| + |
PTPN12 | down-regulates 
dephosphorylation
|
GIT2 |
0.356 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142711 |
Tyr286 |
EELAMDVyDEVDRRE |
Homo sapiens |
|
| pmid |
sentence |
| 16317044 |
Conversely, a gfp-pkl phosphorylation mutant, y286/392/592f (gfp-pkl triple yf) (brown et al., 2005), was not phosphorylated during adhesion and the addition of ptp-pest had no effect, suggesting one or more of these tyrosine residues are dephosphorylated by ptppest. Taken together, these data strongly suggest pkl as a direct substrate for ptp-pest. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142715 |
Tyr392 |
QDNDQPDyDSVASDE |
Homo sapiens |
|
| pmid |
sentence |
| 16317044 |
Conversely, a gfp-pkl phosphorylation mutant, y286/392/592f (gfp-pkl triple yf) (brown et al., 2005), was not phosphorylated during adhesion and the addition of ptp-pest had no effect, suggesting one or more of these tyrosine residues are dephosphorylated by ptppest. Taken together, these data strongly suggest pkl as a direct substrate for ptp-pest. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142719 |
Tyr592 |
NSTPESDyDNTPNDM |
Homo sapiens |
|
| pmid |
sentence |
| 16317044 |
Conversely, a gfp-pkl phosphorylation mutant, y286/392/592f (gfp-pkl triple yf) (brown et al., 2005), was not phosphorylated during adhesion and the addition of ptp-pest had no effect, suggesting one or more of these tyrosine residues are dephosphorylated by ptppest. Taken together, these data strongly suggest pkl as a direct substrate for ptp-pest. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
3.0
GIT2
- 
- 