+ |
PPM1A | down-regulates activity
dephosphorylation
|
IKBKB |
0.314 |
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
dephosphorylation
|
IKBKB |
0.314 |
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
|
PAK1 |
0.342 |
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 | up-regulates activity
dephosphorylation
|
PI3K |
0.329 |
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 | up-regulates activity
dephosphorylation
|
PIK3R1 |
0.329 |
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 | down-regulates activity
dephosphorylation
|
CDK9 |
0.512 |
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 activity
dephosphorylation
|
SMAD2 |
0.653 |
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. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPM1A | down-regulates activity
dephosphorylation
|
SMAD3 |
0.603 |
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 activity
dephosphorylation
|
MAPK14 |
0.418 |
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
dephosphorylation
|
AXIN1 |
0.449 |
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
dephosphorylation
|
GSK3B/Axin/APC |
0.371 |
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
dephosphorylation
|
SMAD1 |
0.512 |
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 |
+ |
PPM1A | down-regulates
dephosphorylation
|
SMAD3 |
0.603 |
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
dephosphorylation
|
SMAD2 |
0.653 |
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 |
+ |
PTEN | up-regulates
binding
|
PPM1A |
0.314 |
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 quantity by destabilization
dephosphorylation
|
AXIN1 |
0.449 |
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 |