+ |
DUSP3 | down-regulates activity
dephosphorylation
|
EGFR |
0.364 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248532 |
Tyr1016 |
DVVDADEyLIPQQGF |
Homo sapiens |
NCI-H1299 Cell |
pmid |
sentence |
21262974 |
We found that EGF receptor (EGFR) was a direct substrate of VHR and that overexpression of VHR down-regulated EGFR phosphorylation, particularly at Tyr-992 residue. Expression of VHR inhibited the activation of phospholipase Cγ and protein kinase C, both downstream effectors of Tyr-992 phosphorylation of EGFR. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DUSP3 | down-regulates activity
dephosphorylation
|
ERBB2 |
0.271 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248534 |
Tyr1221 |
SPAFDNLyYWDQDPP |
Homo sapiens |
NCI-H1299 Cell |
pmid |
sentence |
21262974 |
Expression of VHR inhibited the activation of phospholipase Cγ and protein kinase C, both downstream effectors of Tyr-992 phosphorylation of EGFR. | We found that VHR decreased ErbB2 phosphorylation in vitro and in a cellular context, and the dephosphorylation of ErbB2 was more evident at Tyr-877 and Tyr-1221 than those at Tyr-1139 and Tyr-1248 (supplemental Fig. S1). Our data indicated that VHR was a cellular PTP against EGFR and ErbB2. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248533 |
Tyr877 |
LDIDETEyHADGGKV |
Homo sapiens |
NCI-H1299 Cell |
pmid |
sentence |
21262974 |
Expression of VHR inhibited the activation of phospholipase Cγ and protein kinase C, both downstream effectors of Tyr-992 phosphorylation of EGFR. | We found that VHR decreased ErbB2 phosphorylation in vitro and in a cellular context, and the dephosphorylation of ErbB2 was more evident at Tyr-877 and Tyr-1221 than those at Tyr-1139 and Tyr-1248 (supplemental Fig. S1). Our data indicated that VHR was a cellular PTP against EGFR and ErbB2. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
TYK2 | up-regulates
phosphorylation
|
DUSP3 |
0.268 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-157655 |
Tyr138 |
SPTLVIAyLMMRQKM |
Homo sapiens |
|
pmid |
sentence |
17785772 |
Phosphorylation of vhr at tyr(138) was required for its phosphatase activity toward stat5. In addition, the src homology 2 domain of stat5 was required for the effective dephosphorylation of stat5 by vhr. The tyrosine kinase tyk2, which mediates the phosphorylation of stat5, was also responsible for the phosphorylation of vhr at tyr(138). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SYK | up-regulates activity
phosphorylation
|
DUSP3 |
0.37 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275999 |
Tyr138 |
SPTLVIAyLMMRQKM |
Chlorocebus aethiops |
COS-1 Cell |
pmid |
sentence |
12447358 |
ZAP-70 and Syk also tyrosine-phosphorylated VHR in COS-1 cells (Fig. 2d), whereas other kinases (Csk, Lck, Fyn, Jak2, Bcr-Abl and Itk) had little effect. Finally, recombinant ZAP-70 readily phosphorylated VHR in vitro (Fig. 2f). |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
ZAP70 | up-regulates
phosphorylation
|
DUSP3 |
0.547 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-95877 |
Tyr138 |
SPTLVIAyLMMRQKM |
Homo sapiens |
|
pmid |
sentence |
12447358 |
We report here that vhr, a vaccinia virus vh1-related dual-specific protein phosphatase that inactivates the mitogen-activated kinases erk2 and jnk, is phosphorylated at y138 by zap-70. Tyr138 phosphorylation was required for vhr to inhibit the erk2-elk-1 pathway |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ZAP70 | up-regulates activity
phosphorylation
|
DUSP3 |
0.547 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276000 |
Tyr138 |
SPTLVIAyLMMRQKM |
Chlorocebus aethiops |
COS-1 Cell |
pmid |
sentence |
12447358 |
ZAP-70 and Syk also tyrosine-phosphorylated VHR in COS-1 cells (Fig. 2d), whereas other kinases (Csk, Lck, Fyn, Jak2, Bcr-Abl and Itk) had little effect. Finally, recombinant ZAP-70 readily phosphorylated VHR in vitro (Fig. 2f). |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
DUSP3 | down-regulates activity
dephosphorylation
|
MAPK1 |
0.658 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248536 |
Tyr187 |
HTGFLTEyVATRWYR |
Chlorocebus aethiops |
COS Cell |
pmid |
sentence |
10224087 |
Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway.|Catalysis by VHR requires the native structure of ERK and is specific for tyrosine 185 of ERK2 |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
DUSP3 | down-regulates activity
dephosphorylation
|
MAPK3 |
0.65 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-103035 |
Tyr204 |
HTGFLTEyVATRWYR |
Homo sapiens |
Dermal Fibroblast |
pmid |
sentence |
12840032 |
The activation of the mapk activity requires the dual phosphorylation of the ser/thr and tyr residues in the txy kinase activation motif (1113), and deactivation occurs through the action of either ser/thr protein phosphatase (14), protein-tyrosine phosphatase (ptp) (14, 15), or dual specificity phosphatases |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248535 |
Tyr204 |
HTGFLTEyVATRWYR |
Chlorocebus aethiops |
COS Cell |
pmid |
sentence |
10224087 |
Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway.|Catalysis by VHR requires the native structure of ERK and is specific for tyrosine 185 of ERK2 |
|
Publications: |
2 |
Organism: |
Homo Sapiens, Chlorocebus Aethiops |
+ |
DUSP3 | down-regulates activity
dephosphorylation
|
Gbeta |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269907 |
|
|
Chlorocebus aethiops |
COS Cell |
pmid |
sentence |
10224087 |
Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway.|Catalysis by VHR requires the native structure of ERK and is specific for tyrosine 185 of ERK2 |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
DUSP3 | down-regulates activity
dephosphorylation
|
STAT3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277070 |
|
|
Homo sapiens |
|
pmid |
sentence |
32475380 |
DUSP3 interacted with the C-terminal domain of STAT3 and dephosphorylated p-Y705 of STAT3.|In summary, DUSP3 downregulated the transcriptional activity of STAT3 via dephosphorylation at Y705 and also suppressed the migratory activity of cancer cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DUSP3 | down-regulates activity
dephosphorylation
|
NPM1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277005 |
|
|
Homo sapiens |
|
pmid |
sentence |
33777934 |
In the absence of DUSP3, these three residues remain phosphorylated and favor the dissociation equilibrium of NPM homo-oligomerization and/or its association with ARF, therefore promoting an early nuc|Therefore, here we focused on the molecular mechanisms used by DUSP3-NPM interaction to affect the abovementioned cellular responses and found out that DUSP3 dephosphorylates three tyrosine residues (Y29, Y67, and Y271) of NPM. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
VRK3 | up-regulates activity
binding
|
DUSP3 |
0.693 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275546 |
|
|
|
|
pmid |
sentence |
27346674 |
Vaccinia-related kinase 3 (VRK3), a member of the VRK family, is widely expressed in human tissues and increases VHR phosphatase activity through a direct binding |
|
Publications: |
1 |
+ |
DUSP3 | down-regulates activity
dephosphorylation
|
ERK1/2 |
0.658 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269928 |
|
|
Chlorocebus aethiops |
COS Cell |
pmid |
sentence |
10224087 |
Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway.|Catalysis by VHR requires the native structure of ERK and is specific for tyrosine 185 of ERK2 |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
DUSP3 | down-regulates activity
dephosphorylation
|
PTK2 |
0.333 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277033 |
|
|
Homo sapiens |
|
pmid |
sentence |
28759036 |
Deficiency in VHR/DUSP3, a suppressor of focal adhesion kinase, reveals its role in regulating cell adhesion and migration.|In vitro assays proved that recombinant VHR directly dephosphorylated FAK and paxillin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |