| + |
BAIAP2 | up-regulates activity 
binding
|
ENAH |
0.587 |
| 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 |
| + |
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 |
0.53 |
| 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 |
| + |
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 |
| + |
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 |
| + |
FAT1 | up-regulates activity
binding
|
ENAH |
0.395 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282692 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15343270 |
FAT1 is localized to the leading edge of lamellipodia, filopodia, and microspike tips where FAT1 directly interacts with Ena/VASP proteins that regulate the actin polymerization complex. When targeted to mitochondrial outer leaflets, FAT1 cytoplasmic domain recruits components of the actin polymerization machinery sufficient to induce ectopic actin polymerization. In an epithelial cell wound model, FAT1 knockdown decreased recruitment of endogenous VASP to the leading edge and resulted in impairment of lamellipodial dynamics, failure of polarization, and an attenuation of cell migration. FAT1 binds to and colocalizes with VASP and Mena via two EVH1-binding domains |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKG1 | down-regulates activity 
phosphorylation
|
ENAH |
0.3 |
| 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 |
4.0
ENAH
- 
- 