| + |
GFs | up-regulates activity 
|
AKT1 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245402 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23300340 |
Akt normally resides in the cytosol under serum-starved conditions, but translocates to the plasma membrane where it is subsequently phosphorylated and activated in response to growth factor treatment. Phosphorylation of Akt at Thr308 by phosphoinositide-dependent kinase-1 (PDK1) and at Ser473 by mammalian target of rapamycin (mTOR) complex 2 (mTORC2) is required for full Akt activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GFs | up-regulates
|
mTORC1 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219382 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23863153 |
Growth factors and nutrients regulate the mTORC1 [mammalian (or mechanistic) target of rapamycin complex 1] by different mechanisms. The players that link growth factors and mTORC1 activation have been known for several years and mouse models have validated its relevance for human physiology and disease. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Autophagy |
| + |
GFs | up-regulates activity
|
AKT2 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245405 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23300340 |
Akt normally resides in the cytosol under serum-starved conditions, but translocates to the plasma membrane where it is subsequently phosphorylated and activated in response to growth factor treatment. Phosphorylation of Akt at Thr308 by phosphoinositide-dependent kinase-1 (PDK1) and at Ser473 by mammalian target of rapamycin (mTOR) complex 2 (mTORC2) is required for full Akt activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GFs | up-regulates 
|
RTKs |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256169 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17306385 |
Multiple growth- and differentiation-inducing polypeptide factors bind to and activate transmembrane receptors tyrosine kinases (RTKs), to instigate a plethora of biochemical cascades culminating in regulation of cell fate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | RTKs in cancer |
| + |
GFs | up-regulates activity
|
AKT |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245411 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23300340 |
Akt normally resides in the cytosol under serum-starved conditions, but translocates to the plasma membrane where it is subsequently phosphorylated and activated in response to growth factor treatment. Phosphorylation of Akt at Thr308 by phosphoinositide-dependent kinase-1 (PDK1) and at Ser473 by mammalian target of rapamycin (mTOR) complex 2 (mTORC2) is required for full Akt activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, RTKs in cancer |
| + |
GFs | up-regulates activity
|
AKT3 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245408 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23300340 |
Akt normally resides in the cytosol under serum-starved conditions, but translocates to the plasma membrane where it is subsequently phosphorylated and activated in response to growth factor treatment. Phosphorylation of Akt at Thr308 by phosphoinositide-dependent kinase-1 (PDK1) and at Ser473 by mammalian target of rapamycin (mTOR) complex 2 (mTORC2) is required for full Akt activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
GFs