+ |
CDC14A | down-regulates quantity by destabilization
dephosphorylation
|
KMT5A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248835 |
Ser100 |
SKIYSYMsPNKCSGM |
Homo sapiens |
|
pmid |
sentence |
20966048 |
The dephosphorylation of S29 during late mitosis by the Cdc14 phosphatases was required for APC(cdh1)-mediated ubiquitination of PR-Set7 and subsequent proteolysis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDC14A | up-regulates quantity by stabilization
dephosphorylation
|
WEE1 |
0.567 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267469 |
Ser123 |
EEGFGSSsPVKSPAA |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
23051732 |
In particular, we found that Cdc14A inhibits Wee1 degradation through the dephosphorylation of Ser-123 and Ser-139 residues. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267470 |
Ser139 |
YFLGSSFsPVRCGGP |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
23051732 |
In particular, we found that Cdc14A inhibits Wee1 degradation through the dephosphorylation of Ser-123 and Ser-139 residues. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CDC14A | up-regulates activity
dephosphorylation
|
IREB2 |
0.36 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248829 |
Ser157 |
LQKAGKLsPVKVQPK |
Homo sapiens |
|
pmid |
sentence |
18574241 |
IRP2 Ser-157 is phosphorylated by Cdk1/cyclin B1 during G(2)/M and is dephosphorylated during mitotic exit by the phosphatase Cdc14A. Ser-157 phosphorylation during G(2)/M reduces IRP2 RNA-binding activity and increases ferritin synthesis, whereas Ser-157 dephosphorylation during mitotic exit restores IRP2 RNA-binding activity and represses ferritin synthesis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDC14A | down-regulates activity
dephosphorylation
|
TP53 |
0.412 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248828 |
Ser315 |
LPNNTSSsPQPKKKP |
Homo sapiens |
|
pmid |
sentence |
10644693 |
The human Cdc14 phosphatases interact with and dephosphorylate the tumor suppressor protein p53|. Furthermore, the hCdc14 phosphatases were found to dephosphorylate p53 specifically at the p34Cdc2/clb phosphorylation site (p53-phosphor-Ser315)|Earlier studies showed that Ser315 phosphorylation increases the sequence-specific DNA binding capacity of p53, suggesting that Ser315 phosphorylation is an activating modification |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDC14A |
dephosphorylation
|
SIRT2 |
0.438 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248834 |
Ser368 |
PNPSTSAsPKKSPPP |
Homo sapiens |
|
pmid |
sentence |
17488717 |
Here, we demonstrate that SIRT2 is phosphorylated both in vitro and in vivo on serine 368 by the cell-cycle regulator, cyclin-dependent kinase 1, and dephosphorylated by the phosphatases CDC14A and CDC14B. Overexpression of SIRT2 mediates a delay in cellular proliferation that is dependent on serine 368 phosphorylation|Additionally, we found that SIRT2, like other Cdk1 targets, can be dephosphorylated by the phosphatases CDC14A and CDC14B. In contrast to a published report (8), we did not observe any degradation of SIRT2 by the 26 S proteasome in response to CDC14B overexpression|However, we cannot exclude the possibility that phosphorylation of serine 368 might affect the activity of SIRT2 on other unidentified acetylated substrates. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDC14A | down-regulates
dephosphorylation
|
MAPK6 |
0.625 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164404 |
Ser684 |
IGIPQFHsPVGSPLK |
Homo sapiens |
|
pmid |
sentence |
20236090 |
Using ms analysis, we identified four novel phosphorylation sites, ser684, ser688, thr698 and ser705, located at the extreme c-terminus of erk3.alanine substitution of the four c-terminal phosphorylation sites markedly decreased the half-life of erk3 in mitosis, thereby linking phosphorylation to the stabilization of the kinase.we found that the phosphatases cdc14a and cdc14b (cdc is cell-division cycle) bind to erk3 and reverse its c-terminal phosphorylation in mitosis. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164408 |
Ser688 |
QFHSPVGsPLKSIQA |
Homo sapiens |
|
pmid |
sentence |
20236090 |
Using ms analysis, we identified four novel phosphorylation sites, ser684, ser688, thr698 and ser705, located at the extreme c-terminus of erk3.alanine substitution of the four c-terminal phosphorylation sites markedly decreased the half-life of erk3 in mitosis, thereby linking phosphorylation to the stabilization of the kinase.we found that the phosphatases cdc14a and cdc14b (cdc is cell-division cycle) bind to erk3 and reverse its c-terminal phosphorylation in mitosis. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164412 |
Ser705 |
TPSAMKSsPQIPHQT |
Homo sapiens |
|
pmid |
sentence |
20236090 |
Using ms analysis, we identified four novel phosphorylation sites, ser684, ser688, thr698 and ser705, located at the extreme c-terminus of erk3.alanine substitution of the four c-terminal phosphorylation sites markedly decreased the half-life of erk3 in mitosis, thereby linking phosphorylation to the stabilization of the kinase.we found that the phosphatases cdc14a and cdc14b (cdc is cell-division cycle) bind to erk3 and reverse its c-terminal phosphorylation in mitosis. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164416 |
Thr698 |
KSIQATLtPSAMKSS |
Homo sapiens |
|
pmid |
sentence |
20236090 |
Using ms analysis, we identified four novel phosphorylation sites, ser684, ser688, thr698 and ser705, located at the extreme c-terminus of erk3.alanine substitution of the four c-terminal phosphorylation sites markedly decreased the half-life of erk3 in mitosis, thereby linking phosphorylation to the stabilization of the kinase.we found that the phosphatases cdc14a and cdc14b (cdc is cell-division cycle) bind to erk3 and reverse its c-terminal phosphorylation in mitosis. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
CDC14A | down-regulates quantity by destabilization
dephosphorylation
|
MAPK6 |
0.625 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248830 |
Ser684 |
IGIPQFHsPVGSPLK |
Homo sapiens |
|
pmid |
sentence |
20236090 |
Reciprocally, we found that the phosphatases Cdc14A and Cdc14B (Cdc is cell-division cycle) bind to ERK3 and reverse its C-terminal phosphorylation in mitosis. Importantly, alanine substitution of the four C-terminal phosphorylation sites markedly decreased the half-life of ERK3 in mitosis, thereby linking phosphorylation to the stabilization of the kinase.|In vitro phosphorylation of a series of ERK3-deletion mutants by mitotic cell extracts revealed that phosphorylation is confined to the unique C-terminal extension of the protein. Using MS analysis, we identified four novel phosphorylation sites, Ser684, Ser688, Thr698 and Ser705, located at the extreme C-terminus of ERK3. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248831 |
Ser688 |
QFHSPVGsPLKSIQA |
Homo sapiens |
|
pmid |
sentence |
20236090 |
Reciprocally, we found that the phosphatases Cdc14A and Cdc14B (Cdc is cell-division cycle) bind to ERK3 and reverse its C-terminal phosphorylation in mitosis. Importantly, alanine substitution of the four C-terminal phosphorylation sites markedly decreased the half-life of ERK3 in mitosis, thereby linking phosphorylation to the stabilization of the kinase.|In vitro phosphorylation of a series of ERK3-deletion mutants by mitotic cell extracts revealed that phosphorylation is confined to the unique C-terminal extension of the protein. Using MS analysis, we identified four novel phosphorylation sites, Ser684, Ser688, Thr698 and Ser705, located at the extreme C-terminus of ERK3. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248833 |
Ser705 |
TPSAMKSsPQIPHQT |
Homo sapiens |
|
pmid |
sentence |
20236090 |
Reciprocally, we found that the phosphatases Cdc14A and Cdc14B (Cdc is cell-division cycle) bind to ERK3 and reverse its C-terminal phosphorylation in mitosis. Importantly, alanine substitution of the four C-terminal phosphorylation sites markedly decreased the half-life of ERK3 in mitosis, thereby linking phosphorylation to the stabilization of the kinase.|In vitro phosphorylation of a series of ERK3-deletion mutants by mitotic cell extracts revealed that phosphorylation is confined to the unique C-terminal extension of the protein. Using MS analysis, we identified four novel phosphorylation sites, Ser684, Ser688, Thr698 and Ser705, located at the extreme C-terminus of ERK3. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248832 |
Thr698 |
KSIQATLtPSAMKSS |
Homo sapiens |
|
pmid |
sentence |
20236090 |
Reciprocally, we found that the phosphatases Cdc14A and Cdc14B (Cdc is cell-division cycle) bind to ERK3 and reverse its C-terminal phosphorylation in mitosis. Importantly, alanine substitution of the four C-terminal phosphorylation sites markedly decreased the half-life of ERK3 in mitosis, thereby linking phosphorylation to the stabilization of the kinase.|In vitro phosphorylation of a series of ERK3-deletion mutants by mitotic cell extracts revealed that phosphorylation is confined to the unique C-terminal extension of the protein. Using MS analysis, we identified four novel phosphorylation sites, Ser684, Ser688, Thr698 and Ser705, located at the extreme C-terminus of ERK3. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
BRAP | up-regulates activity
polyubiquitination
|
CDC14A |
0.343 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271777 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19152073 |
Brap2 promotes Lys-63 linked ubiquitination of HsCdc14A. Collectively, these results support the idea that Brap2 facilitates Lys-63 linked ubiquitin modification of HsCdc14A, which may not be targeted for degradation, but mainly for protein–protein interactions or other regulatory functions. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |