| + |
EP300 | up-regulates 
acetylation
|
DUSP1 |
0.317 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166581 |
Lys57 |
TIVRRRAkGAMGLEH |
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 20626350 |
A recent report shows that mkp1 may also be regulated by acetylation. When raw macrophages are stimulated with lps, mkp1 becomes acetylated on lys57 by p300 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | down-regulates 
phosphorylation
|
DUSP1 |
0.799 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141593 |
Ser296 |
KQRRSIIsPNFSFMG |
Homo sapiens |
|
| pmid |
sentence |
| 16286470 |
The dual-specificity mapk phosphatase mkp-1/cl100/dusp1 is an inducible nuclear protein controlled by p44/42 mapk (erk1/2) in a negative feedback mechanism to inhibit kinase activity. Here, we report on the molecular basis for a novel positive feedback mechanism to sustain erk activation by triggering mkp-1 proteolysis. Active erk2 docking to the def motif (fxfp, residues 339-342) of n-terminally truncated mkp-1 in vitro initiated phosphorylation at the ser(296)/ser(323) domain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141601 |
Ser323 |
HCSAEAGsPAMAVLD |
Homo sapiens |
|
| pmid |
sentence |
| 16286470 |
The dual-specificity mapk phosphatase mkp-1/cl100/dusp1 is an inducible nuclear protein controlled by p44/42 mapk (erk1/2) in a negative feedback mechanism to inhibit kinase activity. Here, we report on the molecular basis for a novel positive feedback mechanism to sustain erk activation by triggering mkp-1 proteolysis. Active erk2 docking to the def motif (fxfp, residues 339-342) of n-terminally truncated mkp-1 in vitro initiated phosphorylation at the ser(296)/ser(323) domain |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | down-regulates
phosphorylation
|
DUSP1 |
0.777 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141605 |
Ser296 |
KQRRSIIsPNFSFMG |
Homo sapiens |
|
| pmid |
sentence |
| 16286470 |
The dual-specificity mapk phosphatase mkp-1/cl100/dusp1 is an inducible nuclear protein controlled by p44/42 mapk (erk1/2) in a negative feedback mechanism to inhibit kinase activity. Here, we report on the molecular basis for a novel positive feedback mechanism to sustain erk activation by triggering mkp-1 proteolysis. Active erk2 docking to the def motif (fxfp, residues 339-342) of n-terminally truncated mkp-1 in vitro initiated phosphorylation at the ser(296)/ser(323) domain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141609 |
Ser323 |
HCSAEAGsPAMAVLD |
Homo sapiens |
|
| pmid |
sentence |
| 16286470 |
The dual-specificity mapk phosphatase mkp-1/cl100/dusp1 is an inducible nuclear protein controlled by p44/42 mapk (erk1/2) in a negative feedback mechanism to inhibit kinase activity. Here, we report on the molecular basis for a novel positive feedback mechanism to sustain erk activation by triggering mkp-1 proteolysis. Active erk2 docking to the def motif (fxfp, residues 339-342) of n-terminally truncated mkp-1 in vitro initiated phosphorylation at the ser(296)/ser(323) domain |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | up-regulates
phosphorylation
|
DUSP1 |
0.777 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73629 |
Ser359 |
SALSYLQsPITTSPS |
Homo sapiens |
|
| pmid |
sentence |
| 10617468 |
Mkp-1 was a target in vivo and in vitro for p42(mapk) or p44(mapk), which phosphorylates mkp-1 on two carboxyl-terminal serine residues, serine 359 and serine 364. This phosphorylation did not modify mkp-1's intrinsic ability to dephosphorylate p44(mapk) but led to stabilization of the protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73633 |
Ser364 |
LQSPITTsPSC |
Homo sapiens |
|
| pmid |
sentence |
| 10617468 |
Mkp-1 was a target in vivo and in vitro for p42(mapk) or p44(mapk), which phosphorylates mkp-1 on two carboxyl-terminal serine residues, serine 359 and serine 364. This phosphorylation did not modify mkp-1's intrinsic ability to dephosphorylate p44(mapk) but led to stabilization of the protein. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | up-regulates
phosphorylation
|
DUSP1 |
0.799 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73621 |
Ser359 |
SALSYLQsPITTSPS |
Homo sapiens |
|
| pmid |
sentence |
| 10617468 |
Mkp-1 was a target in vivo and in vitro for p42(mapk) or p44(mapk), which phosphorylates mkp-1 on two carboxyl-terminal serine residues, serine 359 and serine 364. This phosphorylation did not modify mkp-1's intrinsic ability to dephosphorylate p44(mapk) but led to stabilization of the protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73625 |
Ser364 |
LQSPITTsPSC |
Homo sapiens |
|
| pmid |
sentence |
| 10617468 |
Mkp-1 was a target in vivo and in vitro for p42(mapk) or p44(mapk), which phosphorylates mkp-1 on two carboxyl-terminal serine residues, serine 359 and serine 364. This phosphorylation did not modify mkp-1's intrinsic ability to dephosphorylate p44(mapk) but led to stabilization of the protein. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
DUSP1 | down-regulates activity
dephosphorylation
|
MAPK1 |
0.799 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248464 |
Thr185 |
HDHTGFLtEYVATRW |
Rattus norvegicus |
|
| pmid |
sentence |
| 7535768 |
We demonstrate that ERK, JNK, and p38 are activated by distinct combinations of stimuli in T cells that simulate full or partial activation through the T cell receptor. These kinases are regulated by reversible phosphorylation on Tyr and Thr, and the dual specific phosphatases PAC1 and MKP-1 previously have been implicated in the in vivo inactivation of ERK or of ERK and JNK, respectively |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248465 |
Tyr187 |
HTGFLTEyVATRWYR |
Rattus norvegicus |
|
| pmid |
sentence |
| 7535768 |
We demonstrate that ERK, JNK, and p38 are activated by distinct combinations of stimuli in T cells that simulate full or partial activation through the T cell receptor. These kinases are regulated by reversible phosphorylation on Tyr and Thr, and the dual specific phosphatases PAC1 and MKP-1 previously have been implicated in the in vivo inactivation of ERK or of ERK and JNK, respectively |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
DUSP1 | down-regulates activity
dephosphorylation
|
MAPK3 |
0.777 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248462 |
Thr202 |
HDHTGFLtEYVATRW |
Rattus norvegicus |
|
| pmid |
sentence |
| 7535768 |
We demonstrate that ERK, JNK, and p38 are activated by distinct combinations of stimuli in T cells that simulate full or partial activation through the T cell receptor. These kinases are regulated by reversible phosphorylation on Tyr and Thr, and the dual specific phosphatases PAC1 and MKP-1 previously have been implicated in the in vivo inactivation of ERK or of ERK and JNK, respectively |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248463 |
Tyr204 |
HTGFLTEyVATRWYR |
Rattus norvegicus |
|
| pmid |
sentence |
| 7535768 |
We demonstrate that ERK, JNK, and p38 are activated by distinct combinations of stimuli in T cells that simulate full or partial activation through the T cell receptor. These kinases are regulated by reversible phosphorylation on Tyr and Thr, and the dual specific phosphatases PAC1 and MKP-1 previously have been implicated in the in vivo inactivation of ERK or of ERK and JNK, respectively |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
Gbeta | down-regulates
phosphorylation
|
DUSP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270093 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16286470 |
The dual-specificity mapk phosphatase mkp-1/cl100/dusp1 is an inducible nuclear protein controlled by p44/42 mapk (erk1/2) in a negative feedback mechanism to inhibit kinase activity. Here, we report on the molecular basis for a novel positive feedback mechanism to sustain erk activation by triggering mkp-1 proteolysis. Active erk2 docking to the def motif (fxfp, residues 339-342) of n-terminally truncated mkp-1 in vitro initiated phosphorylation at the ser(296)/ser(323) domain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUSP1 | down-regulates activity
dephosphorylation
|
MAPK14 |
0.797 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93873 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12356755 |
Here we show that glucocorticoids synergistically enhance nthi-induced tlr2 expression via specific up-regulation of the mapk phosphatase-1 (mkp-1) that, in turn, leads to dephosphorylation and inactivation of p38 mapk, the negative regulator for tlr2 expression. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166571 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20626350 |
The activity of MAPKs can be also regulated by a family of DUSPs (dual-specificity phosphatases)/MKPs (MAPK phosphatases), which dephosphorylate both phosphotyrosine and phosphothreonine residues MKPs 1, 4, 5 and 7 can dephosphorylate p38_ and p38_ in addition to JNK MAPKs. Importantly, some MKPs are transcriptionally up-regulated by stimuli that activate MAPK signalling, and are thought to play an important role limiting the extent of MAPK activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236867 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 17158101 |
Our results show that Notch specifically induces expression of MKP-1, a member of the dual-specificity MAPK phosphatase, which directly inactivates p38 to negatively regulate C2C12 myogenesis. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens, Mus Musculus |
| Pathways: | NOTCH Signaling and Myogenesis, P38 Signaling |
| + |
RBPJ/NOTCH | up-regulates quantity 
transcriptional regulation
|
DUSP1 |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255744 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 17158101 |
Our results show that Notch specifically induces expression of MKP-1, a member of the dual-specificity MAPK phosphatase, which directly inactivates p38 to negatively regulate C2C12 myogenesis |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Skeletal Muscle |
| Pathways: | NOTCH Signaling and Myogenesis |
| + |
NR3C1 | up-regulates quantity
|
DUSP1 |
0.562 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253546 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 11742987 |
Glucocorticoids inhibit MAP kinase via increased expression and decreased degradation of MKP-1|Both induction of MKP-1 expression and inhibition of its degradation are necessary for glucocorticoid-mediated inhibition of Erk-1/2 activation. In NIH-3T3 fibroblasts, although glucocorticoids up-regulate the MKP-1 level, they do not attenuate the proteasomal degradation of this protein and consequently they are unable to inhibit Erk-1/2 activity. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
DUSP1 | down-regulates
dephosphorylation
|
Gbeta |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269910 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10617468 |
The mitogen-activated protein (map) kinase cascade is inactivated at the level of map kinase by members of the map kinase phosphatase (mkp) family, including mkp-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUSP1 | down-regulates
dephosphorylation
|
MAPK3 |
0.777 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73617 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10617468 |
The mitogen-activated protein (map) kinase cascade is inactivated at the level of map kinase by members of the map kinase phosphatase (mkp) family, including mkp-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUSP1 | down-regulates
dephosphorylation
|
MAPK9 |
0.669 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-40879 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 8626452 |
We assayed the relative ability of mkp-2, pac1, and mkp-1 to dephosphorylate erk2 and the other related map kinases, jnk2 and p38. the dual specific phosphatases pac1 and mkp-1 previously have been implicated in the in vivo inactivation of erk or of erk and jnk, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RBPJ | up-regulates
binding
|
DUSP1 |
0.253 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236851 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 17158101 |
Notch induction of mkp-1 depends on an rbp-j-dependent mechanism. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
DUSP1 | down-regulates
dephosphorylation
|
ERK1/2 |
0.828 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269930 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10617468 |
The mitogen-activated protein (map) kinase cascade is inactivated at the level of map kinase by members of the map kinase phosphatase (mkp) family, including mkp-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK14 | up-regulates activity
binding
|
DUSP1 |
0.797 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-83752 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11062068 |
Here we have shown that mkp-1 associates directly with p38 map kinase both in vivo and in vitro, and that this interaction enhances the catalytic activity of mkp-1. The point mutation asp-316-->asn in the c-terminus of p38, analogous to the erk2 (extracellular-signal-regulated kinase 2) sevenmaker mutation, dramatically decreases its binding to mkp-1 and substantially compromises its stimulatory effect on the catalytic activity of this phosphatase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | NOTCH Signaling and Myogenesis, P38 Signaling |
| + |
ERK1/2 | down-regulates
phosphorylation
|
DUSP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270189 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16286470 |
The dual-specificity mapk phosphatase mkp-1/cl100/dusp1 is an inducible nuclear protein controlled by p44/42 mapk (erk1/2) in a negative feedback mechanism to inhibit kinase activity. Here, we report on the molecular basis for a novel positive feedback mechanism to sustain erk activation by triggering mkp-1 proteolysis. Active erk2 docking to the def motif (fxfp, residues 339-342) of n-terminally truncated mkp-1 in vitro initiated phosphorylation at the ser(296)/ser(323) domain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUSP1 | down-regulates
dephosphorylation
|
MAPK1 |
0.799 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73614 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10617468 |
The mitogen-activated protein (map) kinase cascade is inactivated at the level of map kinase by members of the map kinase phosphatase (mkp) family, including mkp-1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | up-regulates quantity by expression
transcriptional regulation
|
DUSP1 |
0.335 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260053 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11494141 |
Defects in PTEN, a tumor suppressor, have been found in cancers arising in a variety of human tissues. To elucidate the tumor-suppressive function of this gene, we have been analysing expression profiles of cancer cells after introduction of exogenous PTEN. Those experiments identified 99 candidate genes that were transcriptionally transactivated. Among them, we report here the further analyses of eight genes, EGR2/Krox-20, BPOZ, APS, HCLS1/HS1, DUSP1/MKP1, NDRG1/Drg1/RTP, NFIL3/E4BP4, and a novel gene (PINK1, PTEN-induced putative kinase). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUSP1 | down-regulates
dephosphorylation
|
MAPK8 |
0.781 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-46079 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9020184 |
Jnk1 phosphorylation and activation was inhibited by expression of both mkp1 and mkp2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
DUSP1
- 
- 