| + |
SGK1 | down-regulates activity 
phosphorylation
|
TSC2 |
0.597 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277266 |
Ser1130 |
GARDRVRsMSGGHGL |
in vitro |
|
| pmid |
sentence |
| 27451907 |
SGK1, which is activated by PDK1, contributes to the maintenance of residual mTORC1 activity through direct phosphorylation and inhibition of TSC2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277265 |
Ser1132 |
RDRVRSMsGGHGLRV |
in vitro |
|
| pmid |
sentence |
| 27451907 |
SGK1, which is activated by PDK1, contributes to the maintenance of residual mTORC1 activity through direct phosphorylation and inhibition of TSC2. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
SGK1 | up-regulates activity 
phosphorylation
|
WNK4 |
0.425 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276421 |
Ser1201 |
FPTSRRNsLQRSEPP |
in vitro |
|
| pmid |
sentence |
| 23054253 |
In addition, we identified a novel SGK1 phosphorylation site (S1201) in WNK4, and phosphorylation at this site is reduced by Ca(2+)/CaM. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SGK1 | down-regulates activity
phosphorylation
|
KMT2D |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277447 |
Ser1331 |
RGRARLKsTASSIET |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 30943409 |
Elevated SGK1, in turn, phosphorylates KMT2D, suppressing its function, leading to a loss of methylation of lysine 4 on histone H3 (H3K4) and a repressive chromatin state at ER loci to attenuate ER activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGK1 | down-regulates activity
phosphorylation
|
MAP3K3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250004 |
Ser166 |
EPRSRHLsVSSQNPG |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 12392720 |
It was shown that the recombinant MEKK3 protein and fluorescein-labeled MEKK3 peptides (FITC-(159)epRsRhlSVi(168) and FITC-(330)dpRgRlpSAd(339)) are phosphorylated by SGK1 in vitro. It was also observed that the intrinsic kinase activity of MEKK3 on Ser(189) of MKK3 (equivalent to Ser(207) of MKK6) decreased along with phosphorylation of Ser(166) and Ser(337) in MEKK3 in vitro and in vivo. Therefore, it is suggested that SGK1 inhibits MEKK3-MKK3/6 signal transduction by phosphorylation of MEKK3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101211 |
Ser166 |
EPRSRHLsVSSQNPG |
Homo sapiens |
|
| pmid |
sentence |
| 12761204 |
Inhibition of mitogen-activated kinase kinase kinase 3 activity through phosphorylation by the serum- and glucocorticoid-induced kinase 1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101216 |
Ser337 |
DPRGRLRsADSENAL |
Homo sapiens |
|
| pmid |
sentence |
| 12761205 |
Inhibition of mitogen-activated kinase kinase kinase 3 activity through phosphorylation by the serum- and glucocorticoid-induced kinase 2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250005 |
Ser337 |
DPRGRLRsADSENAL |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 12392720 |
It was shown that the recombinant MEKK3 protein and fluorescein-labeled MEKK3 peptides (FITC-(159)epRsRhlSVi(168) and FITC-(330)dpRgRlpSAd(339)) are phosphorylated by SGK1 in vitro. It was also observed that the intrinsic kinase activity of MEKK3 on Ser(189) of MKK3 (equivalent to Ser(207) of MKK6) decreased along with phosphorylation of Ser(166) and Ser(337) in MEKK3 in vitro and in vivo. Therefore, it is suggested that SGK1 inhibits MEKK3-MKK3/6 signal transduction by phosphorylation of MEKK3. |
|
| Publications: |
4 |
Organism: |
Chlorocebus Aethiops, Homo Sapiens |
| + |
SGK1 | up-regulates activity
phosphorylation
|
NR3C1 |
0.474 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251669 |
Ser203 |
DLEFSSGsPGKETNE |
Homo sapiens |
|
| pmid |
sentence |
| 23650397 |
SGK1 also potentiated and maintained GR activation in the presence of cortisol, and even after cortisol withdrawal, by increasing GR phosphorylation and GR nuclear translocation|Having demonstrated that SGK1 mediates the cortisol-induced increase in GR phosphorylation at the S203 and S211 phospho-sites, which enhance GR nuclear translocation, but not at the S226 site, which inhibits nuclear translocation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251670 |
Ser211 |
PGKETNEsPWRSDLL |
Homo sapiens |
|
| pmid |
sentence |
| 23650397 |
SGK1 also potentiated and maintained GR activation in the presence of cortisol, and even after cortisol withdrawal, by increasing GR phosphorylation and GR nuclear translocation|Having demonstrated that SGK1 mediates the cortisol-induced increase in GR phosphorylation at the S203 and S211 phospho-sites, which enhance GR nuclear translocation, but not at the S226 site, which inhibits nuclear translocation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SGK1 | down-regulates
phosphorylation
|
MAPT |
0.336 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161288 |
Ser214 |
GGKERPGsKEEVDED |
Homo sapiens |
|
| pmid |
sentence |
| 16982696 |
Second, sgk1 indirectly depolymerized mts through the phosphorylation of tau at ser214 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGK1 | up-regulates
phosphorylation
|
FBXW7 |
0.296 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170404 |
Ser227 |
QQRRRITsVQPPTGL |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 21147854 |
Here, we report that the serum- and glucocorticoid-inducible protein kinase sgk1 remarkably reduced the protein stability of the active form of notch1 through fbw7activated sgk1 phosphorylated fbw7 at serine 227 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGK1 | down-regulates activity
phosphorylation
|
FOXO |
0.787 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252987 |
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-252989 |
Ser315 |
DFRSRTNsNASTVSG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11154281 |
We show here that sgk1, like akt, promotes cell survival and that it does so in part by phosphorylating and inactivating fkhrl1. 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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252988 |
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: |
3 |
Organism: |
Homo Sapiens |
| + |
SGK1 | down-regulates activity
phosphorylation
|
FOXO3 |
0.787 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249133 |
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-236607 |
Ser315 |
DFRSRTNsNASTVSG |
Homo sapiens |
|
| pmid |
sentence |
| 11154281 |
We show here that sgk1, like akt, promotes cell survival and that it does so in part by phosphorylating and inactivating fkhrl1. 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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249134 |
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: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Insulin Signaling |
| + |
SGK1 | up-regulates activity
phosphorylation
|
SLC2A4 |
0.318 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236653 |
Ser274 |
LERERPLsLLQLLGS |
Xenopus laevis |
|
| pmid |
sentence |
| 17382906 |
We evaluated the putative role of sgk1 in the modulation of glut4. Coexpression of the kinase along with glut4 in xenopus oocytes stimulated glucose transport. The enhanced glut4 activity was paralleled by increased transporter abundance in the plasma membrane. Disruption of the sgk1 phosphorylation site on glut4 ((s274a)glut4) abrogated the stimulating effect of sgk1. In summary, sgk1 promotes glucose transporter membrane abundance via glut4 phosphorylation at ser274. |
|
| Publications: |
1 |
Organism: |
Xenopus Laevis |
| Tissue: |
Muscle |
| Pathways: | Insulin Signaling |
| + |
SGK1 | up-regulates activity
phosphorylation
|
MAPK1 |
0.314 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276223 |
Ser29 |
GPRYTNLsYIGEGAY |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 19447520 |
SGK1 was found to physically interact with ERK1/2 as well as MEK1/2. Furthermore, SGK1 mediated the phosphorylation of ERK2 on Ser(29) in a serum-dependent manner. Replacement of Ser(29) to aspartic acid, which mimics the phosphorylation of Ser(29), enhanced the ERK2 activity as well as the MEK/ERK complexes formation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGK1 | down-regulates
phosphorylation
|
NDRG1 |
0.588 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164898 |
Ser330 |
LMRSRTAsGSSVTSL |
Homo sapiens |
|
| pmid |
sentence |
| 20416281 |
Ndrg1/cap43 is phosphorylated at serine/threonine sites in its c-terminal domain by serum- and glucocorticoid-regulated kinase 1 (sgk1). we further introduced mutations at the serine and threonine sites at 328 [t328a], 330 [s330a] and 346 [t346a], which are susceptible to phosphorylation by sgk1, and also constructed double mutants [t328a, s330a], [t328a, t346a] and [s330a, t346a]. Expression of all these mutants, with the exception of [s330a, t346a], suppressed the production of cxc chemokine to similar levels as their wild-type counterpart. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGK1 | up-regulates
phosphorylation
|
NDRG2 |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129672 |
Ser332 |
LSRSRTAsLTSAASV |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15461589 |
Sgk1 phosphorylated ndrg2 at thr330, ser332 and thr348 in vitro. for example, the phosphorylation of thr330 or ser332 by sgk1 may prime ndrg2 for phosphorylation by gsk3 at ser326 and ser328 respectively, for example, the phosphorylation of thr330 or ser332 by sgk1 may prime ndrg2 for phosphorylation by gsk3 at ser326 and ser328 respectively, the phosphorylation of thr348 by sgk1 may prime for phosphorylation at ser344 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129676 |
Thr330 |
TRLSRSRtASLTSAA |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15461589 |
Sgk1 phosphorylated ndrg2 at thr330, ser332 and thr348 in vitro. for example, the phosphorylation of thr330 or ser332 by sgk1 may prime ndrg2 for phosphorylation by gsk3 at ser326 and ser328 respectively, for example, the phosphorylation of thr330 or ser332 by sgk1 may prime ndrg2 for phosphorylation by gsk3 at ser326 and ser328 respectively, the phosphorylation of thr348 by sgk1 may prime for phosphorylation at ser344 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129680 |
Thr348 |
GNRSRSRtLSQSSES |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15461589 |
Sgk1 phosphorylated ndrg2 at thr330, ser332 and thr348 in vitro. for example, the phosphorylation of thr330 or ser332 by sgk1 may prime ndrg2 for phosphorylation by gsk3 at ser326 and ser328 respectively, for example, the phosphorylation of thr330 or ser332 by sgk1 may prime ndrg2 for phosphorylation by gsk3 at ser326 and ser328 respectively, the phosphorylation of thr348 by sgk1 may prime for phosphorylation at ser344 |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle, Lung |
| + |
SGK1 | up-regulates
phosphorylation
|
NEDD4L |
0.78 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-113052 |
Ser342 |
SSRLRSCsVTDAVAE |
Homo sapiens |
|
| pmid |
sentence |
| 11742982 |
Here we show by expression studies in xenopus laevis oocytes that the aldosterone-induced sgk1 kinase interacts with the ubiquitin protein ligase nedd4-2 in a py motif-dependent manner and phosphorylates nedd4-2 on ser444 and, to a lesser extent, ser338. Such phosphorylation reduces the interaction between nedd4-2 and enac, leading to elevated enac cell surface expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGK1 | down-regulates activity
phosphorylation
|
MKNK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277357 |
Ser352 |
SEAKDLIsKLLVRDA |
in vitro |
|
| pmid |
sentence |
| 28545025 |
We show that SGK1 phosphorylates MNK1 at a conserved site, which represses its activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277357 |
Ser353 |
S-->K |
in vitro |
|
| pmid |
sentence |
| 28545025 |
We show that SGK1 phosphorylates MNK1 at a conserved site, which represses its activity. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
NEK6 | up-regulates activity
phosphorylation
|
SGK1 |
0.344 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262954 |
Ser377 |
PPFNPNVsGPNDLRH |
in vitro |
|
| pmid |
sentence |
| 12023960 |
In contrast, we demonstrate for the first time that NEK6 phosphorylates SGK1 efficiently at its hydrophobic motif in vitro and peptide-mapping analysis indicates that this is the major site of phosphorylation (Fig 3). Ser377 is a more minor site of phosphorylation located in the kinase domain of SGK1, which has not been reported to undergo phosphorylation previously. the phosphorylation of the hydrophobic motif of SGK1 in vitro, coupled with the phosphorylation of the T-loop with PDK1, may be a useful way of generating fully active wild type SGK1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250296 |
Ser377 |
PPFNPNVsGPNDLRH |
in vitro |
|
| pmid |
sentence |
| 12023960 |
The present study is the first report of a protein kinase (NEK6) capable of phosphorylating the hydrophobic motif of SGK1, although our data suggest that NEK6 may not mediate this reaction in cells. Nevertheless, the phosphorylation of the hydrophobic motif of SGK1in vitro, coupled with the phosphorylation of the T-loop with PDK1, may be a useful way of generating fully active wild type SGK1. Ser377 and Ser422of SGK1, and the CDK7 T-loop peptide, which are phosphorylated by NEK6. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250297 |
Ser422 |
AEAFLGFsYAPPTDS |
in vitro |
|
| pmid |
sentence |
| 12023960 |
The present study is the first report of a protein kinase (NEK6) capable of phosphorylating the hydrophobic motif of SGK1, although our data suggest that NEK6 may not mediate this reaction in cells. Nevertheless, the phosphorylation of the hydrophobic motif of SGK1in vitro, coupled with the phosphorylation of the T-loop with PDK1, may be a useful way of generating fully active wild type SGK1. Ser377 and Ser422of SGK1, and the CDK7 T-loop peptide, which are phosphorylated by NEK6. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
SGK1 | down-regulates
phosphorylation
|
HTT |
0.382 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121349 |
Ser419 |
GGRSRSGsIVELIAG |
Homo sapiens |
|
| pmid |
sentence |
| 14725621 |
The serum- and glucocorticoid-induced kinase sgk inhibits mutant huntingtin-induced toxicity by phosphorylating serine 421 of huntingtin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MTOR | up-regulates
phosphorylation
|
SGK1 |
0.844 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181531 |
Ser422 |
AEAFLGFsYAPPTDS |
Homo sapiens |
|
| pmid |
sentence |
| 18925875 |
Mtorc2 immunoprecipitated from wild-type, but not from mlst8- or rictor-knockout cells, phosphorylated sgk1 at ser(422) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179113 |
Ser422 |
AEAFLGFsYAPPTDS |
Homo sapiens |
|
| pmid |
sentence |
| 18570873 |
Mtor phosphorylated sgk1, but not sgk1-s422a, in vitro. Sgk1 phosphorylated p27 in vitro. These data implicate sgk1 as an mtorc1 (mtor-raptor) substrate. mtor may promote g1 progression in part through sgk1 activation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
mTORC2 | up-regulates
phosphorylation
|
SGK1 |
0.654 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217016 |
Ser422 |
AEAFLGFsYAPPTDS |
Homo sapiens |
|
| pmid |
sentence |
| 18925875 |
Mtorc2 immunoprecipitated from wild-type, but not from mlst8- or rictor-knockout cells, phosphorylated sgk1 at ser(422) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
mTORC1 | up-regulates activity
phosphorylation
|
SGK1 |
0.608 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217078 |
Ser422 |
AEAFLGFsYAPPTDS |
in vitro |
|
| pmid |
sentence |
| 18570873 |
Mtor phosphorylated sgk1, but not sgk1-s422a, in vitro. Sgk1 phosphorylated p27 in vitro. These data implicate sgk1 as an mtorc1 (mtor-raptor) substrate. mtor may promote g1 progression in part through sgk1 activation |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Insulin Signaling |
| + |
PDPK1 | up-regulates activity
phosphorylation
|
SGK1 |
0.634 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250274 |
Ser422 |
AEAFLGFsYAPPTDS |
in vitro |
|
| pmid |
sentence |
| 10191262 |
The activation of SGK by PDK1 in vitro is unaffected by PtdIns(3,4,5)P3, abolished by the mutation of Ser422 to Ala, and greatly potentiated by mutation of Ser422 to Asp |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250275 |
Thr256 |
EHNSTTStFCGTPEY |
in vitro |
|
| pmid |
sentence |
| 10191262 |
PDK1 activates SGK in vitro by phosphorylating Thr256. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| Pathways: | Insulin Signaling |
| + |
SGK1 | down-regulates quantity by destabilization
phosphorylation
|
NCSTN |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276415 |
Ser437 |
FLRARNIsGVVLADH |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22590650 |
SGK1 directly bound to and phosphorylated NCT on Ser437, thereby promoting protein degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGK1 | down-regulates
phosphorylation
|
NEDD4L |
0.78 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133438 |
Ser448 |
IRRPRSLsSPTVTLS |
Homo sapiens |
|
| pmid |
sentence |
| 15677482 |
Nedd4-2 function is negatively regulated by phosphorylation via a serum- and glucocorticoid-inducible protein kinase (sgk1), which serves as a mechanism to inhibit the ubiquitination-dependent degradation of enac. Sgk1 catalyzed phosphorylation of hnedd4-2 at ser-468 maintaining hnedd4-2 in an inactive phosphorylated state. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK7 | up-regulates
phosphorylation
|
SGK1 |
0.396 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105728 |
Ser78 |
ANPSPPPsPSQQINL |
Homo sapiens |
|
| pmid |
sentence |
| 11254654 |
Bmk1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinasebmk1 activates sgk by phosphorylation at serine 78. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGK1 | down-regulates
phosphorylation
|
CDKN1B |
0.482 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179117 |
Thr157 |
GIRKRPAtDDSSTQN |
Homo sapiens |
|
| pmid |
sentence |
| 18570873 |
Activated sgk1 and p27 phosphorylation at t157, and both were inhibited by short-term rapamycin treatment and by sgk1 shrna. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGK1 | down-regulates activity
phosphorylation
|
CDKN1B |
0.482 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179121 |
Thr198 |
PGLRRRQt |
Homo sapiens |
|
| pmid |
sentence |
| 18570873 |
Activated sgk1 and p27 phosphorylation at t157, and both were inhibited by short-term rapamycin treatment and by sgk1 shrna.|Akt acts downstream of PI3K to phosphorylate p27 at T157 and T198, leading to impaired nuclear p27 import, p27 accumulation in the cytoplasm, and loss of cyclin E-Cdk2 inhibition |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGK1 | down-regulates activity
phosphorylation
|
FOXO1 |
0.603 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255925 |
Thr24 |
LPRPRSCtWPLPRPE |
Mus musculus |
|
| pmid |
sentence |
| 19965929 |
We demonstrate that SGK1 affects differentiation by direct phosphorylation of Foxo1, thereby changing its cellular localization from the nucleus to the cytosol. In addition we show that SGK1-/- cells are unable to relocalize Foxo1 to the cytosol in response to dexamethasone. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Insulin Signaling |
| + |
PDPK1 | up-regulates
phosphorylation
|
SGK1 |
0.634 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236637 |
Thr256 |
EHNSTTStFCGTPEY |
Homo sapiens |
|
| pmid |
sentence |
| 15209375 |
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236800 |
Thr256 |
EHNSTTStFCGTPEY |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 12387817 |
Thus, it was suggested that NHERF2 mediates the activation and phosphorylation of SGK1 by PDK1 through its first PDZ domain and PIF motif, as a novel SGK1 activation mechanism. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236796 |
Thr256 |
EHNSTTStFCGTPEY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10191262 |
This is followed by the ptdins(3,4,5)p3-independent phosphorylation at thr256 that activates sgk, and is catalysed by pdk1 |
|
| Publications: |
3 |
Organism: |
Homo Sapiens, Chlorocebus Aethiops |
| Pathways: | Insulin Signaling |
| + |
PDPK2P | up-regulates
phosphorylation
|
SGK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66234 |
Thr256 |
EHNSTTStFCGTPEY |
Homo sapiens |
|
| pmid |
sentence |
| 10191262 |
Our results are consistent with a model in which activation of sgk by igf-1 or hydrogen peroxide is initiated by a ptdins(3,4, 5)p3-dependent activation of pdk2, which phosphorylates ser422. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGK1 | up-regulates
phosphorylation
|
NDRG1 |
0.588 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180821 |
Thr346 |
GTRSRSHtSEGTRSR |
Homo sapiens |
|
| pmid |
sentence |
| 18787837 |
Transient expression of active (sgk1-s422d) and inactive (sgk1-k127a) sgk1 mutants confirmed that activating sgk1 stimulates ndrg1-thr(346/356/366) phosphorylation. dexamethasone (0.2 mum) acutely activated sgk1 and the peak of this response (2-3 h) coincided with the induction of g (na), and both responses were pi3k-dependent. While these data suggest that sgk1 might mediate the rise in g (na), transient expression of the inactive sgk1-k127a mutant did not affect the hormonal induction of g (na) but did suppress the activation of sgk1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180825 |
Thr356 |
GTRSRSHtSEGTRSR |
Homo sapiens |
|
| pmid |
sentence |
| 18787837 |
Transient expression of active (sgk1-s422d) and inactive (sgk1-k127a) sgk1 mutants confirmed that activating sgk1 stimulates ndrg1-thr(346/356/366) phosphorylation. dexamethasone (0.2 mum) acutely activated sgk1 and the peak of this response (2-3 h) coincided with the induction of g (na), and both responses were pi3k-dependent. While these data suggest that sgk1 might mediate the rise in g (na), transient expression of the inactive sgk1-k127a mutant did not affect the hormonal induction of g (na) but did suppress the activation of sgk1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180829 |
Thr366 |
GTRSRSHtSEGAHLD |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18787837 |
Transient expression of active (sgk1-s422d) and inactive (sgk1-k127a) sgk1 mutants confirmed that activating sgk1 stimulates ndrg1-thr(346/356/366) phosphorylation. dexamethasone (0.2 mum) acutely activated sgk1 and the peak of this response (2-3 h) coincided with the induction of g (na), and both responses were pi3k-dependent. While these data suggest that sgk1 might mediate the rise in g (na), transient expression of the inactive sgk1-k127a mutant did not affect the hormonal induction of g (na) but did suppress the activation of sgk1. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKACA | up-regulates activity
phosphorylation
|
SGK1 |
0.3 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275972 |
Thr369 |
DLINKKItPPFNPNV |
in vitro |
|
| pmid |
sentence |
| 11096081 |
In this publication, we demonstrate that cAMP can activate Sgk and that this effect is mediated by PKA, which directly phosphorylates Thr369 in Sgk. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SGK1 | down-regulates activity
phosphorylation
|
NEDD4L |
0.78 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263076 |
Thr383 |
PSVAYVHtTPGLPSG |
in vitro |
|
| pmid |
sentence |
| 12911626 |
Site‐directed mutagenesis of the SGK1 phosphorylation sites in the Nedd4‐2 protein (S382A,S468ANedd4‐2) and in the EAAT1 protein (T482AEAAT1, T482DEAAT1) significantly blunts the effect of S422DSGK1. Introduction of a negative charge at the SGK phosphorylation site in the EAAT1 protein leads to a strong stimulation of the carrier, whereas replacement with alanine markedly decreases the EAAT1‐mediated current. These observations suggest that SGK1 exerts its effect not only by phosphorylation of Nedd4‐2 but also by phosphorylation of EAAT1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251949 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15586017 |
The serum and glucocorticoid inducible kinase 1 (SGK1) is induced in the aldosterone sensitive distal nephron (ASDN) where it may stimulate Na reabsorption, partly by inhibiting ubiquitin ligase Nedd4-2-mediated retrieval of epithelial Na+ channel ENaC from the luminal membrane. |
|
| Publications: |
2 |
Organism: |
In Vitro, Homo Sapiens |
| + |
SGK1 | up-regulates activity
phosphorylation
|
SLC1A3 |
0.425 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263075 |
Thr482 |
LDRLRTTtNVLGDSL |
in vitro |
|
| pmid |
sentence |
| 12911626 |
Site‐directed mutagenesis of the SGK1 phosphorylation sites in the Nedd4‐2 protein (S382A,S468ANedd4‐2) and in the EAAT1 protein (T482AEAAT1, T482DEAAT1) significantly blunts the effect of S422DSGK1. Introduction of a negative charge at the SGK phosphorylation site in the EAAT1 protein leads to a strong stimulation of the carrier, whereas replacement with alanine markedly decreases the EAAT1‐mediated current. These observations suggest that SGK1 exerts its effect not only by phosphorylation of Nedd4‐2 but also by phosphorylation of EAAT1. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SGK1 | down-regulates
binding
|
GLI1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251672 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25790864 |
SGK1 is known to inhibit another intrinsic pathway, the Hedgehog pathway, through downregulation of SMO and the GLI transcription factor family |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGK1 | down-regulates
binding
|
SMO |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251673 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25790864 |
SGK1 is known to inhibit another intrinsic pathway, the Hedgehog pathway, through downregulation of SMO and the GLI transcription factor family |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YAP1 | up-regulates quantity by expression 
transcriptional regulation
|
SGK1 |
0.285 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276585 |
|
|
|
|
| pmid |
sentence |
| 35216681 |
Importantly, YAP-dependent regulation of serum- and glucocorticoid-regulated kinase 1 (SGK1) is required to activate mTORC1/SREBP and stimulate de novo lipogenesis. |
|
| Publications: |
1 |
| + |
NR3C1 | up-regulates quantity
transcriptional regulation
|
SGK1 |
0.474 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255926 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 15793248 |
We show here that dexamethasone upregulates transcription and expression of the serum- and glucocorticoid-inducible kinase 1 (SGK1) in insulin-secreting cells, an effect reversed by mifepristone (RU486), an antagonist of the nuclear glucocorticoid receptor. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
MECP2 | down-regulates quantity by repression
transcriptional regulation
|
SGK1 |
0.297 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264543 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 16002417 |
These results are compatible with the hypothesis that MeCP2 associates with the Sgk and Fkbp5 promoters and has a repressive effect that is over-ridden by elevated glucocorticoids in response to stress. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
SGK1
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