ser-311, promotes TAZ nuclear translocation, and stabilizes TAZ by disrupting the binding to the SCF E3 ubiquitin ligase. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277116 |
Ser89 |
AQHVRSHsSPASLQL |
Homo sapiens |
|
pmid |
sentence |
21189257 |
PP1A dephosphorylates TAZ at Ser-89 and Ser-311, promotes TAZ nuclear translocation, and stabilizes TAZ by disrupting the binding to the SCF E3 ubiquitin ligase. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | up-regulates quantity by stabilization
dephosphorylation
|
MDM2 |
0.363 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248566 |
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 |
+ |
PPP1CA | down-regulates activity
dephosphorylation
|
AKT1 |
0.436 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252603 |
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 |
+ |
PPP1CA | down-regulates activity
dephosphorylation
|
AKT |
0.436 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248559 |
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 |
+ |
PPP1CA |
dephosphorylation
|
AHCYL1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248555 |
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 |
+ |
PPP1CA | down-regulates activity
dephosphorylation
|
STAT3 |
0.335 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248563 |
Ser727 |
NTIDLPMsPRTLDSL |
Homo sapiens |
Hep-G2 Cell, U-266 Cell |
pmid |
sentence |
19440292 |
Avicins dephosphorylate Stat3 in a variety of human tumor cell lines, leading to a decrease in the transcriptional activity of Stat3.| However, PD98059, an inhibitor of MEK1/2, had no significant effects on avicin-induced dephosphorylation of Stat3 (Ser 727) |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | up-regulates activity
dephosphorylation
|
DDX58 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264581 |
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 |
+ |
PPP1CA | up-regulates activity
dephosphorylation
|
TRIM28 |
0.327 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277075 |
Ser824 |
LPGAGLSsQELSGGP |
Homo sapiens |
|
pmid |
sentence |
20424263 |
PP1\u03b1 dephosphorylates KAP1 at Ser 824 . |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | up-regulates activity
dephosphorylation
|
IFIH1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264577 |
Ser88 |
EALRRTGsPLAARYM |
Homo sapiens |
HEK-293 Cell |
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: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | up-regulates
dephosphorylation
|
CASP9 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-195992 |
Thr125 |
PEVLRPEtPRPVDIG |
Homo sapiens |
|
pmid |
sentence |
22311969 |
Pp1 dephosphorylated thr125 site of caspase-9 and activated caspase-9 to mediate il-2 deprivation-induced apoptosis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | up-regulates activity
dephosphorylation
|
CASP9 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248565 |
Thr125 |
PEVLRPEtPRPVDIG |
Homo sapiens |
|
pmid |
sentence |
16888006 |
ERK/MAPK phosphorylates caspase-9 at Thr(125), and this phosphorylation is crucial for caspase-9 inhibition. Until now, the phosphatase responsible for Thr(125) dephosphorylation has not been described. Here, we demonstrate that in IL-2-proliferating cells, phosphorylated serine/threonine phosphatase type 1alpha (PP1alpha) associates with phosphorylated caspase-9. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | up-regulates
dephosphorylation
|
CCND3 |
0.248 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-142884 |
Thr283 |
QGPSQTStPTDVTAI |
Homo sapiens |
|
pmid |
sentence |
16331257 |
These results support the hypothesis that pp1 constitutively keeps cyclin d3 in a stable, dephosphorylated state |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LMTK2 | down-regulates activity
phosphorylation
|
PPP1CA |
0.589 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-94631 |
Thr320 |
NPGGRPItPPRNSAK |
Homo sapiens |
|
pmid |
sentence |
12393858 |
Kpi-2 kinase domain phosphorylated protein phosphatase-1 (pp1c) at thr(320), which attenuated pp1c activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK1 | down-regulates activity
phosphorylation
|
PPP1CA |
0.556 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-151799 |
Thr320 |
NPGGRPItPPRNSAK |
Homo sapiens |
|
pmid |
sentence |
12202491 |
Both of these pp1 isoforms contain an arg-pro-ile/val-thr-pro-pro-arg sequence near the c terminus, a known site of phosphorylation by cdc/cdk kinases, and phosphorylation attenuates phosphatase activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates activity
phosphorylation
|
PPP1CA |
0.403 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-92269 |
Thr320 |
NPGGRPItPPRNSAK |
Homo sapiens |
|
pmid |
sentence |
12202491 |
Pp1 isoforms contain an arg-pro-ile/val-thr-pro-pro-arg sequence near the c terminus, a known site of phosphorylation by cdc/cdk kinases, and phosphorylation attenuates phosphatase activity. Increasing doses of cdk2 resulted in increased phosphorylation of the thr-320 site. Phosphorylation of this site in pp1 corresponded to decreased pp1 activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-151803 |
Thr320 |
NPGGRPItPPRNSAK |
Homo sapiens |
|
pmid |
sentence |
17202132 |
We observed that phosphorylation of protein phosphatase 1 (PP1) on Thr320 is reduced in brain extracts from Egr-1-/- mice, indicating that a kinase downstream of Egr-1 phosphorylates PP1. In HEK 293 cells co-transfected with PP1 and Cdk5, Cdk5 phosphorylates PP1. In vitro, Cdk5 purified from bovine brain phosphorylates bacterially expressed recombinant PP1 |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | Dopaminergic Synapse |
+ |
CDK2 | down-regulates activity
phosphorylation
|
PPP1CA |
0.385 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-92265 |
Thr320 |
NPGGRPItPPRNSAK |
Homo sapiens |
|
pmid |
sentence |
12202491 |
Both of these pp1 isoforms contain an arg-pro-ile/val-thr-pro-pro-arg sequence near the c terminus, a known site of phosphorylation by cdc/cdk kinases, and phosphorylation attenuates phosphatase activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | down-regulates
dephosphorylation
|
AKT1 |
0.436 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-163961 |
Thr450 |
TAQMITItPPDQDDS |
Homo sapiens |
|
pmid |
sentence |
20186153 |
Several stps have been reported to negatively regulate akt pathway. It has been shown that pp1 dephosphorylates akt and regulates cell survival. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | up-regulates activity
dephosphorylation
|
NOS3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248558 |
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 |
+ |
PPP1CA | up-regulates activity
dephosphorylation
|
NR3C1 |
0.295 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277161 |
|
|
Homo sapiens |
|
pmid |
sentence |
32585168 |
The current study assessed whether PP1\u03b1 can stimulate GR function and tested two different hypotheses: First, that PP1\u03b1 regulates GR activity through suppression of MDM2 activity by dephosphorylating it at Ser166, thereby reducing the MDM2-mediated ubiquitination of GR and the subsequent proteasomal degradation of the receptor, as shown for the MR and AR ( xref ; xref ); and second, that PP1\u03b1 directly dephosphorylates the GR at a particular site to relieve functional repression as demonstrated for PP2A and PP5 ( xref ; xref ; xref ).|The involvement of GR-Ser211 phosphorylation supports the assumption that altered subcellular trafficking is a mechanism less likely contributing to the PP1\u03b1-dependent GR activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | down-regulates activity
dephosphorylation
|
SP1 |
0.269 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251952 |
|
|
Homo sapiens |
|
pmid |
sentence |
12684058 |
Transcription factors Sp1 and Sp3 activate alpha-ENaC2 transcription through a GC-rich element (Sp1-binding site) in the promoter. Sp1 and Sp3 are essential for alpha-ENaC2 transcription in lung epithelial cells and that dephosphorylation of the Sp transcription factors by PP1 suppresses alpha-ENaC2 expression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMAD7 | up-regulates
binding
|
PPP1CA |
0.405 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145389 |
|
|
Homo sapiens |
|
pmid |
sentence |
16571110 |
Smad7, induced by alk1 activation, recruits pp1? To alk1 and thereby inhibits tgf-?/Alk1-induced smad1/5 phosphorylation in ecs |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SHOC2 | up-regulates activity
binding
|
PPP1CA |
0.577 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251647 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16630891 |
Using a proteomics approach, we have identified a complex comprised of Shoc2/Sur-8 and the catalytic subunit of protein phosphatase 1 (PP1c) as a highly specific M-Ras effector. M-Ras targets Shoc2-PP1c to stimulate Raf activity by dephosphorylating the S259 inhibitory site |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Noonan syndrome |
+ |
PPP1CA | up-regulates activity
dephosphorylation
|
BRAF |
0.298 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277160 |
|
|
Homo sapiens |
|
pmid |
sentence |
29335436 |
To address whether PP1\u03b1 activates B-Raf through these inhibitory sites, we made use of B-Raf protein mutants in which an individual inhibitory site, as well as all four sites (4A), were mutated to alanine.|We confirmed that GST-B-Raf was phosphorylated by ERK2 in vitro xref , mainly on S151 and T753 (Fig.\u00a0 xref ), and found that PP1\u03b1 dephosphorylated B-Raf on both ERK phosphorylation sites (Fig.\u00a0 xref ). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Noonan syndrome |
+ |
PPP1CA | down-regulates
dephosphorylation
|
ERK1/2 |
0.457 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269927 |
|
|
Homo sapiens |
|
pmid |
sentence |
12840032 |
P-erk1/2 proteins were efficiently dephosphorylated in vitro by protein phosphatases 1 and 2a (pp1/2a) and mapk phosphatase 3 (mkp3). the dual specificity phosphatases that specifically dephosphorylate and inactivate the p-erk1/2 are called mapk phosphatases |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Noonan syndrome |
+ |
PPP1R1C | down-regulates activity
binding
|
PPP1CA |
0.4 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275726 |
|
|
|
|
pmid |
sentence |
18310074 |
IPP5, a novel inhibitor of protein phosphatase 1, suppresses tumor growth and progression of cervical carcinoma cells by inducing G2/M arrest |
|
Publications: |
1 |
+ |
PPP1R8 | down-regulates activity
binding
|
PPP1CA |
0.64 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255657 |
|
|
in vitro |
|
pmid |
sentence |
1322907 |
We have purified two of these nuclear inhibitors of PP-1 (NIPP-1a and NIPP-1b) until homogeneity. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PPP1CA | down-regulates
dephosphorylation
|
MAPK1 |
0.457 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-103152 |
|
|
Homo sapiens |
|
pmid |
sentence |
12840032 |
P-erk1/2 proteins were efficiently dephosphorylated in vitro by protein phosphatases 1 and 2a (pp1/2a) and mapk phosphatase 3 (mkp3) |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | up-regulates
binding
|
CDC25C |
0.483 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-118917 |
|
|
Homo sapiens |
|
pmid |
sentence |
14592972 |
Pp1 recognizes cdc25 directly by interacting with a pp1-binding motif in the cdc25 n-terminus. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | up-regulates
dephosphorylation
|
IKZF1 |
0.282 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174859 |
|
|
Homo sapiens |
Leukemia Cell |
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 |
+ |
PPP1CA | down-regulates
dephosphorylation
|
NEK2 |
0.382 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-152949 |
|
|
Homo sapiens |
|
pmid |
sentence |
17283141 |
Nek2 is activated by autophosphorylation, and its dephosphorylation is catalyzed by pp1 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | down-regulates
dephosphorylation
|
MAPK3 |
0.455 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-103155 |
|
|
Homo sapiens |
|
pmid |
sentence |
12840032 |
P-erk1/2 proteins were efficiently dephosphorylated in vitro by protein phosphatases 1 and 2a (pp1/2a) and mapk phosphatase 3 (mkp3). the dual specificity phosphatases that specifically dephosphorylate and inactivate the p-erk1/2 are called mapk phosphatases |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | down-regulates activity
dephosphorylation
|
NMDA |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265061 |
|
|
Homo sapiens |
|
pmid |
sentence |
14751588 |
DARPP-32/PP1 cascade modulates the physiological properties of NMDA and AMPA receptors, and activation of the DARPP-32/PP1 signaling leads to parallel increase in the phosphorylation of NMDA receptor subunits and intracellular Ca2+ levels |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Brain |
Pathways: | Dopaminergic Synapse |
+ |
PPP1CA | down-regulates activity
dephosphorylation
|
AMPA |
0.504 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265060 |
|
|
Homo sapiens |
|
pmid |
sentence |
14751588 |
Dopamine and cyclic adenosine 3',5'-monophosphate-regulated phosphoprotein, 32 kDa (DARPP-32) is a key element of dopamine/D1/DARPP-32/protein phosphatase-1 (PP-1) signaling cascades of mammalian brain. Phosphorylation of AMPA receptors due to DARPP-32/PP1 signaling cascade increases AMPA channel activity and currents |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Dopaminergic Synapse |
+ |
PPP1R2 | down-regulates
binding
|
PPP1CA |
0.79 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160651 |
|
|
Homo sapiens |
|
pmid |
sentence |
18250156 |
Atm phosphorylates i-2 on serine 43, leading to the dissociation of the pp1-i-2 complex and the activation of pp1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | down-regulates
dephosphorylation
|
Gbeta |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269906 |
|
|
Homo sapiens |
|
pmid |
sentence |
12840032 |
P-erk1/2 proteins were efficiently dephosphorylated in vitro by protein phosphatases 1 and 2a (pp1/2a) and mapk phosphatase 3 (mkp3). the dual specificity phosphatases that specifically dephosphorylate and inactivate the p-erk1/2 are called mapk phosphatases |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | down-regulates activity
dephosphorylation
|
SP3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251953 |
|
|
Homo sapiens |
|
pmid |
sentence |
12684058 |
Transcription factors Sp1 and Sp3 activate alpha-ENaC2 transcription through a GC-rich element (Sp1-binding site) in the promoter. Sp1 and Sp3 are essential for alpha-ENaC2 transcription in lung epithelial cells and that dephosphorylation of the Sp transcription factors by PP1 suppresses alpha-ENaC2 expression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | down-regulates
dephosphorylation
|
AKT |
0.436 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-244436 |
|
|
Homo sapiens |
|
pmid |
sentence |
20186153 |
Several stps have been reported to negatively regulate akt pathway. It has been shown that pp1 dephosphorylates akt and regulates cell survival. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1R1B | down-regulates activity
binding
|
PPP1CA |
0.582 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264957 |
|
|
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 |
Pathways: | Dopaminergic Synapse |
+ |
PPP1CA | down-regulates
dephosphorylation
|
AURKA |
0.446 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-110411 |
|
|
Homo sapiens |
|
pmid |
sentence |
11551964 |
Pp1 is shown to dephosphorylate active stk15 and abolish its activity in vitro. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PHACTR1 | up-regulates activity
binding
|
PPP1CA |
0.553 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260062 |
|
|
Homo sapiens |
HUVEC Cell |
pmid |
sentence |
21939755 |
Phactr-1 was previously identified as protein phosphatase 1 (PP1) α-interacting protein that possesses actin-binding domains. We showed that Phactr-1 depletion decreased PP1 activity, disrupted the fine-tuning of actin polymerization and impaired lamellipodial dynamics. Taken together our results strongly suggest that Phactr-1 is a key component in the angiogenic process. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |