+ |
PPM1D | down-regulates activity
dephosphorylation
|
KDM1A |
0.478 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276904 |
Ser131 |
DESLANLsEDEYYSE |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
25999347 |
We demonstrated here that phosphorylation and dephosphorylation of LSD1 at S131 and S137 was mediated by casein kinase 2 (CK2) and wild-type p53-induced phosphatase 1 (WIP1), respectively. LSD1, RNF168 and 53BP1 interacted with each other directly. CK2-mediated phosphorylation of LSD1 exhibited no impact on its interaction with 53BP1, but promoted its interaction with RNF168 and RNF168-dependent 53BP1 ubiquitination and subsequent recruitment to the DNA damage sites. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276905 |
Ser137 |
LSEDEYYsEEERNAK |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
25999347 |
We demonstrated here that phosphorylation and dephosphorylation of LSD1 at S131 and S137 was mediated by casein kinase 2 (CK2) and wild-type p53-induced phosphatase 1 (WIP1), respectively. LSD1, RNF168 and 53BP1 interacted with each other directly. CK2-mediated phosphorylation of LSD1 exhibited no impact on its interaction with 53BP1, but promoted its interaction with RNF168 and RNF168-dependent 53BP1 ubiquitination and subsequent recruitment to the DNA damage sites. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PPM1D | down-regulates activity
dephosphorylation
|
CDKN1B |
0.263 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277109 |
Ser140 |
PKTDPSDsQTGLAEQ |
Homo sapiens |
|
pmid |
sentence |
31959038 |
Increased expression of wildtype WIP1 reduces stability of p27 Kip1 while increased expression of similar amounts of phosphatase-dead WIP1 has no effect on p27 Kip1 protein stability.|We demonstrate that wildtype, but not phosphatase-dead WIP1, efficiently dephosphorylates p27 Kip1 Ser140 both in vitro and in cells and that this dephosphorylation is sensitive to the WIP1 specific inhibitor GSK 2830371. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
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 |
0.576 |
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 quantity by destabilization
dephosphorylation
|
TP53 |
0.576 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276943 |
Ser15 |
PSVEPPLsQETFSDL |
Homo sapiens |
|
pmid |
sentence |
18265945 |
Dephosphorylation of p53 at serine 15 by Wip1 also contributes to p53 degradation, as does dephosphorylation of Mdm2, which stabilizes Mdm2, an E3 ubiquitin ligase specific for p53 [ xref ]. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | P38 Signaling |
+ |
PPM1D | down-regulates activity
dephosphorylation
|
TP53 |
0.576 |
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 | up-regulates activity
dephosphorylation
|
RBM38 |
0.372 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277020 |
Ser195 |
DQYPYAAsPATAASF |
Homo sapiens |
|
pmid |
sentence |
25823026 |
Interestingly, we showed that PPM1D directly interacts with and dephosphorylates RBM38 at serine 195. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPM1D | down-regulates activity
dephosphorylation
|
ATM |
0.504 |
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 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276954 |
Ser1981 |
SLAFEEGsQSTTISS |
Homo sapiens |
|
pmid |
sentence |
18265945 |
More recently, Shreeram et al. have also shown that Wip1 dephosphorylates human ATM at Ser367 as well as Ser1981.|Thus, overexpression of Wip1 in an oncogenic context could contribute to tumor promotion by inhibiting both p53 and ATM functions. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276955 |
Ser367 |
DTRSLEIsQSYTTTQ |
Homo sapiens |
|
pmid |
sentence |
18265945 |
More recently, Shreeram et al. have also shown that Wip1 dephosphorylates human ATM at Ser367 as well as Ser1981.|Thus, overexpression of Wip1 in an oncogenic context could contribute to tumor promotion by inhibiting both p53 and ATM functions. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
PPM1D | down-regulates activity
dephosphorylation
|
RPS6KA3 |
0.369 |
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 |
0.487 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276986 |
Ser345 |
LVQGISFsQPTCPDH |
Homo sapiens |
|
pmid |
sentence |
18265945 |
Because Chk1 phosphorylates and activates p53, the inhibition of Chk1 by Wip1 also places Wip1 in a negative feedback regulatory loop for p53 .|In vitro phosphatase assays showed that Wip1 dephosphorylated Chk1 at Ser345, but not Ser317. |
|
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: |
2 |
Organism: |
Homo Sapiens |
+ |
PPM1D | down-regulates
dephosphorylation
|
CHEK1 |
0.487 |
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 | down-regulates quantity by destabilization
dephosphorylation
|
MDM2 |
0.669 |
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 |
+ |
PPM1D | up-regulates
dephosphorylation
|
MDM2 |
0.669 |
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 |
+ |
CDK1 | down-regulates quantity by destabilization
dephosphorylation
|
PPM1D |
0.355 |
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 |
0.341 |
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 |
0.444 |
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 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276951 |
Ser403 |
DLAHSSEsQETISSM |
Homo sapiens |
|
pmid |
sentence |
19808970 |
Here, we present evidence that Wip1 specifically dephosphorylates MdmX at Ser403 and indirectly suppresses phosphorylation of MdmX at Ser342 and Ser376.|Thus, Wip1 may need to be inhibited in the early stage of DNA damage response to facilitate rapid MdmX degradation. |
|
Publications: |
2 |
Organism: |
, Homo Sapiens |
+ |
HIPK2 | down-regulates quantity by destabilization
phosphorylation
|
PPM1D |
0.431 |
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 |
0.301 |
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 | down-regulates activity
dephosphorylation
|
TP53BP1 |
0.402 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277046 |
Thr543 |
IDEDGENtQIEDTEP |
Homo sapiens |
|
pmid |
sentence |
31619012 |
In addition, WIP1 dephosphorylates 53BP1 at Threonine 543 that was previously implicated in mediating interaction with RIF1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPM1D | up-regulates activity
dephosphorylation
|
CHEK2 |
0.59 |
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 activity
dephosphorylation
|
MAPK14 |
0.456 |
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. |
|
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 |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | P38 Signaling |
+ |
PPM1D | down-regulates activity
dephosphorylation
|
GPI |
0.241 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277155 |
|
|
Homo sapiens |
|
pmid |
sentence |
28185954 |
The WIP1 mediated inhibition of NLK activity markedly decreased the phosphorylation of lymphoid enhancer binding factor 1 (LEF1), enhancing its interaction with beta-catenin.|Wip1 directly dephosphorylates NLK and increases Wnt activity during germ cell development. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPM1D | down-regulates
dephosphorylation
|
ATM |
0.504 |
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 |
+ |
ACSS2 | up-regulates quantity by expression
transcriptional regulation
|
PPM1D |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276560 |
|
|
|
|
pmid |
sentence |
28552616 |
As expected, we found that glucose deprivation induced the binding of TFEB (Figure S4C) and ACSS2 (Figure S4D) to the promoter regions of MAP1LC3B, ATG3, and WIPI-1 as well as mRNA (Figure 3H) and protein (Figure 3I) expression of these genes; |
|
Publications: |
1 |
+ |
PPM1D | down-regulates activity
dephosphorylation
|
BAX |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276993 |
|
|
Homo sapiens |
|
pmid |
sentence |
23907458 |
34 In this study, a novel function of Wip1 was identified, that is, its ability to dephosphorylate directly and thus inactivate apoptotic BAX protein in response to gamma irradiation.|To ascertain whether Wip1 dephosphorylates BAX, recombinant Wip1 was incubated with previously reported BAX-derived phosphopeptides containing Ser87, Ser163, Thr167, and Ser184 in an in vitro phosphatase assay. xref , xref Peptides containing phospho-Thr180 from p38 MAPK and phospho-Thr31 from UNG2 were used as a positive and negative control, respectively. xref As shown in xref , purified Wip1 did not dephosphorylate the four BAX-derived phosphopeptides. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPM1D | down-regulates activity
dephosphorylation
|
UNG |
0.387 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277156 |
|
|
Homo sapiens |
|
pmid |
sentence |
15327777 |
PPM1D dephosphorylation of UNG2 is correlated with reduced UNG2 activity on uracil-containing templates.|This result suggests that PPM1D specifically inhibits UNG2 and not other uracil DNA glycosylases. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TFEB | up-regulates quantity by expression
transcriptional regulation
|
PPM1D |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276557 |
|
|
|
|
pmid |
sentence |
28552616 |
As expected, we found that glucose deprivation induced the binding of TFEB (Figure S4C) and ACSS2 (Figure S4D) to the promoter regions of MAP1LC3B, ATG3, and WIPI-1 as well as mRNA (Figure 3H) and protein (Figure 3I) expression of these genes; |
|
Publications: |
1 |
+ |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
PPM1D |
0.318 |
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 |
+ |
PPM1D | up-regulates activity
dephosphorylation
|
RUNX2 |
0.456 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277110 |
|
|
Homo sapiens |
|
pmid |
sentence |
23907458 |
Activating dephosphorylation of RUNX2 by Wip1 increases its transcriptional activity on the Bax promoter. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |