| + |
ENAH | up-regulates 
|
Axonal_growth_cone_formation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268389 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18508258 |
Here we review recent findings into Ena/VASP function in neurite initiation, axon outgrowth and guidance. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
BAIAP2 | up-regulates activity 
binding
|
ENAH |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268423 |
|
|
Homo sapiens |
Fibroblast |
| pmid |
sentence |
| 11696321 |
We conclude that the interaction of Cdc42 with the partial CRIB motif of IRSp53 relieves an intramolecular, autoinhibitory interaction with the N terminus, allowing the recruitment of Mena to the IRSp53 SH3 domain. This IRSp53:Mena complex initiates actin filament assembly into filopodia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
PRKG1 | down-regulates activity 
phosphorylation
|
ENAH |
0.308 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268288 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15066263 |
Vertebrate Ena/VASP proteins are phosphorylated by PKA, as well as PKG, and the phosphorylation is required for full function in a number of cellular contexts. PKG may preferentially phosphorylate sites of Ena/VASP proteins that reduce or inactivate these proteins. Inactivated Ena/VASP proteins dissociate from actin filaments, allowing capping proteins to bind and block monomer addition to plus ends, resulting in filament retraction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
ENAH | up-regulates
|
Neurite_outgrowth |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268392 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18508258 |
Here we review recent findings into Ena/VASP function in neurite initiation, axon outgrowth and guidance. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
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 |
| + |
PKA | up-regulates activity
phosphorylation
|
ENAH |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268285 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15066263 |
Vertebrate Ena/VASP proteins are phosphorylated by PKA, as well as PKG, and the phosphorylation is required for full function in a number of cellular contexts |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
3.0
ENAH
- 
- 