| + |
MAPK1 |
phosphorylation
|
AHNAK |
0.261 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262762 |
Ser216 |
PSGSGAAsPTGSAVD |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 22028470 |
We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262763 |
Ser5099 |
DVEFDIKsPKFKAEA |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 22028470 |
We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262764 |
Ser5110 |
KAEAPLPsPKLEGEL |
Mus musculus |
|
| pmid |
sentence |
| 22028470 |
We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262767 |
Thr5794 |
REFSGPStPTGTLEF |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 22028470 |
We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262768 |
Thr694 |
LPDMSVKtPKISMPD |
Mus musculus |
|
| pmid |
sentence |
| 22028470 |
We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1) |
|
| Publications: |
5 |
Organism: |
Mus Musculus |
3.0
AHNAK
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- 