| + |
GSK3A | down-regulates activity 
phosphorylation
|
GRB14 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264871 |
Ser358 |
MHPYQGRsGCSSQSI |
in vitro |
|
| pmid |
sentence |
| 28130417 |
Phosphorylation of clustered serine residues in the N-terminus of BPS domain negatively regulates formation of the complex between human Grb14 and insulin receptor| In vitro kinase assay using the motif-derived peptides showed that the serine residues located in N-terminal (Ser358, Ser362 and Ser366) and C-terminal (Ser419 and Ser423) regions of the BPS domain were phosphorylated by GSK-3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264870 |
Ser362 |
QGRSGCSsQSISPMR |
in vitro |
|
| pmid |
sentence |
| 28130417 |
Phosphorylation of clustered serine residues in the N-terminus of BPS domain negatively regulates formation of the complex between human Grb14 and insulin receptor| In vitro kinase assay using the motif-derived peptides showed that the serine residues located in N-terminal (Ser358, Ser362 and Ser366) and C-terminal (Ser419 and Ser423) regions of the BPS domain were phosphorylated by GSK-3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264872 |
Ser366 |
GCSSQSIsPMRSISE |
in vitro |
|
| pmid |
sentence |
| 28130417 |
Phosphorylation of clustered serine residues in the N-terminus of BPS domain negatively regulates formation of the complex between human Grb14 and insulin receptor| In vitro kinase assay using the motif-derived peptides showed that the serine residues located in N-terminal (Ser358, Ser362 and Ser366) and C-terminal (Ser419 and Ser423) regions of the BPS domain were phosphorylated by GSK-3. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
GSK3B | down-regulates activity
phosphorylation
|
GRB14 |
0.328 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264868 |
Ser358 |
MHPYQGRsGCSSQSI |
in vitro |
|
| pmid |
sentence |
| 28130417 |
Phosphorylation of clustered serine residues in the N-terminus of BPS domain negatively regulates formation of the complex between human Grb14 and insulin receptor| In vitro kinase assay using the motif-derived peptides showed that the serine residues located in N-terminal (Ser358, Ser362 and Ser366) and C-terminal (Ser419 and Ser423) regions of the BPS domain were phosphorylated by GSK-3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264867 |
Ser362 |
QGRSGCSsQSISPMR |
in vitro |
|
| pmid |
sentence |
| 28130417 |
Phosphorylation of clustered serine residues in the N-terminus of BPS domain negatively regulates formation of the complex between human Grb14 and insulin receptor| In vitro kinase assay using the motif-derived peptides showed that the serine residues located in N-terminal (Ser358, Ser362 and Ser366) and C-terminal (Ser419 and Ser423) regions of the BPS domain were phosphorylated by GSK-3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264869 |
Ser366 |
GCSSQSIsPMRSISE |
in vitro |
|
| pmid |
sentence |
| 28130417 |
Phosphorylation of clustered serine residues in the N-terminus of BPS domain negatively regulates formation of the complex between human Grb14 and insulin receptor| In vitro kinase assay using the motif-derived peptides showed that the serine residues located in N-terminal (Ser358, Ser362 and Ser366) and C-terminal (Ser419 and Ser423) regions of the BPS domain were phosphorylated by GSK-3. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
GRB14 | down-regulates activity
binding
|
INSR |
0.75 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264873 |
|
|
|
|
| pmid |
sentence |
| 24535599 |
Growth factor receptor-bound protein 14 (Grb14) interacts with insulin receptor (IR) through the between PH and SH2 (BPS) domain. Grb14-IR complex formation is initiated by insulin stimulation, and the binding event results in the inhibition of insulin signalling. |
|
| Publications: |
1 |
3.0
GRB14
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