| + |
DUSP4 | down-regulates activity 
dephosphorylation
|
MAPK1 |
0.752 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248717 |
Thr185 |
HDHTGFLtEYVATRW |
Rattus norvegicus |
|
| pmid |
sentence |
| 7535768 |
Dephosphorylation and Inactivation of ERKs|A single protein kinase, MEK, activates ERK2 by phosphorylating threonine 183 and tyrosine 185 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248718 |
Tyr187 |
HTGFLTEyVATRWYR |
Rattus norvegicus |
|
| pmid |
sentence |
| 7535768 |
Dephosphorylation and Inactivation of ERKs|A single protein kinase, MEK, activates ERK2 by phosphorylating threonine 183 and tyrosine 185 |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
DUSP4 | down-regulates activity
dephosphorylation
|
MAPK3 |
0.696 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248715 |
Thr202 |
HDHTGFLtEYVATRW |
Rattus norvegicus |
|
| pmid |
sentence |
| 7535768 |
Dephosphorylation and Inactivation of ERKs|ERK1 phosphorylated on either threonine (ERK1*Y204F) or tyrosine alone (ERK1*T202A) was utilized as a substrate for HVH2. Threonine 202 and tyrosine 204 in ERK1 (53) correspond to threonine 183 and tyrosine 185 in ERK2 which are the activation-phosphorylation sites by MEK(14, 15, 16). ERK1*, a kinase-deficient mutant, was phosphorylated on both threonine and tyrosine by MEK2 (Fig. 3B). ERK1*T202A, having threonine 202 substituted by an alanine, was phosphorylated only on tyrosine while ERK1*Y204F, having tyrosine 204 substituted by a phenylalanine, was phosphorylated only on threonine (Fig. 3B). GST-HVH2 dephosphorylated all three ERK1* mutants (Fig. 3A), suggesting that double phosphorylations of adjacent threonine and tyrosine were not a prerequisite for HVH2 recognition. However, HVH2 dephosphorylated ERK1* and ERK1*T202A more efficiently than ERK1*Y204F (Fig. 3A), indicating that HVH2 preferred phosphotyrosine over phosphothreonine. Interestingly, MEK also phosphorylated tyrosine residues more efficiently than threonine residues of ERK |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248716 |
Tyr204 |
HTGFLTEyVATRWYR |
Rattus norvegicus |
|
| pmid |
sentence |
| 7535768 |
Dephosphorylation and Inactivation of ERKs|ERK1 phosphorylated on either threonine (ERK1*Y204F) or tyrosine alone (ERK1*T202A) was utilized as a substrate for HVH2. Threonine 202 and tyrosine 204 in ERK1 (53) correspond to threonine 183 and tyrosine 185 in ERK2 which are the activation-phosphorylation sites by MEK(14, 15, 16). ERK1*, a kinase-deficient mutant, was phosphorylated on both threonine and tyrosine by MEK2 (Fig. 3B). ERK1*T202A, having threonine 202 substituted by an alanine, was phosphorylated only on tyrosine while ERK1*Y204F, having tyrosine 204 substituted by a phenylalanine, was phosphorylated only on threonine (Fig. 3B). GST-HVH2 dephosphorylated all three ERK1* mutants (Fig. 3A), suggesting that double phosphorylations of adjacent threonine and tyrosine were not a prerequisite for HVH2 recognition. However, HVH2 dephosphorylated ERK1* and ERK1*T202A more efficiently than ERK1*Y204F (Fig. 3A), indicating that HVH2 preferred phosphotyrosine over phosphothreonine. Interestingly, MEK also phosphorylated tyrosine residues more efficiently than threonine residues of ERK |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
DUSP4 | down-regulates
dephosphorylation
|
MAPK1 |
0.752 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-40926 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8626452 |
Here we characterize a new map kinase phosphatase, mkp-2, that is induced in human peripheral blood t cells with phorbol 12-myristate 13-acetate and is expressed in a variety of nonhematopoietic tissues as well. We show that the in vivo substrate specificities of individual phosphatases are unique. Pac1, mkp-2, and mkp-1 recognize erk and p38, erk and jnk, and erk, p38, and jnk, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUSP4 | down-regulates
dephosphorylation
|
MAPK8 |
0.702 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-27756 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9020184 |
Jnk1 phosphorylation and activation was inhibited by expression of both mkp1 and mkp2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUSP4 | down-regulates
dephosphorylation
|
MAPK14 |
0.65 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147958 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16849326 |
This result suggests that dusp4 represses gluconeogenesis through dephosphorylation of p38 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUSP4 | down-regulates
dephosphorylation
|
MAPK9 |
0.601 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-40929 |
|
|
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. . Mkp-2 had detectable activity against jnk2, although full inactivation of jnk2 was not observed even at the higher phosphatase concentration. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUSP4 | down-regulates activity
dephosphorylation
|
ERK1/2 |
0.752 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269933 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 7535768 |
Dephosphorylation and Inactivation of ERKs|ERK1 phosphorylated on either threonine (ERK1*Y204F) or tyrosine alone (ERK1*T202A) was utilized as a substrate for HVH2. Threonine 202 and tyrosine 204 in ERK1 (53) correspond to threonine 183 and tyrosine 185 in ERK2 which are the activation-phosphorylation sites by MEK(14, 15, 16). ERK1*, a kinase-deficient mutant, was phosphorylated on both threonine and tyrosine by MEK2 (Fig. 3B). ERK1*T202A, having threonine 202 substituted by an alanine, was phosphorylated only on tyrosine while ERK1*Y204F, having tyrosine 204 substituted by a phenylalanine, was phosphorylated only on threonine (Fig. 3B). GST-HVH2 dephosphorylated all three ERK1* mutants (Fig. 3A), suggesting that double phosphorylations of adjacent threonine and tyrosine were not a prerequisite for HVH2 recognition. However, HVH2 dephosphorylated ERK1* and ERK1*T202A more efficiently than ERK1*Y204F (Fig. 3A), indicating that HVH2 preferred phosphotyrosine over phosphothreonine. Interestingly, MEK also phosphorylated tyrosine residues more efficiently than threonine residues of ERK |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
DUSP4 | down-regulates activity
dephosphorylation
|
Gbeta |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269914 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 7535768 |
Dephosphorylation and Inactivation of ERKs|ERK1 phosphorylated on either threonine (ERK1*Y204F) or tyrosine alone (ERK1*T202A) was utilized as a substrate for HVH2. Threonine 202 and tyrosine 204 in ERK1 (53) correspond to threonine 183 and tyrosine 185 in ERK2 which are the activation-phosphorylation sites by MEK(14, 15, 16). ERK1*, a kinase-deficient mutant, was phosphorylated on both threonine and tyrosine by MEK2 (Fig. 3B). ERK1*T202A, having threonine 202 substituted by an alanine, was phosphorylated only on tyrosine while ERK1*Y204F, having tyrosine 204 substituted by a phenylalanine, was phosphorylated only on threonine (Fig. 3B). GST-HVH2 dephosphorylated all three ERK1* mutants (Fig. 3A), suggesting that double phosphorylations of adjacent threonine and tyrosine were not a prerequisite for HVH2 recognition. However, HVH2 dephosphorylated ERK1* and ERK1*T202A more efficiently than ERK1*Y204F (Fig. 3A), indicating that HVH2 preferred phosphotyrosine over phosphothreonine. Interestingly, MEK also phosphorylated tyrosine residues more efficiently than threonine residues of ERK |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
3.0
DUSP4
- 
- 