| + |
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 |
0.562 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276952 |
Ser123 |
EEGFGSSsPVKSPAA |
Homo sapiens |
|
| pmid |
sentence |
| 23051732 |
However, when both Ser-123 and Ser-139 were modified (2A), although Wee1 was still phosphorylated by Cdk1, treatment with active Cdc14A did not decrease the phosphorylation signal to any significant extent ( xref , lane 5), indicating that Cdc14A dephosphorylates Wee1 at Ser-123 and Ser-139 residues.|Our results indicate that Wee1 is a substrate of Cdc14 phosphatases in human cells and that by reversing specific Cdk1 phosphorylation, the Cdc14A isoform induces Wee1 stability, which in turn directly inhibits Cdk1 activity. |
|
| 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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276953 |
Ser139 |
YFLGSSFsPVRCGGP |
Homo sapiens |
|
| pmid |
sentence |
| 23051732 |
However, when both Ser 123 and Ser 139 were modified (2A), although Wee1 was still phosphorylated by Cdk1, treatment with active Cdc14A did not decrease the phosphorylation signal to any significant extent (XREF_FIG, lane 5), indicating that Cdc14A dephosphorylates Wee1 at Ser 123 and Ser 139 residues.|Our results indicate that Wee1 is a substrate of Cdc14 phosphatases in human cells and that by reversing specific Cdk1 phosphorylation, the Cdc14A isoform induces Wee1 stability, which in turn directly inhibits Cdk1 activity. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CDC14A | up-regulates activity
dephosphorylation
|
IREB2 |
0.356 |
| 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 |
0.41 |
| 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 |
0.433 |
| 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 quantity by destabilization
dephosphorylation
|
MAPK6 |
0.627 |
| 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 |
| + |
CDC14A | down-regulates
dephosphorylation
|
MAPK6 |
0.627 |
| 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 |
| + |
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 |
| + |
CDC14A | down-regulates activity
dephosphorylation
|
SPAG5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277066 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27325694 |
We also demonstrate that Cdc14A dephosphorylates Astrin, and therefore the overexpression of Cdc14A sequesters Astrin in the centrosome and results in aberrant chromosome alignment. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC14A | down-regulates activity 
dephosphorylation
|
CDC25A |
0.518 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277065 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20956543 |
Cdc14A inhibits Cdc25A and Cdc25B activity, the latter through direct binding and dephosphorylation ( ).|Indeed, in vitro dephosphorylation of Cdk1-cyclin B1-phosphorylated Cdc25A by Cdc14A did not inhibit its catalytic activity (data not shown).|Taken together, our results suggest that at the G2/M transition Cdc14A acts on an unknown protein, which in turn inhibits Cdc25A phosphatase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC14A | down-regulates activity
dephosphorylation
|
CDC25B |
0.577 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276968 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20956543 |
Cdc14A inhibits Cdc25A and Cdc25B activity, the latter through direct binding and dephosphorylation ( ).|Together, these data indicate that Cdc14A dephosphorylates Cdc25B, inhibiting its catalytic activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CDC14A
- 
- 