| + |
PTPRT | down-regulates activity 
dephosphorylation
|
STAT3 |
0.531 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263981 |
Tyr705 |
DPGSAAPyLKTKFIC |
Homo sapiens |
HCT-116 Cell, HT-29 Cell |
| pmid |
sentence |
| 17360477 |
Identification of STAT3 as a substrate of receptor protein tyrosine phosphatase T|Phosphorylation of a tyrosine at amino acid Y705 is essential for the function of STAT3, and PTPRT specifically dephosphorylated STAT3 at this position. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277043 |
|
|
Homo sapiens |
|
| 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. Accordingly, overexpression of normal PTPRT in colorectal cancer cells reduced the expression of STAT3 target genes.|Phosphorylation of a tyrosine at amino acid Y705 is essential for the function of STAT3, and PTPRT specifically dephosphorylated STAT3 at this position. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRT | down-regulates activity
dephosphorylation
|
PXN |
0.474 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263978 |
Tyr88 |
PQSSSPVyGSSAKTS |
Homo sapiens |
HT-29 Cell |
| pmid |
sentence |
| 27447856 |
To this end, using a phospho-proteomics approach, we identified and validated paxillin and STAT3 as the substrates of PTPRT [15, 16]|the PTPRT target site on paxillin is a previously uncharacterized tyrosine-88 residue (paxillin Y88)|In this study, we also show how pY88 paxillin transduces a signal to activate Akt |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FYN | down-regulates activity
phosphorylation
|
PTPRT |
0.425 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275543 |
Tyr915 |
Y-->K |
|
|
| pmid |
sentence |
| 19816407 |
Synapse formation by PTPRT was inhibited by phosphorylation of tyrosine 912 within the membrane-proximal catalytic domain of PTPRT by Fyn. This tyrosine phosphorylation reduced phosphatase activity of PTPRT |
|
| Publications: |
1 |
3.0
PTPRT
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