| + |
ERK1/2 | down-regulates quantity by destabilization 
phosphorylation
|
LIMA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263062 |
Ser362 |
PVHPKPLsPDSRASS |
Homo sapiens |
Prostate Cancer Cell Line |
| pmid |
sentence |
| 23188829 |
Mechanistic study revealed that EGF could activate the phosphorylation, ubiquitination, and degradation of EPLIN through an extracellular signal-regulated kinase 1/2 (ERK1/2)-dependent signaling cascade. Pharmacological inhibition of the ERK1/2 pathway effectively antagonized EGF-induced EPLIN degradation. Two serine residues, i.e. serine 362 and serine 604, were identified as putative ERK1/2 phosphorylation sites in human EPLIN, whose point mutation rendered resistance to EGF-induced protein turnover. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263063 |
Ser604 |
FQSTSVKsPKTVSPP |
Homo sapiens |
Prostate Cancer Cell Line |
| pmid |
sentence |
| 23188829 |
Mechanistic study revealed that EGF could activate the phosphorylation, ubiquitination, and degradation of EPLIN through an extracellular signal-regulated kinase 1/2 (ERK1/2)-dependent signaling cascade. Pharmacological inhibition of the ERK1/2 pathway effectively antagonized EGF-induced EPLIN degradation. Two serine residues, i.e. serine 362 and serine 604, were identified as putative ERK1/2 phosphorylation sites in human EPLIN, whose point mutation rendered resistance to EGF-induced protein turnover. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | down-regulates quantity by destabilization
phosphorylation
|
LIMA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263054 |
Ser362 |
PVHPKPLsPDSRASS |
Homo sapiens |
Prostate Cancer Cell Line |
| pmid |
sentence |
| 23188829 |
Mechanistic study revealed that EGF could activate the phosphorylation, ubiquitination, and degradation of EPLIN through an extracellular signal-regulated kinase 1/2 (ERK1/2)-dependent signaling cascade. Pharmacological inhibition of the ERK1/2 pathway effectively antagonized EGF-induced EPLIN degradation. Two serine residues, i.e. serine 362 and serine 604, were identified as putative ERK1/2 phosphorylation sites in human EPLIN, whose point mutation rendered resistance to EGF-induced protein turnover. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263055 |
Ser604 |
FQSTSVKsPKTVSPP |
Homo sapiens |
|
| pmid |
sentence |
| 23188829 |
Mechanistic study revealed that EGF could activate the phosphorylation, ubiquitination, and degradation of EPLIN through an extracellular signal-regulated kinase 1/2 (ERK1/2)-dependent signaling cascade. Pharmacological inhibition of the ERK1/2 pathway effectively antagonized EGF-induced EPLIN degradation. Two serine residues, i.e. serine 362 and serine 604, were identified as putative ERK1/2 phosphorylation sites in human EPLIN, whose point mutation rendered resistance to EGF-induced protein turnover. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
4.0
LIMA1
- 
- 