| + |
HCK | up-regulates 
phosphorylation
|
ELMO1 |
0.59 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138142 |
Tyr18 |
AIEWPGAyPKLMEID |
Homo sapiens |
|
| pmid |
sentence |
| 15952790 |
We previously showed that elmo1 binds directly to the hck sh3 domain and is phosphorylated by hck. In this study, we used mass spectrometry to identify the following sites of elmo1 phosphorylation: tyr 18, tyr 216, tyr 511, tyr 395, and tyr 720. Mutant forms of elmo1 lacking these sites were defective in their ability to promote phagocytosis and migration in fibroblasts. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138146 |
Tyr216 |
VLNSHDLyQKVAQEI |
Homo sapiens |
|
| pmid |
sentence |
| 15952790 |
We previously showed that elmo1 binds directly to the hck sh3 domain and is phosphorylated by hck. In this study, we used mass spectrometry to identify the following sites of elmo1 phosphorylation: tyr 18, tyr 216, tyr 511, tyr 395, and tyr 720. Mutant forms of elmo1 lacking these sites were defective in their ability to promote phagocytosis and migration in fibroblasts. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138150 |
Tyr395 |
AKHHQDAyIRIVLEN |
Homo sapiens |
|
| pmid |
sentence |
| 15952790 |
We previously showed that elmo1 binds directly to the hck sh3 domain and is phosphorylated by hck. In this study, we used mass spectrometry to identify the following sites of elmo1 phosphorylation: tyr 18, tyr 216, tyr 511, tyr 395, and tyr 720. Mutant forms of elmo1 lacking these sites were defective in their ability to promote phagocytosis and migration in fibroblasts. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138154 |
Tyr511 |
SKLQNLSyTEILKIR |
Homo sapiens |
|
| pmid |
sentence |
| 15952790 |
We previously showed that elmo1 binds directly to the hck sh3 domain and is phosphorylated by hck. In this study, we used mass spectrometry to identify the following sites of elmo1 phosphorylation: tyr 18, tyr 216, tyr 511, tyr 395, and tyr 720. Mutant forms of elmo1 lacking these sites were defective in their ability to promote phagocytosis and migration in fibroblasts. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138158 |
Tyr720 |
IPKEPSNyDFVYDCN |
Homo sapiens |
|
| pmid |
sentence |
| 15952790 |
We previously showed that elmo1 binds directly to the hck sh3 domain and is phosphorylated by hck. In this study, we used mass spectrometry to identify the following sites of elmo1 phosphorylation: tyr 18, tyr 216, tyr 511, tyr 395, and tyr 720. Mutant forms of elmo1 lacking these sites were defective in their ability to promote phagocytosis and migration in fibroblasts. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
3.0
ELMO1
- 
- 