| + |
MAPK6 | up-regulates 
phosphorylation
|
MAPK6 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-40097 |
Ser189 |
YSHKGHLsEGLVTKW |
Homo sapiens |
|
| pmid |
sentence |
| 8621539 |
Ser189 of erk3, which corresponds to thr183, one of the activating phosphorylation sites of erk2, is autophosphorylated in vitro and phosphorylated in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK6 | up-regulates activity
phosphorylation
|
TDP2 |
0.378 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278245 |
Ser60 |
EMERALNsYFEPPVE |
Homo sapiens |
|
| pmid |
sentence |
| 26701725 |
ERK3 phosphorylates TDP2 and promotes its phosphodiesterase activity, thereby upregualting TDP2-mediated DNA damage response and desensitizing lung cancer cells to Top2 inhibitor-induced growth inhibition.|In the current study, we have found that ERK3, an atypical MAPK, phosphorylates TDP2 at S60 and regulates TDP2 's phosphodiesterase activity, thereby cooperatively protecting lung cancer cells against Top2 inhibitors induced DNA damage and growth inhibition. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277188 |
Ser60 |
EMERALNsYFEPPVE |
in vitro |
|
| pmid |
sentence |
| 26701725 |
In the current study, we have found that ERK3, an atypical MAPK, phosphorylates TDP2 at S60 and regulates TDP2's phosphodiesterase activity, thereby cooperatively protecting lung cancer cells against Top2 inhibitors-induced DNA damage and growth inhibition. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, In Vitro |
| + |
CDC14B | down-regulates 
dephosphorylation
|
MAPK6 |
0.572 |
| 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 | down-regulates quantity by destabilization
dephosphorylation
|
MAPK6 |
0.572 |
| 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 |
| + |
CDC14A | down-regulates
dephosphorylation
|
MAPK6 |
0.643 |
| 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 |
| + |
CyclinB/CDK1 | up-regulates
phosphorylation
|
MAPK6 |
0.383 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216797 |
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. All four sites are followed by a proline residue. We have shown that purified cyclin b-cdk1 (cyclindependent kinase 1) phosphorylates these sitesalanine 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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216801 |
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. All four sites are followed by a proline residue. We have shown that purified cyclin b-cdk1 (cyclindependent kinase 1) phosphorylates these sitesalanine 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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216805 |
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. All four sites are followed by a proline residue. We have shown that purified cyclin b-cdk1 (cyclindependent kinase 1) phosphorylates these sitesalanine 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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216809 |
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. All four sites are followed by a proline residue. We have shown that purified cyclin b-cdk1 (cyclindependent kinase 1) phosphorylates these sitesalanine 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. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CDC14A | down-regulates quantity by destabilization
dephosphorylation
|
MAPK6 |
0.643 |
| 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 |
| + |
CDK1 | up-regulates
phosphorylation
|
MAPK6 |
0.485 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164487 |
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. All four sites are followed by a proline residue. We have shown that purified cyclin b-cdk1 (cyclindependent kinase 1) phosphorylates these sitesalanine 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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164491 |
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. All four sites are followed by a proline residue. We have shown that purified cyclin b-cdk1 (cyclindependent kinase 1) phosphorylates these sitesalanine 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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164495 |
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. All four sites are followed by a proline residue. We have shown that purified cyclin b-cdk1 (cyclindependent kinase 1) phosphorylates these sitesalanine 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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164499 |
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. All four sites are followed by a proline residue. We have shown that purified cyclin b-cdk1 (cyclindependent kinase 1) phosphorylates these sitesalanine 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. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
MAPK6 | up-regulates
phosphorylation
|
NCOA3 |
0.484 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-196957 |
Ser857 |
PPYNRAVsLDSPVSV |
Homo sapiens |
Lung Cancer Cell |
| pmid |
sentence |
| 22505454 |
Here, we report that erk3 interacted with and phosphorylated steroid receptor coactivator 3 (src-3), an oncogenic protein overexpressed in multiple human cancers at serine 857 (s857) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK6 | up-regulates activity
phosphorylation
|
MAPKAPK5 |
0.689 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279073 |
Thr182 |
IDQGDLMtPQFTPYY |
Homo sapiens |
|
| pmid |
sentence |
| 20734105 |
ERK3, ERK4 and p38 MAPK can all phosphorylate MK5 at Thr 182 , , , - ], but it is not known whether these enzymes also can phosphorylate Ser 115 and whether this modification contributes to ERK3-, ERK4-, or p38 MAPK -regulated subcellular localization of MK5. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUSP2 | down-regulates activity
dephosphorylation
|
MAPK6 |
0.375 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277069 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28252035 |
DUSP2 can dephosphorylate both ERK3 and ERK4 when expressed in mammalian cells.|Finally, we demonstrate that DUSP2 inhibits ERK3 and ERK4 mediated activation of MK5. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK6 | up-regulates activity
phosphorylation
|
KALRN |
0.408 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263094 |
|
|
in vitro |
|
| pmid |
sentence |
| 22508986 |
The brain-specific nucleotide exchange factor kalirin-7 (Kal7) was identified as an MK5 interaction partner and substrate protein. The MK5 substrate Kal7, a Rho GEF and known activator of Rac GTPases, further contributes to PAK activation and actin filament reorganization. Thus, the coordinated phosphorylation of Borg proteins and Kal7 by ERK3 and MK5 constitute a novel signaling cascade involving feed-forward circuits, multiple GTPases, and cytoskeletal elements. |
|
| Publications: |
1 |
Organism: |
In Vitro |
4.0
MAPK6
- 
- 