| + |
PPM1D | down-regulates 
dephosphorylation
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163693 |
Ser140 |
GKKATQAsQEY |
Homo sapiens |
|
| pmid |
sentence |
| 20118229 |
Wild-type p53-induced phosphatase 1 dephosphorylates histone variant gamma-h2ax and suppresses dna double strand break repair. Here, we demonstrate that the wild-type p53-induced phosphatase 1 (wip1) also dephosphorylates gamma-h2ax at serine 139 in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1D | down-regulates
dephosphorylation
|
TP53 |
0.582 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135980 |
Ser15 |
PSVEPPLsQETFSDL |
Homo sapiens |
|
| pmid |
sentence |
| 15870257 |
PPM1D also dephosphorylates p53 at phospho-Ser 15. PPM1D dephosphorylations are correlated with reduced cellular intra-S and G2/M checkpoint activity in response to DNA damage induced by ultraviolet and ionizing radiation. Thus, a primary function of PPM1D may be to reverse the p53 and Chk1-induced DNA damage and cell cycle checkpoint responses and return the cell to a homeostatic state following completion of DNA repair. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | P38 Signaling |
| + |
PPM1D | down-regulates activity
dephosphorylation
|
TP53 |
0.582 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248319 |
Ser15 |
PSVEPPLsQETFSDL |
Homo sapiens |
|
| pmid |
sentence |
| 15870257 |
PPM1D binds Chk1 and dephosphorylates the ATR-targeted phospho-Ser 345, leading to decreased Chk1 kinase activity. PPM1D also dephosphorylates p53 at phospho-Ser 15. PPM1D dephosphorylations are correlated with reduced cellular intra-S and G2/M checkpoint activity in response to DNA damage induced by ultraviolet and ionizing radiation. Thus, a primary function of PPM1D may be to reverse the p53 and Chk1-induced DNA damage and cell cycle checkpoint responses and return the cell to a homeostatic state following completion of DNA repair. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | P38 Signaling |
| + |
PPM1D | down-regulates activity
dephosphorylation
|
ATM |
0.511 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248325 |
Ser1981 |
SLAFEEGsQSTTISS |
Homo sapiens |
|
| pmid |
sentence |
| 16949371 |
Here, we report that deficiency of Wip1 resulted in activation of the ataxia-telangiectasia mutated (ATM) kinase. In turn, overexpression of Wip1 was sufficient to reduce activation of the ATM-dependent signaling cascade after DNA damage. Wip1 dephosphorylated ATM Ser1981, a site critical for ATM monomerization and activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1D | down-regulates activity
dephosphorylation
|
RPS6KA3 |
0.373 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248320 |
Ser227 |
DHEKKAYsFCGTVEY |
Mus musculus |
|
| pmid |
sentence |
| 15206906 |
RSK2 (p90 ribosomal S6 kinase 2) is activated via the ERK (extracellular-signal-regulated kinase) pathway by phosphorylation on four sites: Ser227 in the activation loop of the N-terminal kinase domain, Ser369 in the linker, Ser386 in the hydrophobic motif and Thr577 in the C-terminal kinase domain of RSK2. In the present study, we demonstrate that RSK2 is associated in vivo with PP2Cdelta (protein phosphatase 2Cdelta). In epidermal growth factorstimulated cells, RSK2 is partially dephosphorylated on all four sites in an Mn2+-dependent manner, leading to reduced protein kinase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248321 |
Ser369 |
TAKTPKDsPGIPPSA |
Mus musculus |
|
| pmid |
sentence |
| 15206906 |
RSK2 (p90 ribosomal S6 kinase 2) is activated via the ERK (extracellular-signal-regulated kinase) pathway by phosphorylation on four sites: Ser227 in the activation loop of the N-terminal kinase domain, Ser369 in the linker, Ser386 in the hydrophobic motif and Thr577 in the C-terminal kinase domain of RSK2. In the present study, we demonstrate that RSK2 is associated in vivo with PP2Cdelta (protein phosphatase 2Cdelta). In epidermal growth factorstimulated cells, RSK2 is partially dephosphorylated on all four sites in an Mn2+-dependent manner, leading to reduced protein kinase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248322 |
Ser386 |
HQLFRGFsFVAITSD |
Mus musculus |
|
| pmid |
sentence |
| 15206906 |
RSK2 (p90 ribosomal S6 kinase 2) is activated via the ERK (extracellular-signal-regulated kinase) pathway by phosphorylation on four sites: Ser227 in the activation loop of the N-terminal kinase domain, Ser369 in the linker, Ser386 in the hydrophobic motif and Thr577 in the C-terminal kinase domain of RSK2. In the present study, we demonstrate that RSK2 is associated in vivo with PP2Cdelta (protein phosphatase 2Cdelta). In epidermal growth factorstimulated cells, RSK2 is partially dephosphorylated on all four sites in an Mn2+-dependent manner, leading to reduced protein kinase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248323 |
Thr577 |
AENGLLMtPCYTANF |
Mus musculus |
|
| pmid |
sentence |
| 15206906 |
RSK2 (p90 ribosomal S6 kinase 2) is activated via the ERK (extracellular-signal-regulated kinase) pathway by phosphorylation on four sites: Ser227 in the activation loop of the N-terminal kinase domain, Ser369 in the linker, Ser386 in the hydrophobic motif and Thr577 in the C-terminal kinase domain of RSK2. In the present study, we demonstrate that RSK2 is associated in vivo with PP2Cdelta (protein phosphatase 2Cdelta). In epidermal growth factorstimulated cells, RSK2 is partially dephosphorylated on all four sites in an Mn2+-dependent manner, leading to reduced protein kinase activity |
|
| Publications: |
4 |
Organism: |
Mus Musculus |
| + |
PPM1D | down-regulates activity
dephosphorylation
|
CHEK1 |
0.494 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248317 |
Ser345 |
LVQGISFsQPTCPDH |
Homo sapiens |
|
| pmid |
sentence |
| 15870257 |
Here we show that the oncogenic p53-induced serine/threonine phosphatase, PPM1D (or Wip1), dephosphorylates two ATM/ATR targets, Chk1 and p53. PPM1D binds Chk1 and dephosphorylates the ATR-targeted phospho-Ser 345, leading to decreased Chk1 kinase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1D | down-regulates
dephosphorylation
|
CHEK1 |
0.494 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135972 |
Ser345 |
LVQGISFsQPTCPDH |
Homo sapiens |
|
| pmid |
sentence |
| 15870257 |
Ppm1d dephosphorylates chk1 phospho-ser 345 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1D | up-regulates 
dephosphorylation
|
MDM2 |
0.667 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-158328 |
Ser395 |
SQESEDYsQPSTSSS |
Homo sapiens |
|
| pmid |
sentence |
| 17936559 |
Wip1 interacts with and dephosphorylates mdm2 at serine 395, a site phosphorylated by the atm kinase. Dephosphorylated mdm2 has increased stability and affinity for p53, facilitating p53 ubiquitination and degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1D | down-regulates quantity by destabilization
dephosphorylation
|
MDM2 |
0.667 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248324 |
Ser395 |
SQESEDYsQPSTSSS |
Homo sapiens |
|
| pmid |
sentence |
| 17936559 |
Here we show that the wild-type p53-induced phosphatase 1 (Wip1), or PPM1D, downregulates p53 protein levels by stabilizing Mdm2 and facilitating its access to p53. Wip1 interacts with and dephosphorylates Mdm2 at serine 395, a site phosphorylated by the ATM kinase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK1 | down-regulates quantity by destabilization
dephosphorylation
|
PPM1D |
0.359 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275489 |
Ser40 |
PTAEEKPsPRRSLSQ |
|
|
| pmid |
sentence |
| 33309518 |
Phosphorylation of multiple residues in the catalytic domain of PPM1D during mitosis, including Ser40 by Cyclin-dependent kinase 1 (CDK1), leads to ubiquitination of PPM1D and subsequent proteasomal degradation by Adenomatous polyposis coli (APC) and cell-division cycle protein 20 (CDC20) |
|
| Publications: |
1 |
| + |
CyclinB/CDK1 | down-regulates quantity by destabilization
dephosphorylation
|
PPM1D |
0.344 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275490 |
Ser40 |
PTAEEKPsPRRSLSQ |
|
|
| pmid |
sentence |
| 33309518 |
Phosphorylation of multiple residues in the catalytic domain of PPM1D during mitosis, including Ser40 by Cyclin-dependent kinase 1 (CDK1), leads to ubiquitination of PPM1D and subsequent proteasomal degradation by Adenomatous polyposis coli (APC) and cell-division cycle protein 20 (CDC20) |
|
| Publications: |
1 |
| + |
PPM1D | up-regulates quantity by stabilization
dephosphorylation
|
MDM4 |
0.45 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275491 |
Ser403 |
DLAHSSEsQETISSM |
|
|
| pmid |
sentence |
| 33309518 |
PPM1D also inhibits p53 activity by dephosphorylating Ser395 and stabilizing MDM2 and by dephosphorylating Ser403 on MDMX |
|
| Publications: |
1 |
| + |
HIPK2 | down-regulates quantity by destabilization
phosphorylation
|
PPM1D |
0.437 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275480 |
Ser54 |
QPLPPRPsPAALPGG |
|
|
| pmid |
sentence |
| 23871434 |
WIP1, a homeostatic regulator of the DNA damage response, is targeted by HIPK2 for phosphorylation and degradation|Analysis of the phosphoamino acids of WIP1 revealed that both Ser85 and Ser54 are phosphorylation sites, confirming that HIPK2 is a protein kinase for WIP1 phosphorylation at Ser54 as well as Ser85 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275481 |
Ser85 |
PLPDAGAsPAPSRCC |
|
|
| pmid |
sentence |
| 23871434 |
WIP1, a homeostatic regulator of the DNA damage response, is targeted by HIPK2 for phosphorylation and degradation|Analysis of the phosphoamino acids of WIP1 revealed that both Ser85 and Ser54 are phosphorylation sites, confirming that HIPK2 is a protein kinase for WIP1 phosphorylation at Ser54 as well as Ser85 |
|
| Publications: |
2 |
| + |
PPM1D | down-regulates
dephosphorylation
|
MAPK12 |
0.302 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135976 |
Thr183 |
RQADSEMtGYVVTRW |
Homo sapiens |
|
| pmid |
sentence |
| 15870257 |
Ppm1d selectively inhibits p38 activation by dephosphorylating thr 180. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1D | up-regulates activity
dephosphorylation
|
CHEK2 |
0.596 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248318 |
Thr68 |
SSLETVStQELYSIP |
in vitro |
|
| pmid |
sentence |
| 16311512 |
an in vitro phosphatase assay revealed that Wip1 (WT), but not Wip1 (D314A), dephosphorylates Thr68 on phosphorylated Chk2 in vitro, resulting in the inhibition of Chk2 kinase activity toward glutathione S-transferase-Cdc25C. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PPM1D | down-regulates
dephosphorylation
|
ATM |
0.511 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185135 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19360021 |
The negative regulator wip1 plays an important role in inhibiting atm, resulting in a pulse of atm activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1D | down-regulates activity
dephosphorylation
|
MAPK14 |
0.461 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84793 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11101524 |
Wip1 selectively inactivates p38 by specific dephosphorylation of its conserved threonine residue |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187770 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19713933 |
In addition, wip1 can dephosphorylate atm, as well as other components of the dna damage checkpoint, such as p38. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | P38 Signaling |
| + |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
PPM1D |
0.32 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275492 |
|
|
|
|
| pmid |
sentence |
| 33309518 |
Phosphorylation of multiple residues in the catalytic domain of PPM1D during mitosis, including Ser40 by Cyclin-dependent kinase 1 (CDK1), leads to ubiquitination of PPM1D and subsequent proteasomal degradation by Adenomatous polyposis coli (APC) and cell-division cycle protein 20 (CDC20) |
|
| Publications: |
1 |
3.0
PPM1D
- 
- 