| + |
SRC | up-regulates 
phosphorylation
|
TNS3 |
0.417 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187843 |
Tyr1173 |
QDTSKFWyKADISRE |
Homo sapiens |
Breast Cancer Cell, Lung Cancer Cell, Melanoma Cell |
| pmid |
sentence |
| 19732724 |
Tyrosines in the sh2 domain contribute to the biological activity of tensin-3, and phosphorylation of these tyrosines can regulate ligand binding. tensin-3 is a src substrate |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187847 |
Tyr1206 |
SHSFRGAyGLAMKVA |
Homo sapiens |
Breast Cancer Cell, Lung Cancer Cell, Melanoma Cell |
| pmid |
sentence |
| 19732724 |
Tyrosines in the sh2 domain contribute to the biological activity of tensin-3, and phosphorylation of these tyrosines can regulate ligand binding. tensin-3 is a src substrate |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187851 |
Tyr1256 |
KGCSNEPyFGSLTAL |
Homo sapiens |
Breast Cancer Cell, Lung Cancer Cell, Melanoma Cell |
| pmid |
sentence |
| 19732724 |
Tyrosines in the sh2 domain contribute to the biological activity of tensin-3, and phosphorylation of these tyrosines can regulate ligand binding. tensin-3 is a src substrate |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187854 |
|
|
Homo sapiens |
Breast Cancer Cell, Lung Cancer Cell, Melanoma Cell |
| pmid |
sentence |
| 19732724 |
Although sh2 domains have not been reported previously to be phosphorylated, the tensin-3 sh2 domain is a physiologic substrate for src. Tyrosines in the sh2 domain contribute to the biological activity of tensin-3, and phosphorylation of these tyrosines can regulate ligand binding. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
3.0
TNS3
- 
- 