| + |
PRKACA | down-regulates activity 
phosphorylation
|
PTPRR |
0.343 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250038 |
Ser339 |
GLQERRGsNVSLTLD |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 10601328 |
The PKA phosphorylation site on PTP-SL was identified as the Ser(231) residue. treatment of COS-7 cells with PKA activators, or overexpression of the Calpha catalytic subunit of PKA, inhibited the cytoplasmic retention of ERK2 and p38alpha by wild-type PTP-SL, but not by a PTP-SL S231A mutant.‚ |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
MAPK1 | up-regulates activity 
phosphorylation
|
PTPRR |
0.823 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249438 |
Thr361 |
EPFVSIPtPREKVAM |
|
|
| pmid |
sentence |
| 11493009 |
Specifically, the complex formation between PTP-SL and ERK2 involves an unusual interaction leading to the phosphorylation of PTP-SL by ERK2 at Thr253 and the inactivating dephosphorylation of ERK2 by PTP-SL. |
|
| Publications: |
1 |
| + |
MAPK3 | up-regulates activity
phosphorylation
|
PTPRR |
0.669 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249477 |
Thr361 |
EPFVSIPtPREKVAM |
|
|
| pmid |
sentence |
| 11493009 |
Specifically, the complex formation between PTP-SL and ERK2 involves an unusual interaction leading to the phosphorylation of PTP-SL by ERK2 at Thr253 and the inactivating dephosphorylation of ERK2 by PTP-SL. |
|
| Publications: |
1 |
| + |
PTPRR | down-regulates activity
dephosphorylation
|
MAPK1 |
0.823 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248840 |
Tyr187 |
HTGFLTEyVATRWYR |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 11493009 |
Specifically, the complex formation between PTP-SL and ERK2 involves an unusual interaction leading to the phosphorylation of PTP-SL by ERK2 at Thr253 and the inactivating dephosphorylation of ERK2 by PTP-SL.|PTP-SL dephosphorylates the regulatory phosphotyrosine on the active loop of ERK1/2. Tyrosine dephosphorylation of ERK1/2 causes the inactivation of ERK1/2 and its retention in the cytoplasm |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PTPRR | down-regulates activity
dephosphorylation
|
MAPK7 |
0.45 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248721 |
Tyr221 |
HQYFMTEyVATRWYR |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 12042304 |
In this study we concentrated on whether and how PTP-SL, a kinase-interacting motif-containing PTP, might be involved in the down-regulation of the ERK5 signal|Whereas inactivation of ERK5 by PTP-SL monitored in vitro is most probably simply due to the dephosphorylation of tyrosine 220 in the activating TEY motif |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PTPRR | down-regulates activity
dephosphorylation
|
STAT3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248719 |
Tyr705 |
DPGSAAPyLKTKFIC |
Homo sapiens |
Colorectal Cancer Cell Line |
| pmid |
sentence |
| 17360477 |
Here, we report identification of signal transducer and activator of transcription 3 (STAT3) as a substrate of PTPRT. Phosphorylation of a tyrosine at amino acid Y705 is essential for the function of STAT3, and PTPRT specifically dephosphorylated STAT3 at this position. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRR | down-regulates activity
dephosphorylation
|
PXN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248720 |
Tyr88 |
PQSSSPVyGSSAKTS |
Homo sapiens |
|
| pmid |
sentence |
| 20133777 |
Here, we show that paxillin is a direct substrate of PTPRT and that PTPRT specifically regulates paxillin phosphorylation at tyrosine residue 88 (Y88) in colorectal cancer (CRC) cells. We engineered CRC cells homozygous for a paxillin Y88F knock-in mutant and found that these cells exhibit significantly reduced cell migration and impaired anchorage-independent growth, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | up-regulates activity
phosphorylation
|
PTPRR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270147 |
|
|
|
|
| pmid |
sentence |
| 11493009 |
Specifically, the complex formation between PTP-SL and ERK2 involves an unusual interaction leading to the phosphorylation of PTP-SL by ERK2 at Thr253 and the inactivating dephosphorylation of ERK2 by PTP-SL. |
|
| Publications: |
1 |
| + |
Gbeta | up-regulates activity
phosphorylation
|
PTPRR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270021 |
|
|
|
|
| pmid |
sentence |
| 11493009 |
Specifically, the complex formation between PTP-SL and ERK2 involves an unusual interaction leading to the phosphorylation of PTP-SL by ERK2 at Thr253 and the inactivating dephosphorylation of ERK2 by PTP-SL. |
|
| Publications: |
1 |
| + |
PTPRR | down-regulates
dephosphorylation
|
MAPK14 |
0.556 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-111762 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11711538 |
As shown, gst-ptp-sl dephosphorylated efficiently both erk2 and p38 wild typetogether, these results indicate that the defective association of the tyrosine phosphatase ptp-sl with erk2 d319n and p38 d316n mutations impairs the retention and inactivation in the cytosol of these map kinases by ptp-sl. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
PTPRR
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