| + |
CDK1 | up-regulates 
phosphorylation
|
CDC25C |
0.866 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78416 |
Ser122 |
DQHLMKCsPAQLLCS |
Homo sapiens |
|
| pmid |
sentence |
| 10864927 |
Activation of human cdc25c at the g2/m transition occurs concomitantly with phosphorylation of five serine/threonine-proline sites: thr48, thr67, ser122, thr130, and ser214, presumably by cdc2-cyclin b. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-64960 |
Ser214 |
SRSGLYRsPSMPENL |
Homo sapiens |
|
| pmid |
sentence |
| 10037602 |
Phosphorylation at thr-48, thr-67, ser-122, thr-130, ser-168 and ser-214 occurs at g2 and g2-m transition and is catalyzed by cdk1. Ser-168 phosphorylation levels are lower than those at the other 5 cdk1 sites. Phosphorylation by cdk1 leads to increased activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-36267 |
Ser214 |
SRSGLYRsPSMPENL |
Homo sapiens |
|
| pmid |
sentence |
| 8119945 |
Phosphorylation at thr-48, thr-67, ser-122, thr-130, ser-168 and ser-214 occurs at g2 and g2-m transition and is catalyzed by cdk1. Ser-168 phosphorylation levels are lower than those at the other 5 cdk1 sites. Phosphorylation by cdk1 leads to increased activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78420 |
Ser214 |
SRSGLYRsPSMPENL |
Homo sapiens |
|
| pmid |
sentence |
| 10864927 |
Activation of human cdc25c at the g2/m transition occurs concomitantly with phosphorylation of five serine/threonine-proline sites: thr48, thr67, ser122, thr130, and ser214, presumably by cdc2-cyclin b. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78424 |
Thr130 |
PAQLLCStPNGLDRG |
Homo sapiens |
|
| pmid |
sentence |
| 10864927 |
Activation of human cdc25c at the g2/m transition occurs concomitantly with phosphorylation of five serine/threonine-proline sites: thr48, thr67, ser122, thr130, and ser214, presumably by cdc2-cyclin b. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78428 |
Thr48 |
VCPDVPRtPVGKFLG |
Homo sapiens |
|
| pmid |
sentence |
| 10864927 |
Activation of human cdc25c at the g2/m transition occurs concomitantly with phosphorylation of five serine/threonine-proline sites: thr48, thr67, ser122, thr130, and ser214, presumably by cdc2-cyclin b. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-36271 |
Thr48 |
VCPDVPRtPVGKFLG |
Homo sapiens |
|
| pmid |
sentence |
| 8119945 |
Phosphorylation at thr-48, thr-67, ser-122, thr-130, ser-168 and ser-214 occurs at g2 and g2-m transition and is catalyzed by cdk1. Ser-168 phosphorylation levels are lower than those at the other 5 cdk1 sites. Phosphorylation by cdk1 leads to increased activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-64964 |
Thr48 |
VCPDVPRtPVGKFLG |
Homo sapiens |
|
| pmid |
sentence |
| 10037602 |
Phosphorylation at thr-48, thr-67, ser-122, thr-130, ser-168 and ser-214 occurs at g2 and g2-m transition and is catalyzed by cdk1. Ser-168 phosphorylation levels are lower than those at the other 5 cdk1 sites. Phosphorylation by cdk1 leads to increased activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-64968 |
Thr67 |
LSILSGGtPKRCLDL |
Homo sapiens |
|
| pmid |
sentence |
| 10037602 |
Phosphorylation at thr-48, thr-67, ser-122, thr-130, ser-168 and ser-214 occurs at g2 and g2-m transition and is catalyzed by cdk1. Ser-168 phosphorylation levels are lower than those at the other 5 cdk1 sites. Phosphorylation by cdk1 leads to increased activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78432 |
Thr67 |
LSILSGGtPKRCLDL |
Homo sapiens |
|
| pmid |
sentence |
| 10864927 |
Activation of human cdc25c at the g2/m transition occurs concomitantly with phosphorylation of five serine/threonine-proline sites: thr48, thr67, ser122, thr130, and ser214, presumably by cdc2-cyclin b. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-36275 |
Thr67 |
LSILSGGtPKRCLDL |
Homo sapiens |
|
| pmid |
sentence |
| 8119945 |
Phosphorylation at thr-48, thr-67, ser-122, thr-130, ser-168 and ser-214 occurs at g2 and g2-m transition and is catalyzed by cdk1. Ser-168 phosphorylation levels are lower than those at the other 5 cdk1 sites. Phosphorylation by cdk1 leads to increased activity. |
|
| Publications: |
11 |
Organism: |
Homo Sapiens |
| + |
CyclinB/CDK1 | up-regulates
phosphorylation
|
CDC25C |
0.854 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216741 |
Ser122 |
DQHLMKCsPAQLLCS |
Homo sapiens |
|
| pmid |
sentence |
| 10864927 |
Activation of human cdc25c at the g2/m transition occurs concomitantly with phosphorylation of five serine/threonine-proline sites: thr48, thr67, ser122, thr130, and ser214, presumably by cdc2-cyclin b. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216765 |
Ser214 |
SRSGLYRsPSMPENL |
Homo sapiens |
|
| pmid |
sentence |
| 10864927 |
Activation of human cdc25c at the g2/m transition occurs concomitantly with phosphorylation of five serine/threonine-proline sites: thr48, thr67, ser122, thr130, and ser214, presumably by cdc2-cyclin b. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216769 |
Thr130 |
PAQLLCStPNGLDRG |
Homo sapiens |
|
| pmid |
sentence |
| 10864927 |
Activation of human cdc25c at the g2/m transition occurs concomitantly with phosphorylation of five serine/threonine-proline sites: thr48, thr67, ser122, thr130, and ser214, presumably by cdc2-cyclin b. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216773 |
Thr48 |
VCPDVPRtPVGKFLG |
Homo sapiens |
|
| pmid |
sentence |
| 10864927 |
Activation of human cdc25c at the g2/m transition occurs concomitantly with phosphorylation of five serine/threonine-proline sites: thr48, thr67, ser122, thr130, and ser214, presumably by cdc2-cyclin b. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216777 |
Thr67 |
LSILSGGtPKRCLDL |
Homo sapiens |
|
| pmid |
sentence |
| 10864927 |
Activation of human cdc25c at the g2/m transition occurs concomitantly with phosphorylation of five serine/threonine-proline sites: thr48, thr67, ser122, thr130, and ser214, presumably by cdc2-cyclin b. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
MAPK9 | down-regulates 
phosphorylation
|
CDC25C |
0.369 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164093 |
Ser168 |
SEMKYLGsPITTVPK |
Homo sapiens |
|
| pmid |
sentence |
| 20220133 |
Here we show that jnk directly phosphorylates cdc25c at serine 168 during g(2) phase of the cell cycle. Cdc25c phosphorylation by jnk negatively regulates its phosphatase activity and thereby cdk1 activation, enabling a timely control of mitosis onset. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK10 | down-regulates
phosphorylation
|
CDC25C |
0.244 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164085 |
Ser168 |
SEMKYLGsPITTVPK |
Homo sapiens |
|
| pmid |
sentence |
| 20220133 |
Here we show that jnk directly phosphorylates cdc25c at serine 168 during g(2) phase of the cell cycle. Cdc25c phosphorylation by jnk negatively regulates its phosphatase activity and thereby cdk1 activation, enabling a timely control of mitosis onset. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK1 | down-regulates
phosphorylation
|
CDC25C |
0.866 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-36279 |
Ser168 |
SEMKYLGsPITTVPK |
Homo sapiens |
|
| pmid |
sentence |
| 8119945 |
Phosphorylation at thr-48, thr-67, ser-122, thr-130, ser-168 and ser-214 occurs at g2 and g2-m transition and is catalyzed by cdk1. Ser-168 phosphorylation levels are lower than those at the other 5 cdk1 sites. Phosphorylation by cdk1 leads to increased activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-64972 |
Ser168 |
SEMKYLGsPITTVPK |
Homo sapiens |
|
| pmid |
sentence |
| 10037602 |
Phosphorylation at thr-48, thr-67, ser-122, thr-130, ser-168 and ser-214 occurs at g2 and g2-m transition and is catalyzed by cdk1. Ser-168 phosphorylation levels are lower than those at the other 5 cdk1 sites. Phosphorylation by cdk1 leads to increased activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK8 | down-regulates
phosphorylation
|
CDC25C |
0.407 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164089 |
Ser168 |
SEMKYLGsPITTVPK |
Homo sapiens |
|
| pmid |
sentence |
| 20220133 |
Here we show that jnk directly phosphorylates cdc25c at serine 168 during g(2) phase of the cell cycle. Cdc25c phosphorylation by jnk negatively regulates its phosphatase activity and thereby cdk1 activation, enabling a timely control of mitosis onset. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK3 | up-regulates
phosphorylation
|
CDC25C |
0.743 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122090 |
Ser191 |
EDQAEEIsDELMEFS |
Homo sapiens |
|
| pmid |
sentence |
| 14968113 |
Cdc25c phosphorylation on serine 191 by plk3 promotes its nuclear translocation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122094 |
Ser198 |
SDELMEFsLKDQEAK |
Homo sapiens |
|
| pmid |
sentence |
| 14968113 |
Cdc25c phosphorylation on serine 191 by plk3 promotes its nuclear translocation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates
phosphorylation
|
CDC25C |
0.815 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-115993 |
Ser198 |
SDELMEFsLKDQEAK |
Homo sapiens |
|
| pmid |
sentence |
| 11897663 |
The nuclear accumulation of active m-phase promoting factor (mpf) during prophase is thought to be essential for coordinating m-phase events in vertebrate cells. The protein phosphatase cdc25c, an activator of mpf, enters the nucleus to keep mpf active in the nucleus during prophase. these results suggest that plk1 phosphorylates cdc25c on ser198 and regulates nuclear translocation of cdc25c during prophase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CyclinE/CDK2 | up-regulates
phosphorylation
|
CDC25C |
0.595 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216721 |
Ser214 |
SRSGLYRsPSMPENL |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 20530684 |
The cyclin e/cdk2 complex phosphorylates cdc25c on ser(214), leading to its premature activation, which coincides with higher cyclin b/cdk1 and polo-like kinase 1 (plk1) activities in an s-phase-enriched population that result in faster mitotic entry. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK2 | up-regulates
phosphorylation
|
CDC25C |
0.761 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165872 |
Ser214 |
SRSGLYRsPSMPENL |
Homo sapiens |
|
| pmid |
sentence |
| 20530684 |
The cyclin e/cdk2 complex phosphorylates cdc25c on ser(214), leading to its premature activation, which coincides with higher cyclin b/cdk1 and polo-like kinase 1 (plk1) activities in an s-phase-enriched population that result in faster mitotic entry. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRSK1 | down-regulates
phosphorylation
|
CDC25C |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-56473 |
Ser216 |
SGLYRSPsMPENLNR |
Homo sapiens |
|
| pmid |
sentence |
| 9543386 |
Overexpression of hssad1 resulted in an increased phosphorylation of cdc25c on ser-216 in vivo.Phosphorylation of cdc25 triggers cell-cycle arrest by the sequestration of cdc25 by 14-3-3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHEK2 | down-regulates activity
phosphorylation
|
CDC25C |
0.864 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102779 |
Ser216 |
SGLYRSPsMPENLNR |
Homo sapiens |
|
| pmid |
sentence |
| 12835754 |
Activated chk2 in turn phosphorylates cdc25c at serine-216 contributing to the g2/m checkpoints. Cds1 phosphorylates and inactivates cdc25 in vitro|CDC25C is phosphorylated on Ser 216 throughout interphase, but not in mitosis. This creates a binding site for 14‐3‐3 proteins | It has been suggested that 14‐3‐3 protein binding is responsible for retaining Cdc25C in the cytoplasm during interphase, thereby contributing to the prevention of premature initiation of mitotic events |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK14 | down-regulates activity
phosphorylation
|
CDC25C |
0.428 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250091 |
Ser216 |
SGLYRSPsMPENLNR |
in vitro |
|
| pmid |
sentence |
| 9543386 |
P38 binds and phosphorylates Cdc25B at serines 309 and 361, and Cdc25C at serine 216; phosphorylation of these residues is required for binding to 14-3-3 proteins. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
BRSK1 | down-regulates activity
phosphorylation
|
CDC25C |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107408 |
Ser216 |
SGLYRSPsMPENLNR |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15150265 |
Overexpression of hssad1 resulted in an increased phosphorylation of cdc25c on ser-216 in vivo. Phosphorylation of cdc25 triggers cell-cycle arrest by the sequestration of cdc25 by 14-3-3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK3 |
phosphorylation
|
CDC25C |
0.743 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249030 |
Ser216 |
SGLYRSPsMPENLNR |
in vitro |
|
| pmid |
sentence |
| 10557092 |
The physical association and phosphorylation of Cdc25C protein phosphatase by Prk. | Further studies reveal that His6-Prk phosphorylates Cdc25C on serine216, a residue also phosphorylated by Chk1 and Chk2. Together, these observations strongly suggest that Prk's role in mitosis is at least partly mediated through direct regulation of Cdc25C. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
p38 | down-regulates activity
phosphorylation
|
CDC25C |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107420 |
Ser216 |
SGLYRSPsMPENLNR |
Homo sapiens |
|
| pmid |
sentence |
| 11333986 |
P38 binds and phosphorylates cdc25-b and -c at serines 309 and 361 and at serine 216, respectively, and phosphorylation of these residues is required for binding to 14-3-3 proteins phosphorylation of cdc25 triggers cell-cycle arrest by the sequestration of cdc25 by 14-3-3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PKN1 |
phosphorylation
|
CDC25C |
0.548 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249277 |
Ser216 |
SGLYRSPsMPENLNR |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15791647 |
A role for PKN1 in mediating arsenite-induced G(2)/M delay was supported by the finding that expression of a constitutively active form of PKN1 (PKN1AF3) in HeLa cells delayed the mitotic entry of cell cycle. Further experiments indicate that PKN1 directly phosphorylated serine 216 (Ser216) in Cdc25C, which then facilitated association between Cdc25C and 14-3-3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHEK1 | down-regulates quantity by destabilization
phosphorylation
|
CDC25C |
0.858 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163158 |
Ser216 |
SGLYRSPsMPENLNR |
Homo sapiens |
|
| pmid |
sentence |
| 20068082 |
The signal for ubiquitination after uv and ir exposure is created by phosphorylation of cdc25a mediated by chk1 and chk2, respectively. Chk1 is a major kinase phosphorylating cdc25a (ser76/124) and cdc25c (ser216). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATR | up-regulates activity
phosphorylation
|
CDC25C |
0.659 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279008 |
Ser216 |
SGLYRSPsMPENLNR |
Homo sapiens |
|
| pmid |
sentence |
| 28264028 |
We also found that activated ATR phosphorylates CDC25C (Cell Division Cycle 25C) at serine 216, which in turn inactivates the cyclin B1/Cyclin-Dependent Kinase 1(CDK1) complex and induces G2-phase arrest. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROBO | down-regulates
phosphorylation
|
CDC25C |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124851 |
Ser216 |
SGLYRSPsMPENLNR |
Homo sapiens |
HeLa Cell, Neuron |
| pmid |
sentence |
| 15150265 |
P38 binds and phosphorylates cdc25-b and -c at serines 309 and 361 and at serine 216, respectively, and phosphorylation of these residues is required for binding to 14-3-3 proteinsphosphorylation of cdc25 triggers cell-cycle arrest by the sequestration of cdc25 by 14-3-3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
SYK | down-regulates activity
phosphorylation
|
CDC25C |
0.357 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278328 |
Ser216 |
SGLYRSPsMPENLNR |
Homo sapiens |
|
| pmid |
sentence |
| 25506060 |
SYK Phosphorylates CDC25C on Serine 216.|We now provide new genetic and biochemical evidence that SYK is an inhibitor of CDC25C in B-lineage lymphoid cells as well as non lymphohematopoietic cells, that prevents premature entry into mitosis by phosphorylating CDC25C at S216 when G 2 checkpoint responses are activated. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MARK3 | down-regulates activity
phosphorylation
|
CDC25C |
0.475 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250176 |
Ser216 |
SGLYRSPsMPENLNR |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 9543386 |
C-TAK1 protein kinase phosphorylates human Cdc25C on serine 216 and promotes 14-3-3 protein binding. Phosphorylation of serine 21 6 promotes 1 4-3-3 binding to Cdc25C and is inhibitory to Cdc25C function. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
CDC25C | up-regulates activity
dephosphorylation
|
CDK1 |
0.866 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276945 |
Thr14 |
IEKIGEGtYGVVYKG |
Homo sapiens |
|
| pmid |
sentence |
| 17634129 |
The activity of Cdc2 is regulated by the phosphatase Cdc25C. Dephosphorylation of Cdc2 at threonine 14 and tyrosine 15 by Cdc25C results in activation of Cdc2 and initiation of an autoactivation loop between Cdc25C and Cdc2 that efficiently drives cells into mitosis.|Cdc2 is activated by Cdc25C that removes phosphate groups from tyrosine 15 and threonine 14 .|Dephosphorylation of Cdc2 at threonine 14 and tyrosine 15 by Cdc25C results in activation of Cdc2 and initiation of an autoactivation loop between Cdc25C and Cdc2 that efficiently drives cells into mitosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276944 |
Tyr15 |
EKIGEGTyGVVYKGR |
Homo sapiens |
|
| pmid |
sentence |
| 24643073 |
At the onset of mitosis, the protein phosphatase Cdc25C activates the Cdc2 and cyclin B1 complex by removing the inhibitory phosphate groups from Thr 14 and Tyr 15 on Cdc2.|Dephosphorylation of Tyr15 of Cdc2 is catalyzed by Cdc25C phosphatases, and this reaction is believed to be the rate limited step for the entrance into mitosis . |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDC25C | up-regulates activity
dephosphorylation
|
CyclinB/CDK1 |
0.854 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251509 |
Thr14 |
IEKIGEGtYGVVYKG |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 10913154 |
Cyclin B-Cdc2 complexes are maintained in an inactive state until the end of G2 by phosphorylation of the Thr14/Tyr15 residues. Around the time of nuclear translocation of the complex, these residues are dephosphorylated, resulting in the formation of an active cyclin B-Cdc2 complex (2). As mentioned, this dephosphorylation occurs by a Cdc25 protein phosphatase. Three Cdc25 family members have been identified to date, A, B and C, the last one being the active one at the onset of mitosis. The activity of Cdc25C itself can be enhanced through phosphorylation by cyclin B-Cdc2 (9, 10). Therefore, activation of cyclin B-Cdc2 has been proposed to result in an autocatalytic feedback loop to ensure rapid activation of these complexes at the G2/M transition |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255037 |
Tyr15 |
EKIGEGTyGVVYKGR |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 10913154 |
Cyclin B-Cdc2 complexes are maintained in an inactive state until the end of G2 by phosphorylation of the Thr14/Tyr15 residues. Around the time of nuclear translocation of the complex, these residues are dephosphorylated, resulting in the formation of an active cyclin B-Cdc2 complex (2). As mentioned, this dephosphorylation occurs by a Cdc25 protein phosphatase. Three Cdc25 family members have been identified to date, A, B and C, the last one being the active one at the onset of mitosis. The activity of Cdc25C itself can be enhanced through phosphorylation by cyclin B-Cdc2 (9, 10). Therefore, activation of cyclin B-Cdc2 has been proposed to result in an autocatalytic feedback loop to ensure rapid activation of these complexes at the G2/M transition |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDC25C | up-regulates
dephosphorylation
|
CDK1 |
0.866 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186617 |
Thr14 |
IEKIGEGtYGVVYKG |
Homo sapiens |
|
| pmid |
sentence |
| 19574738 |
Cdk1/cdc2 activation involves tyr15/thr14 dephosphorylation by cdc25c |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186621 |
Tyr15 |
EKIGEGTyGVVYKGR |
Homo sapiens |
|
| pmid |
sentence |
| 19574738 |
Cdk1/cdc2 activation involves tyr15/thr14 dephosphorylation by cdc25c |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 | down-regulates
phosphorylation
|
CDC25C |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123713 |
Thr236 |
VEKFKDNtIPDKVKK |
Homo sapiens |
|
| pmid |
sentence |
| 15064744 |
Inhibition of protein kinase ck2 enzyme activity in vivo resulted in an enhanced nuclear localization of cdc25c. Thus, phosphorylation of cdc25c at threonine 236 is an important signal for the retention of cdc25c in the cytoplasm |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC25C | up-regulates activity
dephosphorylation
|
CCNB1 |
0.841 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277099 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25949173 |
Cdc25C is an activator of Cdc2 kinase and dephosphorylates and activates the CyclinB-Cdc2 complex shortly before the entry into the mitosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK4 | up-regulates quantity
phosphorylation
|
CDC25C |
0.455 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280074 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 35912011 |
Conclusion: PLK4 contributes to the formation of PGCCs by regulating the expression of CDC25C and is associated with the expression and subcellular location of CDC25C, pCDC25C-ser216 and pCDC25C-ser198.|PLK4 could interact with CDC25C and promote CDC25C phosphorylation which was associated with the formation of PGCCs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1 | down-regulates quantity by destabilization
ubiquitination
|
CDC25C |
0.456 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278623 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23246971 |
BRCA1 mediates cyclin B and Cdc25C ubiquitination.|Thus, BRCA1 dependent proteasomal degradation of cyclin B and Cdc25C precede the subsequent BRCA1 dependent cell cycle arrest. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC25C | down-regulates activity
dephosphorylation
|
MAP3K5 |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277100 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32518522 |
At the interval CDC25C inhibits ASK1, dephosphorylating pThr838 in its activation loop.|CDC25C dephosphorylates ASK1 to inhibit its activity during the interphase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PP1 | up-regulates
binding
|
CDC25C |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264654 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14592972 |
Pp1 recognizes cdc25 directly by interacting with a pp1-binding motif in the cdc25 n-terminus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YWHAQ | down-regulates
relocalization
|
CDC25C |
0.588 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163237 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20068082 |
Cdc25c: nuclear exclusion/cytoplasmic sequestration via binding to 14-3-3 proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1CA | up-regulates
binding
|
CDC25C |
0.516 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118917 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14592972 |
Pp1 recognizes cdc25 directly by interacting with a pp1-binding motif in the cdc25 n-terminus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CyclinB/CDK1 | up-regulates activity
phosphorylation
|
CDC25C |
0.854 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251510 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 10913154 |
Cyclin B-Cdc2 complexes are maintained in an inactive state until the end of G2 by phosphorylation of the Thr14/Tyr15 residues. Around the time of nuclear translocation of the complex, these residues are dephosphorylated, resulting in the formation of an active cyclin B-Cdc2 complex (2). As mentioned, this dephosphorylation occurs by a Cdc25 protein phosphatase. Three Cdc25 family members have been identified to date, A, B and C, the last one being the active one at the onset of mitosis. The activity of Cdc25C itself can be enhanced through phosphorylation by cyclin B-Cdc2 (9, 10). Therefore, activation of cyclin B-Cdc2 has been proposed to result in an autocatalytic feedback loop to ensure rapid activation of these complexes at the G2/M transition |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JNK | down-regulates
phosphorylation
|
CDC25C |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269983 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20220133 |
Here we show that jnk directly phosphorylates cdc25c at serine 168 during g(2) phase of the cell cycle. Cdc25c phosphorylation by jnk negatively regulates its phosphatase activity and thereby cdk1 activation, enabling a timely control of mitosis onset. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIM1 | up-regulates activity
phosphorylation
|
CDC25C |
0.344 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278298 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16356754 |
First, Pim-1 activates the Cdc25C phosphatase directly through phosphorylation, very probably at the N-terminal part of the protein.|We find that phosphorylation by Pim-1 enhances the phosphatase activity of Cdc25C and in transfected cells that are arrested in G2/M by bleomycin, Pim-1 can enhance progression into G1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATM | down-regulates 
|
CDC25C |
0.487 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-65966 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10097108 |
Atm also contributes to the cdc25c activity, particularly in ir-damaged cells, by activating chk2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
CDC25C
- 
- 