| + |
MAPK8 | down-regulates quantity by destabilization 
phosphorylation
|
CDC25B |
0.288 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276352 |
Ser101 |
ASESSLSsESSESSD |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21807946 |
Recently, we showed that Cdc25B is degraded rapidly by non-genotoxic stimuli that activate stress-responsive MAPKs, such as Jun N-terminal kinase (JNK) and p38 (Uchida et al., 2009). Our results suggested that these kinases phosphorylate specific Ser residues in the N-terminal region (S101 and S103) to induce Cdc25B degradation.Here, we report that Cdc25B was ubiquitylated by SCF(βTrCP) E3 ligase upon phosphorylation at two Ser residues in the βTrCP-binding-motif-like sequence D(94)AGLCMDSPSP(104). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276351 |
Ser103 |
ESSLSSEsSESSDAG |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21807946 |
Recently, we showed that Cdc25B is degraded rapidly by non-genotoxic stimuli that activate stress-responsive MAPKs, such as Jun N-terminal kinase (JNK) and p38 (Uchida et al., 2009). Our results suggested that these kinases phosphorylate specific Ser residues in the N-terminal region (S101 and S103) to induce Cdc25B degradation.Here, we report that Cdc25B was ubiquitylated by SCF(βTrCP) E3 ligase upon phosphorylation at two Ser residues in the βTrCP-binding-motif-like sequence D(94)AGLCMDSPSP(104). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
p38 | down-regulates quantity by destabilization
phosphorylation
|
CDC25B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276350 |
Ser101 |
ASESSLSsESSESSD |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21807946 |
Recently, we showed that Cdc25B is degraded rapidly by non-genotoxic stimuli that activate stress-responsive MAPKs, such as Jun N-terminal kinase (JNK) and p38 (Uchida et al., 2009). Our results suggested that these kinases phosphorylate specific Ser residues in the N-terminal region (S101 and S103) to induce Cdc25B degradation.Here, we report that Cdc25B was ubiquitylated by SCF(βTrCP) E3 ligase upon phosphorylation at two Ser residues in the βTrCP-binding-motif-like sequence D(94)AGLCMDSPSP(104). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276349 |
Ser103 |
ESSLSSEsSESSDAG |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21807946 |
Recently, we showed that Cdc25B is degraded rapidly by non-genotoxic stimuli that activate stress-responsive MAPKs, such as Jun N-terminal kinase (JNK) and p38 (Uchida et al., 2009). Our results suggested that these kinases phosphorylate specific Ser residues in the N-terminal region (S101 and S103) to induce Cdc25B degradation.Here, we report that Cdc25B was ubiquitylated by SCF(βTrCP) E3 ligase upon phosphorylation at two Ser residues in the βTrCP-binding-motif-like sequence D(94)AGLCMDSPSP(104). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDK1 | up-regulates 
phosphorylation
|
CDC25B |
0.825 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90451 |
Ser160 |
PVRLLGHsPVLRNIT |
Homo sapiens |
|
| pmid |
sentence |
| 12107172 |
We demonstrate that serine 146 is required for two crucial features of cdc25b1. It is essential for cdc25b1 to function as a mitotic inducer and to prevent cdc25b1 export from the nucleus. We also show that serine 146 is phosphorylated in vitro by cdk1-cyclin b. Serine 146 phosphorylation is proposed to be a key event in the regulation of the cdc25b function |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167641 |
Ser321 |
KCQRLFRsPSMPCSV |
Homo sapiens |
|
| pmid |
sentence |
| 20801879 |
Ser(321) is phosphorylated in mitosis by cdk1. The mitotic phosphorylation of ser(321) acts to maintain full activation of cdc25b by disrupting 14-3-3 binding to ser(323) and enhancing the dephosphorylation of ser(323) to block 14-3-3 binding to this site. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CyclinB/CDK1 | up-regulates
phosphorylation
|
CDC25B |
0.761 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216753 |
Ser160 |
PVRLLGHsPVLRNIT |
Homo sapiens |
|
| pmid |
sentence |
| 12107172 |
We demonstrate that serine 146 is required for two crucial features of cdc25b1. It is essential for cdc25b1 to function as a mitotic inducer and to prevent cdc25b1 export from the nucleus. We also show that serine 146 is phosphorylated in vitro by cdk1-cyclin b. Serine 146 phosphorylation is proposed to be a key event in the regulation of the cdc25b function |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MELK | up-regulates
phosphorylation
|
CDC25B |
0.547 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-137378 |
Ser169 |
VLRNITNsQAPDGRR |
Homo sapiens |
|
| pmid |
sentence |
| 15908796 |
We demonstrate that cdc25b is phosphorylated in vitro by peg3 on serine 169this phosphorylated form of cdc25b accumulates during mitosis, and is localized to the centrosomes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 | up-regulates activity
phosphorylation
|
CDC25B |
0.342 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250836 |
Ser186 |
EAGSGAAsSSGEDKE |
in vitro |
|
| pmid |
sentence |
| 12527891 |
Mass spectrometry analysis demonstrates that at least two serine residues, Ser-186 and Ser-187, are phosphorylated in vivo. | Finally, we demonstrate that phosphorylation of CDC25B by protein kinase CK2 increases the catalytic activity of the phosphatase in vitro as well as in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250837 |
Ser187 |
AGSGAASsSGEDKEN |
in vitro |
|
| pmid |
sentence |
| 12527891 |
Mass spectrometry analysis demonstrates that at least two serine residues, Ser-186 and Ser-187, are phosphorylated in vivo. | Finally, we demonstrate that phosphorylation of CDC25B by protein kinase CK2 increases the catalytic activity of the phosphatase in vitro as well as in vivo. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MELK | down-regulates activity
phosphorylation
|
CDC25B |
0.547 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255655 |
Ser219 |
HALAEWAsRREAFAQ |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 12400006 |
In the present study we show that the human pEg3 kinase is able to specifically phosphorylate CDC25B in vitro. One phosphorylation site was identified and corresponded to serine 323[Ä] Taken together these results suggest that pEg3 is a potential regulator of the G2/M progression and may act antagonistically to the CDC25B phosphatase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHEK1 | down-regulates activity
phosphorylation
|
CDC25B |
0.782 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149898 |
Ser230 |
AFAQRPSsAPDLMCL |
Homo sapiens |
|
| pmid |
sentence |
| 17003105 |
Here, we show that cdc25b is phosphorylated by chk1 in vitro on multiple residues, including s230 and s563.We show that the s230-phosphorylated form of cdc25b is located at the centrosome from early s phase until mitosis. Furthermore, mutation of s230 to alanine increases the mitotic-inducing activity of cdc25b |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROBO | down-regulates
phosphorylation
|
CDC25B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124843 |
Ser323 |
QRLFRSPsMPCSVIR |
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124847 |
Ser375 |
ARVLRSKsLCHDEIE |
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: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
p38 | down-regulates activity
phosphorylation
|
CDC25B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107412 |
Ser323 |
QRLFRSPsMPCSVIR |
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107416 |
Ser375 |
ARVLRSKsLCHDEIE |
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: |
2 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates
phosphorylation
|
CDC25B |
0.714 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139396 |
Ser353 |
VQNKRRRsVTPPEEQ |
Homo sapiens |
|
| pmid |
sentence |
| 16082213 |
We show that bypass of the g2/m checkpoint by the chk1 kinase inhibitor ucn-01 results in the activation of aurora-a and phosphorylation of cdc25b on s353 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6K | up-regulates
phosphorylation
|
CDC25B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252781 |
Ser353 |
VQNKRRRsVTPPEEQ |
Homo sapiens |
|
| pmid |
sentence |
| 23708659 |
Rsk promotes g2/m transition through activating phosphorylation of cdc25a and cdc25b rsk is likely to be more active in mitotic cells than in interphase cells, as evidenced by the phosphorylation status of t359/s363 in rsk. Together, these findings indicate that rsk promotes g2/m transition in mammalian cells through activating phosphorylation of cdc25a and cdc25b. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252779 |
Thr355 |
NKRRRSVtPPEEQQE |
Homo sapiens |
|
| pmid |
sentence |
| 23708659 |
Rsk promotes g2/m transition through activating phosphorylation of cdc25a and cdc25b rsk is likely to be more active in mitotic cells than in interphase cells, as evidenced by the phosphorylation status of t359/s363 in rsk. Together, these findings indicate that rsk promotes g2/m transition in mammalian cells through activating phosphorylation of cdc25a and cdc25b. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | up-regulates
phosphorylation
|
CDC25B |
0.255 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202121 |
Ser353 |
VQNKRRRsVTPPEEQ |
Homo sapiens |
|
| pmid |
sentence |
| 23708659 |
Rsk promotes g2/m transition through activating phosphorylation of cdc25a and cdc25b rsk is likely to be more active in mitotic cells than in interphase cells, as evidenced by the phosphorylation status of t359/s363 in rsk. Together, these findings indicate that rsk promotes g2/m transition in mammalian cells through activating phosphorylation of cdc25a and cdc25b. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202125 |
Thr355 |
NKRRRSVtPPEEQQE |
Homo sapiens |
|
| pmid |
sentence |
| 23708659 |
Rsk promotes g2/m transition through activating phosphorylation of cdc25a and cdc25b rsk is likely to be more active in mitotic cells than in interphase cells, as evidenced by the phosphorylation status of t359/s363 in rsk. Together, these findings indicate that rsk promotes g2/m transition in mammalian cells through activating phosphorylation of cdc25a and cdc25b. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
BRSK1 | down-regulates activity
phosphorylation
|
CDC25B |
0.518 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107404 |
Ser375 |
ARVLRSKsLCHDEIE |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15150265 |
Hssad1 specifically phosphorylated wee1a, cdc25-c, and -b on ser-642, ser-216, and ser-361 in vitro, respectively phosphorylation of cdc25 triggers cell-cycle arrest by the sequestration of cdc25 by 14-3-3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRSK1 | down-regulates
phosphorylation
|
CDC25B |
0.518 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124839 |
Ser375 |
ARVLRSKsLCHDEIE |
Homo sapiens |
HeLa Cell, Neuron |
| pmid |
sentence |
| 15150265 |
Hssad1 specifically phosphorylated wee1a, cdc25-c, and -b on ser-642, ser-216, and ser-361 in vitro, respectivelyphosphorylation of cdc25 triggers cell-cycle arrest by the sequestration of cdc25 by 14-3-3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
CDC25B | up-regulates activity
dephosphorylation
|
CDK1 |
0.825 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276969 |
Thr14 |
IEKIGEGtYGVVYKG |
Homo sapiens |
|
| pmid |
sentence |
| 25384584 |
CDC25B facilitates dephosphorylation of the key cell cycle regulator CDC2 (also called CDK1) at Tyr15 or Thr14, thereby initiating the G 2 /M transition ( xref ).|CDC25B facilitates dephosphorylation of the key cell cycle regulator CDC2 (also called CDK1) at Tyr15 or Thr14, thereby initiating the G2/M transition ( ). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276970 |
Tyr15 |
EKIGEGTyGVVYKGR |
Homo sapiens |
|
| pmid |
sentence |
| 25384584 |
CDC25B facilitates dephosphorylation of the key cell cycle regulator CDC2 (also called CDK1) at Tyr15 or Thr14, thereby initiating the G 2 /M transition ( xref ).|CDC25B facilitates dephosphorylation of the key cell cycle regulator CDC2 (also called CDK1) at Tyr15 or Thr14, thereby initiating the G2/M transition ( ). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates activity
phosphorylation
|
CDC25B |
0.657 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267560 |
|
|
|
|
| pmid |
sentence |
| 21640712 |
These data indicated that PLK1 phosphorylates CDC25B and that pre-phosphorylation of CDC25B by CDK1/CyclinB enhances its substrate properties for PLK1 in vitro |
|
| Publications: |
1 |
| + |
PCSK7 | down-regulates
phosphorylation
|
CDC25B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107423 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11333986 |
We propose that regulation of cdc25b phosphorylation by p38 is a critical event for initiating the g2/m checkpoint after ultraviolet radiation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC25B | up-regulates activity
dephosphorylation
|
CDK2 |
0.76 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277140 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26474275 |
CDC25B is also able to dephosphorylate and activate CDK2-Cyclin A and CDK2-Cyclin E complexes [ xref \u2013 xref ]. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC25B | up-regulates
dephosphorylation
|
CyclinB/CDK1 |
0.761 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217511 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7880537 |
Cdc25 dephosphorylates cdc2/cdk1 within the activation loop of the kinase domain to achieve full activity of the cyclin-cdk complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC25B | up-regulates
dephosphorylation
|
CDK1 |
0.825 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-34541 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7880537 |
Cdc25 dephosphorylates cdc2/cdk1 within the activation loop of the kinase domain to achieve full activity of the cyclin-cdk complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC14A | down-regulates activity
dephosphorylation
|
CDC25B |
0.574 |
| 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 |
| + |
SCF-betaTRCP | down-regulates quantity by destabilization
ubiquitination
|
CDC25B |
0.385 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276353 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21807946 |
Recently, we showed that Cdc25B is degraded rapidly by non-genotoxic stimuli that activate stress-responsive MAPKs, such as Jun N-terminal kinase (JNK) and p38 (Uchida et al., 2009). Our results suggested that these kinases phosphorylate specific Ser residues in the N-terminal region (S101 and S103) to induce Cdc25B degradation.Here, we report that Cdc25B was ubiquitylated by SCF(βTrCP) E3 ligase upon phosphorylation at two Ser residues in the βTrCP-binding-motif-like sequence D(94)AGLCMDSPSP(104). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK13 | down-regulates 
|
CDC25B |
0.463 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85999 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11333986 |
P38 map k can also induce a g2/m checkpoint through the phosphorylation and the phosphatase cdc25b. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CDC25B
- 
- 