| + |
CDC14B | down-regulates quantity by destabilization 
dephosphorylation
|
KMT5A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248339 |
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 |
| + |
CDC14B | down-regulates quantity by destabilization
dephosphorylation
|
USP9X |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275613 |
Ser2547 |
YEGSEEVsPPQTKDQ |
|
|
| pmid |
sentence |
| 32152317 |
Here, we find that CDC14B antagonizes CDK1-mediated activating mitotic phosphorylation of the deubiquitinase USP9X at serine residue 2563, which we show to be essential for USP9X to mediate mitotic survival. Starting from an unbiased proteome-wide screening approach, we specify Wilms' tumor protein 1 (WT1) as the relevant substrate that becomes deubiquitylated and stabilized by serine 2563-phosphorylated USP9X in mitosis. |
|
| Publications: |
1 |
| + |
CDC14B | down-regulates activity
dephosphorylation
|
TP53 |
0.338 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248332 |
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 |
| + |
CDC14B |
dephosphorylation
|
SIRT2 |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248338 |
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 |
| + |
CDC14B | down-regulates quantity by destabilization
dephosphorylation
|
SKP2 |
0.364 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248333 |
Ser64 |
SNLGHPEsPPRKRLK |
Homo sapiens |
|
| pmid |
sentence |
| 18239684 |
The activity of SCF(Skp2) is regulated by the Cyclin-dependent kinase (CDK)2-mediated phosphorylation of Skp2 on Ser64 allows its expression in mid-G1 phase, even in the presence of active APC(Cdh1). Reciprocally, dephosphorylation of Skp2 by the mitotic phosphatase Cdc14B at the M --> G1 transition promotes its degradation by APC(Cdh1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC14B | down-regulates quantity by destabilization
dephosphorylation
|
MAPK6 |
0.552 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248334 |
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-248335 |
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-248337 |
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-248336 |
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 |
| + |
CDC14B | down-regulates
dephosphorylation
|
MAPK6 |
0.552 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164471 |
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-164475 |
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-164479 |
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-164483 |
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 |
| + |
CDC14B | up-regulates activity 
dephosphorylation
|
CDH1 |
0.318 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277017 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18662541 |
Cdc14B activates APC/C Cdh1 after DNA damage in G2.|Importantly, after DNA damage, thein vivo phosphorylation of wild type Cdh1 - but not that of Cdh1 (4xA) - increased after Cdc14B silencing (XREF_FIG), indicating that in response to genotoxic stress, Cdc14B dephosphorylates Cdh1 on the four sites phosphorylated by Cdk2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC14B | up-regulates
dephosphorylation
|
APC |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179636 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18662541 |
The phosphatase cdc14b translocates from the nucleolus to the nucleoplasm and induces the activation of the ubiquitin ligase apc/ccdh1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC14B | up-regulates
dephosphorylation
|
CDCA3 |
0.286 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179664 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18662541 |
The phosphatase cdc14b translocates from the nucleolus to the nucleoplasm and induces the activation of the ubiquitin ligase apc/ccdh1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC14B | up-regulates activity
dephosphorylation
|
TAF1C |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277135 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26023773 |
Consistent with prior studies showing that the phosphatase hCdc14B regulates progression through mitosis by counteracting mitotic phosphorylation by Cdk1/cyclin B [ ], hCdc14B dephosphorylates TAFI110, thus promoting its reactivation as cells exit mitosis.|Here we show that hCdc14B, the phosphatase that regulates Cdk1/cyclin B activity and progression through mitosis, promotes reactivation of rDNA transcription by dephosphorylating TAFI110. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC14B | up-regulates
dephosphorylation
|
GSK3B/Axin/APC |
0.255 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-227927 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18662541 |
The phosphatase cdc14b translocates from the nucleolus to the nucleoplasm and induces the activation of the ubiquitin ligase apc/ccdh1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CDC14B
- 
- 