| + |
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 |
dephosphorylation
|
AHCYL1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264657 |
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 |
| + |
PP1 | up-regulates activity
dephosphorylation
|
GSK3B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264820 |
Ser9 |
SGRPRTTsFAESCKP |
|
|
| pmid |
sentence |
| 26088133 |
Anchored PP1 may relieve PKA-mediated inhibition of GSK3beta by dephosphorylating Ser-9, providing bi-directional control of AKAP220 complex formation in response to cAMP. |
|
| Publications: |
1 |
| + |
PP1 | up-regulates
dephosphorylation
|
CCND3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264662 |
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 |
| + |
PP1 | up-regulates activity
dephosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264668 |
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 |
| + |
PPP1R1C | down-regulates activity
binding
|
PP1 |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275725 |
|
|
|
|
| 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 |
| + |
PPP1R3B | up-regulates
binding
|
PP1 |
0.702 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271736 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 36551183 |
In the liver, PTG and PPP1R3B(GL)are expressed at roughly equivalent levels [55], and they jointly promote hepatic glycogen mobilization and storage. PTG overexpression significantly increased glycogen content, mainly due to its ability to promote the redistribution of PP1 and glycogen synthase to glycogen granules, significantly increasing GS activity and glycogen synthesis (Figure 2) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Liver |
| + |
NEK2 | down-regulates
phosphorylation
|
PP1 |
0.503 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264655 |
|
|
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 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PP1 | down-regulates activity
dephosphorylation
|
SP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264669 |
|
|
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 |
| + |
PPP1R2 | down-regulates
binding
|
PP1 |
0.807 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264672 |
|
|
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 |
| + |
CDK1 | down-regulates activity
phosphorylation
|
PP1 |
0.557 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264648 |
|
|
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 |
| + |
PP1 | up-regulates
dephosphorylation
|
IKZF1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264663 |
|
|
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 |
| + |
PP1 | up-regulates activity
dephosphorylation
|
CFTR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264646 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 21317537 |
WNK kinases acted as scaffolds to recruit SPAK, which phosphorylated CFTR and NBCe1-B, reducing their cell surface expression. IRBIT opposed the effects of WNKs and SPAK by recruiting PP1 to the complex to dephosphorylate CFTR and NBCe1-B, restoring their cell surface expression, |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Pancreas |
| + |
CDK5 | down-regulates activity
phosphorylation
|
PP1 |
0.484 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264649 |
|
|
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. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PP1 | down-regulates
dephosphorylation
|
ERK1/2 |
0.505 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269923 |
|
|
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 |
| + |
PP1 | down-regulates activity
dephosphorylation
|
SP3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264652 |
|
|
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 |
| + |
PP1 | down-regulates activity
dephosphorylation
|
PYG |
0.397 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267961 |
|
|
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 |
| Pathways: | Glycogenolysis |
| + |
PP1 | down-regulates activity
dephosphorylation
|
AKT |
0.452 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264659 |
|
|
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 |
| + |
PPP1R8 | down-regulates activity
binding
|
PP1 |
0.667 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264673 |
|
|
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 |
| + |
PP1 | down-regulates
dephosphorylation
|
AURKA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264651 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11551964 |
Pp1 is shown to dephosphorylate active stk15 and abolish its activity in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PP1 | down-regulates
dephosphorylation
|
MAPK3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264665 |
|
|
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 |
| + |
PP1 | down-regulates
dephosphorylation
|
Gbeta |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269901 |
|
|
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 |
| + |
AHCYL1 | up-regulates activity
relocalization
|
PP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264645 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 21317537 |
WNK kinases acted as scaffolds to recruit SPAK, which phosphorylated CFTR and NBCe1-B, reducing their cell surface expression. IRBIT opposed the effects of WNKs and SPAK by recruiting PP1 to the complex to dephosphorylate CFTR and NBCe1-B, restoring their cell surface expression, |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Pancreas |
| + |
CDK2 | down-regulates activity
phosphorylation
|
PP1 |
0.385 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264650 |
|
|
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 |
| + |
PP1 | down-regulates
dephosphorylation
|
MAPK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264664 |
|
|
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 |
| + |
PP1 | up-regulates
binding
|
CDC25C |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264654 |
|
|
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 |
| + |
PPP1R1B | down-regulates activity
binding
|
PP1 |
0.674 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269869 |
|
|
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 |
| + |
PPP1R9B | up-regulates activity
binding
|
PP1 |
0.764 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269178 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 10194355 |
In the present study, the interaction between PP1 and spinophilin, a neuronal protein that targets PP1 to dendritic spines, has been characterized. . These studies support the notion that spinophilin functions in vivo as a neuronal PP1 targeting subunit by directing the enzyme to postsynaptic densities and regulating its activity toward physiological substrates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PP1 | down-regulates
dephosphorylation
|
NEK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264667 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17283141 |
Nek2 is activated by autophosphorylation, and its dephosphorylation is catalyzed by pp1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PHACTR1 | up-regulates activity
binding
|
PP1 |
0.553 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264656 |
|
|
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 |
| + |
PP1 | up-regulates activity
dephosphorylation
|
SLC4A4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264647 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 21317537 |
WNK kinases acted as scaffolds to recruit SPAK, which phosphorylated CFTR and NBCe1-B, reducing their cell surface expression. IRBIT opposed the effects of WNKs and SPAK by recruiting PP1 to the complex to dephosphorylate CFTR and NBCe1-B, restoring their cell surface expression, |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Pancreas |
| + |
PPP1R3C | up-regulates
binding
|
PP1 |
0.669 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271735 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 36551183 |
In the liver, PTG and PPP1R3B(GL)are expressed at roughly equivalent levels [55], and they jointly promote hepatic glycogen mobilization and storage. PTG overexpression significantly increased glycogen content, mainly due to its ability to promote the redistribution of PP1 and glycogen synthase to glycogen granules, significantly increasing GS activity and glycogen synthesis (Figure 2) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Liver |
3.0
PP1