| + |
CSNK2A1 | down-regulates 
phosphorylation
|
WASF2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182350 |
Ser482 |
RRIAVEYsDSEDDSS |
Homo sapiens |
|
| pmid |
sentence |
| 19012317 |
Here we identify five casein kinase 2 (ck2) phosphorylation sites within the vca domain of wave2, serines 482, 484, 488, 489, and 497. Phosphorylation of these sites is required for a high affinity interaction with the arp2/3 complex;we and show that their mutation to non-phosphorylatable alanine residues inhibits wave2 function in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182354 |
Ser484 |
IAVEYSDsEDDSSEF |
Homo sapiens |
|
| pmid |
sentence |
| 19012317 |
Here we identify five casein kinase 2 (ck2) phosphorylation sites within the vca domain of wave2, serines 482, 484, 488, 489, and 497. Phosphorylation of these sites is required for a high affinity interaction with the arp2/3 complex;we and show that their mutation to non-phosphorylatable alanine residues inhibits wave2 function in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182358 |
Ser488 |
YSDSEDDsSEFDEDD |
Homo sapiens |
|
| pmid |
sentence |
| 19012317 |
Here we identify five casein kinase 2 (ck2) phosphorylation sites within the vca domain of wave2, serines 482, 484, 488, 489, and 497. Phosphorylation of these sites is required for a high affinity interaction with the arp2/3 complex;we and show that their mutation to non-phosphorylatable alanine residues inhibits wave2 function in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182362 |
Ser497 |
EFDEDDWsD |
Homo sapiens |
|
| pmid |
sentence |
| 19012317 |
Here we identify five casein kinase 2 (ck2) phosphorylation sites within the vca domain of wave2, serines 482, 484, 488, 489, and 497. Phosphorylation of these sites is required for a high affinity interaction with the arp2/3 complex;we and show that their mutation to non-phosphorylatable alanine residues inhibits wave2 function in vivo. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
WASF2 | form complex 
binding
|
WAVE complex |
0.907 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261871 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15070726 |
Here we purify Wave-2 from HeLa cells. Five proteins, Sra, Nap, Wave-2, Abi, and Hspc, are copurified, indicating that they form a tight complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DTNBP1 | up-regulates activity 
binding
|
WASF2 |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265659 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 20531346 |
Dysbindin-1, WAVE2 and Abi-1 form a complex that regulates dendritic spine formation. Although dysbindin-1, WAVE2 and Abi-1 form a ternary complex, dysbindin-1 promoted the binding of WAVE2 to Abi-1. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| Tissue: |
Hippocampus |
| + |
BAIAP2 | up-regulates activity
binding
|
WASF2 |
0.794 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265556 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 11130076 |
Here we demonstrate that IRSp53, a substrate for insulin receptor with unknown function, is the 'missing link' between Rac and WAVE. Activated Rac binds to the amino terminus of IRSp53, and carboxy-terminal Src-homology-3 domain of IRSp53 binds to WAVE to form a trimolecular complex. From studies of ectopic expression, we found that IRSp53 is essential for Rac to induce membrane ruffling, probably because it recruits WAVE, which stimulates actin polymerization mediated by the Arp2/3 complex. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
WASF2
- 
- 