+ |
CTDP1 | down-regulates activity
dephosphorylation
|
MASTL |
0.446 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276971 |
Ser453 |
NFELVDSsPCKKIIQ |
Homo sapiens |
|
pmid |
sentence |
26653855 |
Taken together, these data suggest that Fcp1 bound and dephosphorylated Gwl at S90 and S453, and possibly at other Cdk1 dependent sites, during mitosis exit and that Fcp1 catalyzed dephosphorylation lowered Gwl activity towards Ensa and ARPP19, allowing PP2A-B55 to autoactivate.|Together, these data indicate that Fcp1 dependent dephosphorylation greatly reduces S67-Ensa kinase activity of Gwl and that, downstream inactivation of Cdk1, Fcp1 deficit substantially blunts inactivation of Gwl. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276972 |
Ser90 |
DALALSKsPFIVHLY |
Homo sapiens |
|
pmid |
sentence |
26653855 |
Taken together, these data suggest that Fcp1 bound and dephosphorylated Gwl at S90 and S453, and possibly at other Cdk1 dependent sites, during mitosis exit and that Fcp1 catalyzed dephosphorylation lowered Gwl activity towards Ensa and ARPP19, allowing PP2A-B55 to autoactivate.|Together, these data indicate that Fcp1 dependent dephosphorylation greatly reduces S67-Ensa kinase activity of Gwl and that, downstream inactivation of Cdk1, Fcp1 deficit substantially blunts inactivation of Gwl. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
MASTL | up-regulates activity
phosphorylation
|
ARPP19 |
0.721 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-243611 |
Ser62 |
KGQKYFDsGDYNMAK |
in vitro |
|
pmid |
sentence |
21164014 |
We identified cyclic adenosine monophosphateregulated phosphoprotein 19 (Arpp19) and -Endosulfine as two substrates of Gwl that, when phosphorylated by this kinase, associate with and inhibit PP2A, thus promoting mitotic entry. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
MASTL | up-regulates activity
phosphorylation
|
ENSA |
0.723 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-243690 |
Ser67 |
KGQKYFDsGDYNMAK |
in vitro |
|
pmid |
sentence |
21164014 |
We identified cyclic adenosine monophosphateregulated phosphoprotein 19 (Arpp19) and -Endosulfine as two substrates of Gwl that, when phosphorylated by this kinase, associate with and inhibit PP2A, thus promoting mitotic entry. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
MASTL | up-regulates activity
phosphorylation
|
MASTL |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-243409 |
Ser875 |
TAQHLTVsGFSL |
Xenopus laevis |
|
pmid |
sentence |
22354989 |
After this priming step, Gwl can intramolecularly phosphorylate its C-terminal tail at pS883; this site probably plays a role similar to that of the tail/Z motif of other AGC kinases. |
|
Publications: |
1 |
Organism: |
Xenopus Laevis |
+ |
CyclinB/CDK1 | up-regulates activity
phosphorylation
|
MASTL |
0.511 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-243403 |
Thr194 |
NMMDILTtPSMAKPR |
Xenopus laevis |
|
pmid |
sentence |
22354989 |
We propose a model in which the initiating event for Gwl activation is phosphorylation by MPF of the proline-directed sites T193 and T206 in the presumptive activation loop |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249652 |
Thr207 |
PRQDYSRtPGQVLSL |
Xenopus laevis |
|
pmid |
sentence |
22354989 |
We propose a model in which the initiating event for Gwl activation is phosphorylation by MPF of the proline-directed sites T193 and T206 in the presumptive activation loop |
|
Publications: |
2 |
Organism: |
Xenopus Laevis |
+ |
PP2CA_R1A_R2A | down-regulates activity
dephosphorylation
|
MASTL |
0.481 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276615 |
Thr194 |
NMMDILTtPSMAKPR |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
24391510 |
We demonstrate that PP2A/B55 is required for Gwl dephosphorylation at the essential Cdk site Thr194.Gwl phosphorylation by CycA/Cdk2 in vitro. Flag WT and Thr194A Gwl was transiently expressed and purified from asynchronous HEK 293T cells and incubated with recombinant CycA/Cdk2, following treatment with alkaline phosphatase (aPh) in the indicated samples. The proteins were analysed by immuno-blotting with anti-Gwl and Gwl pThr194 antibodies |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK1 | up-regulates activity
phosphorylation
|
MASTL |
0.492 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-243414 |
Thr194 |
NMMDILTtPSMAKPR |
Xenopus laevis |
|
pmid |
sentence |
22354989 |
We propose a model in which the initiating event for Gwl activation is phosphorylation by MPF of the proline-directed sites T193 and T206 in the presumptive activation loop |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249653 |
Thr207 |
PRQDYSRtPGQVLSL |
Xenopus laevis |
|
pmid |
sentence |
22354989 |
We propose a model in which the initiating event for Gwl activation is phosphorylation by MPF of the proline-directed sites T193 and T206 in the presumptive activation loop |
|
Publications: |
2 |
Organism: |
Xenopus Laevis |
+ |
CyclinA2/CDK2 | up-regulates activity
phosphorylation
|
MASTL |
0.278 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276614 |
Thr194 |
NMMDILTtPSMAKPR |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
24391510 |
We demonstrate that PP2A/B55 is required for Gwl dephosphorylation at the essential Cdk site Thr194.Gwl phosphorylation by CycA/Cdk2 in vitro. Flag WT and Thr194A Gwl was transiently expressed and purified from asynchronous HEK 293T cells and incubated with recombinant CycA/Cdk2, following treatment with alkaline phosphatase (aPh) in the indicated samples. The proteins were analysed by immuno-blotting with anti-Gwl and Gwl pThr194 antibodies |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT1 | up-regulates activity
phosphorylation
|
MASTL |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277515 |
Thr299 |
QSRKRLAtSSASSQS |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
32123010 |
Here, we report that AKT phosphorylates MASTL at residue T299, which plays a critical role in its activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |