| + |
ABL1 | up-regulates activity 
phosphorylation
|
RAPH1 |
0.289 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262605 |
Tyr1226 |
GGSHISGyATLRRGP |
in vitro |
|
| pmid |
sentence |
| 20417104 |
Here we show that phosphorylation of Lpd by c-Abl increases its interaction with Ena/VASP proteins. This analysis revealed that, in vitro, four Lpd peptides harboring tyrosines (Y426, Y456, Y513, Y1226) are highly phosphorylated, and eight additional peptides are phosphorylated to a lesser extent (Figure 1C). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262606 |
Tyr426 |
LLRASGIyYVPKGKA |
in vitro |
|
| pmid |
sentence |
| 20417104 |
Here we show that phosphorylation of Lpd by c-Abl increases its interaction with Ena/VASP proteins. This analysis revealed that, in vitro, four Lpd peptides harboring tyrosines (Y426, Y456, Y513, Y1226) are highly phosphorylated, and eight additional peptides are phosphorylated to a lesser extent (Figure 1C). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262607 |
Tyr456 |
NVYYGQDyRNKYKAP |
in vitro |
|
| pmid |
sentence |
| 20417104 |
Here we show that phosphorylation of Lpd by c-Abl increases its interaction with Ena/VASP proteins. This analysis revealed that, in vitro, four Lpd peptides harboring tyrosines (Y426, Y456, Y513, Y1226) are highly phosphorylated, and eight additional peptides are phosphorylated to a lesser extent (Figure 1C). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262608 |
Tyr513 |
GKQLYMNyQEALKRT |
in vitro |
|
| pmid |
sentence |
| 20417104 |
Here we show that phosphorylation of Lpd by c-Abl increases its interaction with Ena/VASP proteins. This analysis revealed that, in vitro, four Lpd peptides harboring tyrosines (Y426, Y456, Y513, Y1226) are highly phosphorylated, and eight additional peptides are phosphorylated to a lesser extent (Figure 1C). |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
RAPH1 | up-regulates activity
binding
|
VASP |
0.597 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268426 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20417104 |
Here we show that Lpd is a substrate of Abl kinases and binds to the Abl SH2 domain. Phosphorylation of Lpd positively regulates the interaction between Lpd and Ena/VASP proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
RAPH1 | up-regulates activity
binding
|
EVL |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268427 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20417104 |
Here we show that Lpd is a substrate of Abl kinases and binds to the Abl SH2 domain. Phosphorylation of Lpd positively regulates the interaction between Lpd and Ena/VASP proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
RAPH1 | up-regulates activity
binding
|
ENAH |
0.56 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268425 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20417104 |
Here we show that Lpd is a substrate of Abl kinases and binds to the Abl SH2 domain. Phosphorylation of Lpd positively regulates the interaction between Lpd and Ena/VASP proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
3.0
RAPH1
- 
- 