| + |
SGK2 | down-regulates activity 
phosphorylation
|
FOXO3 |
0.511 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249130 |
Ser253 |
APRRRAVsMDNSNKY |
Homo sapiens |
|
| pmid |
sentence |
| 11154281 |
Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a)|However, SGK and Akt display differences with respect to the efficacy with which they phosphorylate the three regulatory sites on FKHRL1. While both kinases can phosphorylate Thr-32, SGK displays a marked preference for Ser-315 whereas Akt favors Ser-253. These findings suggest that SGK and Akt may coordinately regulate the function of FKHRL1 by phosphorylating this transcription factor at distinct sites. The efficient phosphorylation of these three sites on FKHRL1 by SGK and Akt appears to be critical to the ability of growth factors to suppress FKHRL1-dependent transcription, thereby preventing FKHRL1 from inducing cell cycle arrest and apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249132 |
Thr32 |
QSRPRSCtWPLQRPE |
Homo sapiens |
|
| pmid |
sentence |
| 11154281 |
Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a)|However, SGK and Akt display differences with respect to the efficacy with which they phosphorylate the three regulatory sites on FKHRL1. While both kinases can phosphorylate Thr-32, SGK displays a marked preference for Ser-315 whereas Akt favors Ser-253. These findings suggest that SGK and Akt may coordinately regulate the function of FKHRL1 by phosphorylating this transcription factor at distinct sites. The efficient phosphorylation of these three sites on FKHRL1 by SGK and Akt appears to be critical to the ability of growth factors to suppress FKHRL1-dependent transcription, thereby preventing FKHRL1 from inducing cell cycle arrest and apoptosis. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SGK2 | down-regulates activity
phosphorylation
|
FOXO |
0.513 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252990 |
Ser253 |
APRRRAVsMDNSNKY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11154281 |
Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a)|However, SGK and Akt display differences with respect to the efficacy with which they phosphorylate the three regulatory sites on FKHRL1. While both kinases can phosphorylate Thr-32, SGK displays a marked preference for Ser-315 whereas Akt favors Ser-253. These findings suggest that SGK and Akt may coordinately regulate the function of FKHRL1 by phosphorylating this transcription factor at distinct sites. The efficient phosphorylation of these three sites on FKHRL1 by SGK and Akt appears to be critical to the ability of growth factors to suppress FKHRL1-dependent transcription, thereby preventing FKHRL1 from inducing cell cycle arrest and apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252991 |
Thr32 |
QSRPRSCtWPLQRPE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11154281 |
Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a)|However, SGK and Akt display differences with respect to the efficacy with which they phosphorylate the three regulatory sites on FKHRL1. While both kinases can phosphorylate Thr-32, SGK displays a marked preference for Ser-315 whereas Akt favors Ser-253. These findings suggest that SGK and Akt may coordinately regulate the function of FKHRL1 by phosphorylating this transcription factor at distinct sites. The efficient phosphorylation of these three sites on FKHRL1 by SGK and Akt appears to be critical to the ability of growth factors to suppress FKHRL1-dependent transcription, thereby preventing FKHRL1 from inducing cell cycle arrest and apoptosis. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PDPK1 | up-regulates activity 
phosphorylation
|
SGK2 |
0.576 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250376 |
Ser416 |
SSAFLGFsYAPEDDD |
|
|
| pmid |
sentence |
| 10548550 |
SGK2 and SGK3 are activated in vitro by PDK1, albeit more slowly than SGK1, and their activation is accompanied by the phosphorylation of Thr(193) and Thr(253) respectively. The PDK1-catalysed phosphorylation and activation of SGK2 and SGK3, like SGK1, is greatly potentiated by mutating Ser(356) and Ser(419) respectively to Asp, these residues being equivalent to the C-terminal phosphorylation site of PKB. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250277 |
Thr193 |
EPEDTTStFCGTPEY |
|
|
| pmid |
sentence |
| 10548550 |
SGK2 and SGK3 are activated in vitro by PDK1, albeit more slowly than SGK1, and their activation is accompanied by the phosphorylation of Thr(193) and Thr(253) respectively. The PDK1-catalysed phosphorylation and activation of SGK2 and SGK3, like SGK1, is greatly potentiated by mutating Ser(356) and Ser(419) respectively to Asp, these residues being equivalent to the C-terminal phosphorylation site of PKB. |
|
| Publications: |
2 |
| + |
2-cyclopentyl-4-(5-phenyl-1H-pyrrolo[2,3-b]pyridin-3-yl)benzoic acid | down-regulates activity
chemical inhibition
|
SGK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262018 |
|
|
in vitro |
|
| pmid |
sentence |
| 18794135 |
GSK650394 quantitatively inhibits the activity of SGK1 and SGK2 in a scintillation proximity assay. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PDPK1 | up-regulates
phosphorylation
|
SGK2 |
0.576 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126177 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15209375 |
One of the most studiedevents controlled by ptdins(3,4,5)p3, comprises the activation of aof agc family protein kinases, including isoforms of protein kinase b (pkb)/akt, p70 ribosomal s6 kinase (s6k), serum- and glucocorticoid-induced protein kinase (sgk) and protein kinase c (pkc), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (pdk1), which phosphorylates and activates the agc kinase members regulated by pi 3-kinase. We also discuss whether inhibitors of pdk1 might have chemotherapeutic potential in the treatment of cancers in which the pdk1-regulated agc kinases are constitutively activated. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SGK2
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