| + |
PPM1A | up-regulates activity 
dephosphorylation
|
YAP1 |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276984 |
Ser127 |
PQHVRAHsSPASLQL |
Homo sapiens |
|
| pmid |
sentence |
| 33630828 |
Although the authors show an in vitro kinase assay where PPM1A supposedly dephosphorylates YAP on Ser127, Fig. 4A lacks a positive control to ensure that PPM1A purified from cells is active.|The protein phosphatase PPM1A dephosphorylates and activates YAP to govern mammalian intestinal and liver regeneration. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1A | down-regulates activity 
dephosphorylation
|
TBK1 |
0.419 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276966 |
Ser172 |
EDDEQFVsLYGTEEY |
Homo sapiens |
|
| pmid |
sentence |
| 27419230 |
Furthermore, PPM1A, but not PPM1B, serves as an efficient phosphatase to dephosphorylate Ser 172 residue of both TBK1 and IKKepsilon kinases, which is critical for their kinase activities.|In a similar in vitro phosphatase assay, incubation of PPM1A also eliminated TBK1 and IKKepsilon phosphorylation at Ser 172 residue, evidenced by phospho-S172 immunoblotting (XREF_FIG, F and G).|These observations suggest that PPM1A may block kinase activities of TBK1 and IKKepsilon. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1A | down-regulates activity
dephosphorylation
|
IKBKE |
0.282 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277072 |
Ser172 |
DDDEKFVsVYGTEEY |
Homo sapiens |
|
| pmid |
sentence |
| 27419230 |
PPM1A directly dephosphorylates both MAVS and TBK1 and IKKepsilon.|In a similar in vitro phosphatase assay, incubation of PPM1A also eliminated TBK1 and IKKepsilon phosphorylation at Ser 172 residue, evidenced by phospho-S172 immunoblotting (XREF_FIG, F and G).|These observations suggest that PPM1A may block kinase activities of TBK1 and IKKepsilon. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1A | down-regulates
dephosphorylation
|
IKBKB |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181655 |
Ser177 |
AKELDQGsLCTSFVG |
Homo sapiens |
|
| pmid |
sentence |
| 18930133 |
Using a functional genomic approach, we have identified two protein serine/threonine phosphatases, ppm1a and ppm1b, as ikkbeta phosphatases. Overexpression of ppm1a or ppm1b results in dephosphorylation of ikkbeta at ser177 and ser181 and termination of ikkbeta-induced nf-kappab activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181659 |
Ser181 |
DQGSLCTsFVGTLQY |
Homo sapiens |
|
| pmid |
sentence |
| 18930133 |
Using a functional genomic approach, we have identified two protein serine/threonine phosphatases, ppm1a and ppm1b, as ikkbeta phosphatases. Overexpression of ppm1a or ppm1b results in dephosphorylation of ikkbeta at ser177 and ser181 and termination of ikkbeta-induced nf-kappab activation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PPM1A | down-regulates activity
dephosphorylation
|
IKBKB |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248486 |
Ser177 |
AKELDQGsLCTSFVG |
Homo sapiens |
|
| pmid |
sentence |
| 18930133 |
PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation|Overexpression of PPM1A or PPM1B results in dephosphorylation of IKKbeta at Ser177 and Ser181 and termination of IKKbeta-induced NF-kappaB activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248487 |
Ser181 |
DQGSLCTsFVGTLQY |
Homo sapiens |
|
| pmid |
sentence |
| 18930133 |
PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation|Overexpression of PPM1A or PPM1B results in dephosphorylation of IKKbeta at Ser177 and Ser181 and termination of IKKbeta-induced NF-kappaB activation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PPM1A | down-regulates activity
dephosphorylation
|
PAK1 |
0.341 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248492 |
Ser199 |
PRPEHTKsVYTRSVI |
Rattus norvegicus |
|
| pmid |
sentence |
| 18586681 |
Purified PP2Cα protein efficiently dephosphorylated PAK1 in vitro (Fig. 1, D and E). We previously assessed the time course of phospho-PAK1 dephosphorylation assessed using specific antibodies against either Ser(P)198/203 or Thr(P)422 sites in the PAK1 activation loop. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248493 |
Ser57 |
KKDRFYRsILPGDKT |
Rattus norvegicus |
|
| pmid |
sentence |
| 18586681 |
Both sites were dephosphorylated with the same kinetics; the anti-Ser(P)198 antibody was subsequently used as it exhibited lower background staining. Direct comparison of PP2Cα with purified PP1 and PP2A lead us to conclude that at the same molar ratio PP2Cα was the most efficient in dephosphorylating PAK1 (Fig. 1D). In this case we monitored two autophosphorylation sites in the Pak1 N-terminal regulatory region (Ser57 and Ser198/203) using phosphospecific antibodies: both sites showed the same kinetics of inactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248491 |
Thr423 |
PEQSKRStMVGTPYW |
Rattus norvegicus |
|
| pmid |
sentence |
| 18586681 |
Purified PP2Cα protein efficiently dephosphorylated PAK1 in vitro (Fig. 1, D and E). We previously assessed the time course of phospho-PAK1 dephosphorylation assessed using specific antibodies against either Ser(P)198/203 or Thr(P)422 sites in the PAK1 activation loop. |
|
| Publications: |
3 |
Organism: |
Rattus Norvegicus |
| + |
PPM1A | down-regulates activity
dephosphorylation
|
RELA |
0.36 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276963 |
Ser276 |
SMQLRRPsDRELSEP |
Homo sapiens |
|
| pmid |
sentence |
| 23812431 |
23 Here we show that PPM1A directly dephosphorylated RelA at S536 and S276, with resultant inhibition of NF-kappaB transactivation and decreased expression of target genes, notably including MCP-1 and CCL2.|Taken together, these data suggest that dephosphorylation of S276 by PPM1A may contribute to inhibit RelA transcriptional activity, but the majority of PPM1A activity to inhibit RelA transcription relies on dephos phorylation of S536 of RelA.|We show that PPM1A directly dephosphorylated RelA at residues S536 and S276 and selectively inhibited Nuclear factor-\u03baB transcriptional activity, resulting in decreased expression of monocyte chemotactic protein-1/chemokine (C-C motif) ligand 2 and interleukin-6, cytokines implicated in cancer metastasis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276964 |
Ser536 |
SGDEDFSsIADMDFS |
Homo sapiens |
|
| pmid |
sentence |
| 23812431 |
We show that PPM1A directly dephosphorylated RelA at residues S536 and S276 and selectively inhibited NF-kappaB transcriptional activity, resulting in decreased expression of monocyte chemotactic protein-1 and chemokine (C-C motif) ligand 2 and interleukin-6, cytokines implicated in cancer metastasis.|18 Wild-type, but not phosphatase-dead, PPM1A dephosphorylated the pS536 peptide with equivalent efficacy as the known RelA S536 phosphatase, Wip1 (XREF_FIG, compare lanes 4 and 7).|Taken together, these data suggest that dephosphorylation of S276 by PPM1A may contribute to inhibit RelA transcriptional activity, but the majority of PPM1A activity to inhibit RelA transcription relies on dephos phorylation of S536 of RelA. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PPM1A | down-regulates activity
dephosphorylation
|
STING1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276958 |
Ser358 |
VPSTSTMsQEPELLI |
Homo sapiens |
|
| pmid |
sentence |
| 25815785 |
Collectively, our findings suggest that the overexpression of PPM1A antagonizes the STING- and TBK1-induced type I interferon signaling pathway.|First, PPM1A directly dephosphorylated STING, likely via its S358 site (Figs.|Moreover, our study demonstrates that while TBK1 enhances STING aggregation in a kinase activity-dependent manner, PPM1A suppresses STING aggregation by dephosphorylating both STING and TBK1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1A | up-regulates activity
dephosphorylation
|
PIK3R1 |
0.328 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248489 |
Ser608 |
ENTEDQYsLVEDDED |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 15016818 |
Protein phosphatase-2C alpha as a positive regulator of insulin sensitivity through direct activation of phosphatidylinositol 3-kinase in 3T3-L1 adipocytes|PP2Cα dephosphorylates the p85 subunit of PI3K, and dephosphorylation of the p85 subunit of PI3K at Ser608 increases its activity |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PPM1A | up-regulates activity
dephosphorylation
|
PI3K |
0.328 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252724 |
Ser608 |
ENTEDQYsLVEDDED |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 15016818 |
Protein phosphatase-2C alpha as a positive regulator of insulin sensitivity through direct activation of phosphatidylinositol 3-kinase in 3T3-L1 adipocytes|PP2C_ dephosphorylates the p85 subunit of PI3K, and dephosphorylation of the p85 subunit of PI3K at Ser608 increases its activity |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PPM1A | down-regulates activity
dephosphorylation
|
CDK9 |
0.506 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248490 |
Thr186 |
NSQPNRYtNRVVTLW |
Homo sapiens |
|
| pmid |
sentence |
| 18829461 |
Taken together, our data indicate that PPM1A and to some extent PPM1B are important negative regulators of P-TEFb function |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1A | down-regulates
dephosphorylation
|
GSK3B/Axin/APC |
0.368 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-227955 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10644691 |
Pp2c utilizes axin as a substrate both in vitro and in vivo and decreases its half-life. These results indicate that pp2c is a positive regulator of wnt signal transduction and mediates its effects through the dephosphorylation of axin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1A | down-regulates activity
dephosphorylation
|
SMAD2 |
0.658 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217628 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16751101 |
Ppm1a dephosphorylates and promotes nuclear export of tgfbeta-activated smad2/3; these results suggest that phospho-smad2 is a direct substrate of mg2+-dependent ppm1a. in conclusion, ppm1a is a bona fide phosphatase that directly dephosphorylates the critical sxs motif of r-smads. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277034 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25026293 |
All of these results lead to the conclusion that PPM1A inhibits the TGF-\u03b2-induced the activity of Smad2, Smad3 and transcriotional responses, whereas depletion of PPM1A enhances the activation of TGF-\u03b2/Smads signaling in bladder cancer cells.|Protein phosphatase PPM1A has been reported to dephosphorylate TGF-\u03b2-activated Smad2/3, thus inhibiting the TGF-\u03b2 signaling pathway. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PPM1A | down-regulates
dephosphorylation
|
SMAD2 |
0.658 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146919 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16751101 |
Ppm1a dephosphorylates and promotes nuclear export of tgfbeta-activated smad2/3; these results suggest that phospho-smad2 is a direct substrate of mg2+-dependent ppm1a. in conclusion, ppm1a is a bona fide phosphatase that directly dephosphorylates the critical sxs motif of r-smads. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1A | down-regulates
dephosphorylation
|
AXIN1 |
0.444 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74231 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10644691 |
Pp2c utilizes axin as a substrate both in vitro and in vivo and decreases its half-life. These results indicate that pp2c is a positive regulator of wnt signal transduction and mediates its effects through the dephosphorylation of axin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1A | down-regulates activity
dephosphorylation
|
CDK2 |
0.296 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277107 |
|
|
in vitro |
|
| pmid |
sentence |
| 10934208 |
Moreover, purified recombinant PP2C alpha and PP2C beta 2 proteins efficiently dephosphorylated monomeric Cdk2/Cdk6 in vitro. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PPM1A | down-regulates activity
dephosphorylation
|
SMAD3 |
0.61 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-232110 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16751101 |
Ppm1a dephosphorylates and promotes nuclear export of tgfbeta-activated smad2/3; these results suggest that phospho-smad2 is a direct substrate of mg2+-dependent ppm1a. in conclusion, ppm1a is a bona fide phosphatase that directly dephosphorylates the critical sxs motif of r-smads. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1A | down-regulates
dephosphorylation
|
SMAD1 |
0.521 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149077 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16931515 |
In this study, we have found that ppm1a, a metal ion-dependent protein serine/threonine phosphatase, physically interacts with and dephosphorylates smad1 both in vitro and in vivo. considering the highly conserved nature of the sxs motif in all r-smads, we reasoned that ppm1a might also recognize the sxs motif in the bmp-activated smad1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | up-regulates
binding
|
PPM1A |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178643 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18482992 |
Upon complex formation with pten, ppm1a is protected from degradation induced by the tgf-? Signaling. this study establishes a novel role for nuclear pten in the stabilization of ppm1a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1A | down-regulates activity
dephosphorylation
|
MAPK14 |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59618 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9707433 |
Moreover, when expressed in mammalian cells, pp2ca inhibited the activation of the p38 and jnk cascades induced by environmental stresses. Both in vivo and in vitro observations indicated that pp2ca dephosphorylated and inactivated mapkks (mkk6 and sek1) and a mapk (p38) in the stress-responsive mapk cascades. Furthermore, a direct interaction of pp2ca and p38 was demonstrated by a co-immunoprecipitation assay |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | P38 Signaling |
| + |
PPM1A | down-regulates activity
dephosphorylation
|
IRF3 |
0.25 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277152 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27419230 |
In contrast, coexpression of wild-type PPM1A, but not its D239N or R174G mutant, abolished IRF3 activation (XREF_FIG).|We found that PPM1A abolished the C-terminal phosphorylation of IRF3 (XREF_FIG), whereas depletion of PPM1A expression improved virus induced pIRF3 level (XREF_FIG and XREF_FIG). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1A | down-regulates
dephosphorylation
|
SMAD3 |
0.61 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146922 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16751101 |
Ppm1a dephosphorylates and promotes nuclear export of tgfbeta-activated smad2/3. in conclusion, ppm1a is a bona fide phosphatase that directly dephosphorylates the critical sxs motif of r-smads. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1A | down-regulates quantity by destabilization
dephosphorylation
|
AXIN1 |
0.444 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248488 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10644691 |
In addition, PP2C expression relieves Axin-mediated repression of LEF-1-dependent transcription. PP2C utilizes Axin as a substrate both in vitro and in vivo and decreases its half-life. These results indicate that PP2C is a positive regulator of Wnt signal transduction and mediates its effects through the dephosphorylation of Axin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PPM1A
- 
- 