| + |
AKT2 | up-regulates quantity by stabilization 
phosphorylation
|
PKP1 |
0.27 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273486 |
Ser118 |
EPDNRRFsSYSQMEN |
in vitro |
|
| pmid |
sentence |
| 23444369 |
Akt2 phosphorylates PKP1 in vitro. Phosphorylated PKP1 is more resistant to degradation. PKP1 phosphorylation sites identified by peptide microarray analyses and mass spectrometry. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273492 |
Ser174 |
LRKGTLGsKGQKTTQ |
in vitro |
|
| pmid |
sentence |
| 23444369 |
Akt2 phosphorylates PKP1 in vitro. Phosphorylated PKP1 is more resistant to degradation. PKP1 phosphorylation sites identified by peptide microarray analyses and mass spectrometry. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273494 |
Ser185 |
KTTQNRYsFYSTCSG |
in vitro |
|
| pmid |
sentence |
| 23444369 |
Akt2 phosphorylates PKP1 in vitro. Phosphorylated PKP1 is more resistant to degradation. PKP1 phosphorylation sites identified by peptide microarray analyses and mass spectrometry. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273490 |
Ser188 |
QNRYSFYsTCSGQKA |
in vitro |
|
| pmid |
sentence |
| 23444369 |
Akt2 phosphorylates PKP1 in vitro. Phosphorylated PKP1 is more resistant to degradation. PKP1 phosphorylation sites identified by peptide microarray analyses and mass spectrometry. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273487 |
Ser191 |
YSFYSTCsGQKAIKK |
in vitro |
|
| pmid |
sentence |
| 23444369 |
Akt2 phosphorylates PKP1 in vitro. Phosphorylated PKP1 is more resistant to degradation. PKP1 phosphorylation sites identified by peptide microarray analyses and mass spectrometry. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273491 |
Thr166 |
LYCDPRGtLRKGTLG |
in vitro |
|
| pmid |
sentence |
| 23444369 |
Akt2 phosphorylates PKP1 in vitro. Phosphorylated PKP1 is more resistant to degradation. PKP1 phosphorylation sites identified by peptide microarray analyses and mass spectrometry. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273488 |
Thr171 |
RGTLRKGtLGSKGQK |
in vitro |
|
| pmid |
sentence |
| 23444369 |
Akt2 phosphorylates PKP1 in vitro. Phosphorylated PKP1 is more resistant to degradation. PKP1 phosphorylation sites identified by peptide microarray analyses and mass spectrometry. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273489 |
Thr179 |
LGSKGQKtTQNRYSF |
in vitro |
|
| pmid |
sentence |
| 23444369 |
Akt2 phosphorylates PKP1 in vitro. Phosphorylated PKP1 is more resistant to degradation. PKP1 phosphorylation sites identified by peptide microarray analyses and mass spectrometry. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273485 |
Thr180 |
GSKGQKTtQNRYSFY |
in vitro |
|
| pmid |
sentence |
| 23444369 |
Akt2 phosphorylates PKP1 in vitro. Phosphorylated PKP1 is more resistant to degradation. PKP1 phosphorylation sites identified by peptide microarray analyses and mass spectrometry. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273493 |
Thr189 |
NRYSFYStCSGQKAI |
in vitro |
|
| pmid |
sentence |
| 23444369 |
Akt2 phosphorylates PKP1 in vitro. Phosphorylated PKP1 is more resistant to degradation. PKP1 phosphorylation sites identified by peptide microarray analyses and mass spectrometry. |
|
| Publications: |
10 |
Organism: |
In Vitro |
| + |
AKT2 | down-regulates 
phosphorylation
|
BAD |
0.505 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81110 |
Ser118 |
GRELRRMsDEFVDSF |
Homo sapiens |
|
| pmid |
sentence |
| 10949026 |
Ser-136 is the major phosphoacceptor site for akt;akt can weakly phosphorilate ser-155. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81114 |
Ser99 |
PFRGRSRsAPPNLWA |
Homo sapiens |
|
| pmid |
sentence |
| 10949026 |
Ser-136 is the major phosphoacceptor site for akt;akt can weakly phosphorilate ser-155. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AKT2 | up-regulates
phosphorylation
|
CREB1 |
0.493 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-62253 |
Ser119 |
EILSRRPsYRKILND |
Homo sapiens |
|
| pmid |
sentence |
| 9829964 |
Creb is a nuclear target for activation via the growth factor-dependent ser/thr kinase akt/pkb. When overexpressed in serum-stimulated cells, akt/pkb potently induced ser-133 phosphorylation of creb and promoted recruitment of cbp. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | up-regulates quantity by stabilization
phosphorylation
|
YBX2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277869 |
Ser137 |
NPRKFLRsVGDGETV |
Mus musculus |
Brown Adipocyte |
| pmid |
sentence |
| 37860762 |
In this context, YBX2 is a dual substrate for both AMPK and Akt2. The phosphorylation at Thr115 by AMPK or at Ser137 by Akt2 facilitates YBX2 accumulation in brown adipocytes by decreasing ubiquitination-mediated degradation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
AKT2 | up-regulates quantity by stabilization
phosphorylation
|
ATP7A |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272269 |
Ser1424 |
SYELPARsQIGQKSP |
Mus musculus |
|
| pmid |
sentence |
| 29301787 |
Akt2 (Protein Kinase B Beta) Stabilizes ATP7A, a Copper Transporter for Extracellular Superoxide Dismutase, in Vascular Smooth Muscle: Novel Mechanism to Limit Endothelial Dysfunction in Type 2 Diabetes Mellitus|Immunoprecipitation, in vitro kinase assay, and mass spectrometry analysis reveal that insulin stimulates Akt2 binding to ATP7A to induce phosphorylation at Ser1424/1463/1466 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272268 |
Ser1463 |
IVNYSRAsINSLLSD |
Mus musculus |
|
| pmid |
sentence |
| 29301787 |
Akt2 (Protein Kinase B Beta) Stabilizes ATP7A, a Copper Transporter for Extracellular Superoxide Dismutase, in Vascular Smooth Muscle: Novel Mechanism to Limit Endothelial Dysfunction in Type 2 Diabetes Mellitus|Immunoprecipitation, in vitro kinase assay, and mass spectrometry analysis reveal that insulin stimulates Akt2 binding to ATP7A to induce phosphorylation at Ser1424/1463/1466 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272270 |
Ser1466 |
YSRASINsLLSDKRS |
Mus musculus |
|
| pmid |
sentence |
| 29301787 |
Akt2 (Protein Kinase B Beta) Stabilizes ATP7A, a Copper Transporter for Extracellular Superoxide Dismutase, in Vascular Smooth Muscle: Novel Mechanism to Limit Endothelial Dysfunction in Type 2 Diabetes Mellitus|Immunoprecipitation, in vitro kinase assay, and mass spectrometry analysis reveal that insulin stimulates Akt2 binding to ATP7A to induce phosphorylation at Ser1424/1463/1466 |
|
| Publications: |
3 |
Organism: |
Mus Musculus |
| + |
AKT2 | up-regulates quantity by stabilization
phosphorylation
|
MDM2 |
0.541 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109732 |
Ser166 |
SSRRRAIsETEENSD |
Homo sapiens |
|
| pmid |
sentence |
| 11504915 |
Mitogen-induced activation of phosphatidylinositol 3-kinase (pi3-kinase) and its downstream target, the akt/pkb serine-threonine kinase, results in phosphorylation of mdm2 on serine 166 and serine 186. Phosphorylation on these sites is necessary for translocation of mdm2 from the cytoplasm into the nucleus.. Both akt expression and serum treatment induced phosphorylation of mdm2 at ser186. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | up-regulates activity
phosphorylation
|
ESR1 |
0.523 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251490 |
Ser167 |
GGRERLAsTNDKGSM |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 11139588 |
AKT activate ERalpha in the absence of estrogen. The consensus AKT phosphorylation site Ser-167 of ERalpha is required for phosphorylation and activation by AKT. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
AKT2 | up-regulates
phosphorylation
|
EP300 |
0.332 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148987 |
Ser1834 |
MLRRRMAsMQRTGVV |
Homo sapiens |
|
| pmid |
sentence |
| 16926151 |
We find that suberoylanilide hydroxamic acid stimulates akt activity, which is required to phosphorylate p300 at ser(1834). Akt-mediated phosphorylation of p300 dramatically increases its acetyltransferase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-158627 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17964260 |
Akt1 and 2 promote the association of myod with p300 and pcaf acetyltransferases, via direct phosphorylation of p300. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
AKT2 | up-regulates activity
phosphorylation
|
MDM2 |
0.541 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109736 |
Ser186 |
RQRKRHKsDSISLSF |
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 11504915 |
Mitogen-induced activation of phosphatidylinositol 3-kinase (pi3-kinase) and its downstream target, the akt/pkb serine-threonine kinase, results in phosphorylation of mdm2 on serine 166 and serine 186. Phosphorylation on these sites is necessary for translocation of mdm2 from the cytoplasm into the nucleus.. Both akt expression and serum treatment induced phosphorylation of mdm2 at ser186. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates
phosphorylation
|
KHSRP |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151220 |
Ser193 |
GLPERSVsLTGAPES |
Rattus norvegicus |
|
| pmid |
sentence |
| 17177604 |
AKT phosphorylates the mRNA decay-promoting factor KSRP at a unique serine residue, induces its association with the multifunctional protein 14-3-3, and prevents KSRP interaction with the exoribonucleolytic complex exosome. This impairs KSRPs ability to promote rapid mRNA decay. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| Pathways: | P38 Signaling and Myogenesis |
| + |
AKT2 | down-regulates
phosphorylation
|
CASP9 |
0.508 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-61561 |
Ser196 |
KLRRRFSsLHFMVEV |
Homo sapiens |
|
| pmid |
sentence |
| 9812896 |
Akt phosphorylated recombinant casp9 in vitro on serine-196 and inhibited its protease activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123243 |
Ser196 |
KLRRRFSsLHFMVEV |
Homo sapiens |
|
| pmid |
sentence |
| 15004527 |
Akt phosphorylated recombinant casp9 in vitro on serine-196 and inhibited its protease activity |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates
phosphorylation
|
HTRA2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153327 |
Ser212 |
RVRVRLLsGDTYEAV |
Homo sapiens |
|
| pmid |
sentence |
| 17311912 |
Akt attenuation of the serine protease activity of htra2/omi through phosphorylation of serine 212 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates quantity by destabilization
phosphorylation
|
FOXO |
0.756 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252863 |
Ser253 |
APRRRAVsMDNSNKY |
|
|
| pmid |
sentence |
| 19951971 |
AKT phosphorylates FOXO3a at three conserved sites (Thr32, Ser253 and Ser315), therefore creating binding sites for the 14-3-3 chaperone proteins and leading to the active export of FOXO3a to the cytoplasm where it is targeted for proteasomal degradation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252864 |
Ser315 |
DFRSRTNsNASTVSG |
|
|
| pmid |
sentence |
| 19951971 |
AKT phosphorylates FOXO3a at three conserved sites (Thr32, Ser253 and Ser315), therefore creating binding sites for the 14-3-3 chaperone proteins and leading to the active export of FOXO3a to the cytoplasm where it is targeted for proteasomal degradation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252865 |
Thr32 |
QSRPRSCtWPLQRPE |
|
|
| pmid |
sentence |
| 19951971 |
AKT phosphorylates FOXO3a at three conserved sites (Thr32, Ser253 and Ser315), therefore creating binding sites for the 14-3-3 chaperone proteins and leading to the active export of FOXO3a to the cytoplasm where it is targeted for proteasomal degradation. |
|
| Publications: |
3 |
| + |
AKT2 | down-regulates quantity by destabilization
phosphorylation
|
FOXO3 |
0.741 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249640 |
Ser253 |
APRRRAVsMDNSNKY |
|
|
| pmid |
sentence |
| 19951971 |
AKT phosphorylates FOXO3a at three conserved sites (Thr32, Ser253 and Ser315), therefore creating binding sites for the 14-3-3 chaperone proteins and leading to the active export of FOXO3a to the cytoplasm where it is targeted for proteasomal degradation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249641 |
Ser315 |
DFRSRTNsNASTVSG |
|
|
| pmid |
sentence |
| 19951971 |
AKT phosphorylates FOXO3a at three conserved sites (Thr32, Ser253 and Ser315), therefore creating binding sites for the 14-3-3 chaperone proteins and leading to the active export of FOXO3a to the cytoplasm where it is targeted for proteasomal degradation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249639 |
Thr32 |
QSRPRSCtWPLQRPE |
|
|
| pmid |
sentence |
| 19951971 |
AKT phosphorylates FOXO3a at three conserved sites (Thr32, Ser253 and Ser315), therefore creating binding sites for the 14-3-3 chaperone proteins and leading to the active export of FOXO3a to the cytoplasm where it is targeted for proteasomal degradation. |
|
| Publications: |
3 |
| + |
AKT2 | down-regulates activity
phosphorylation
|
FOXO |
0.756 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252867 |
Ser253 |
APRRRAVsMDNSNKY |
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
Akt-dependent phosphorylation of foxo3a (thr32, ser253, and ser315 for human foxo3) enhances foxo3a/14-3-3 Interaction and promotes foxo3a nuclear export to the cytoplasm, resulting in the repression of foxo3a transcriptional function akt phosphorylates members of the foxo factors (forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localisation. In particular, akt phosphorylates foxo1 on thr24, ser256 and ser319. Foxo 3alfa and foxo4 are phosphorylated on equivalent sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252871 |
Ser256 |
SPRRRAAsMDNNSKF |
Homo sapiens |
|
| pmid |
sentence |
| 10377430 |
Our results demonstrate that pkb/akt directly phosphorylates fkhr1, a member of the closely related fkhr subclass of the forkhead family of transcription factors, on at least two residues (threonine-24 and serine-253). These results indicate that phosphorylation by pkbyakt negatively regulates fkhr1 by promoting export from the nucleus. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252868 |
Ser315 |
DFRSRTNsNASTVSG |
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
Akt-dependent phosphorylation of foxo3a (thr32, ser253, and ser315 for human foxo3) enhances foxo3a/14-3-3 Interaction and promotes foxo3a nuclear export to the cytoplasm, resulting in the repression of foxo3a transcriptional function akt phosphorylates members of the foxo factors (forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localisation. In particular, akt phosphorylates foxo1 on thr24, ser256 and ser319. Foxo 3alfa and foxo4 are phosphorylated on equivalent sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252872 |
Thr24 |
LPRPRSCtWPLPRPE |
Homo sapiens |
|
| pmid |
sentence |
| 10377430 |
Our results demonstrate that pkb/akt directly phosphorylates fkhr1, a member of the closely related fkhr subclass of the forkhead family of transcription factors, on at least two residues (threonine-24 and serine-253). These results indicate that phosphorylation by pkbyakt negatively regulates fkhr1 by promoting export from the nucleus. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252869 |
Thr32 |
QSRPRSCtWPLQRPE |
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
Akt-dependent phosphorylation of foxo3a (thr32, ser253, and ser315 for human foxo3) enhances foxo3a/14-3-3 Interaction and promotes foxo3a nuclear export to the cytoplasm, resulting in the repression of foxo3a transcriptional function akt phosphorylates members of the foxo factors (forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localisation. In particular, akt phosphorylates foxo1 on thr24, ser256 and ser319. Foxo 3alfa and foxo4 are phosphorylated on equivalent sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252870 |
Thr32 |
QSRPRSCtWPLPRPE |
Homo sapiens |
|
| pmid |
sentence |
| 16272144 |
FOXO4 transcription factor, also referred to AFX, contains three putative phosphorylation motif sites for protein kinase B (PKB), Thr32, Ser197, and Ser262, and it is proposed that phosphorylated FOXO4 stays in the cytosol and is imported to the nucleus through dephosphorylation to induce target gene expression.[...]These results indicate that phosphorylation at Thr32 and Ser197 is indispensable, whereas that at Ser262 is not critical, for regulation of the nuclear localization and transcriptional activity of FOXO4 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252873 |
Thr32 |
QSRPRSCtWPLPRPE |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 11313479 |
Phosphorylation of AFX by PKB occurs in the nucleus. Phosphorylation of S193 reduces the rate of nuclear import. PKB-mediated phosphorylation of AFX, therefore, attenuates the import of the transcription factor, which shifts the localization of the protein from the nucleus to the cytoplasm and results in the inhibition of AFX transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252866 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21620960 |
Akt phosphorylates members of the foxo factors (forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localisation. In particular, akt phosphorylates foxo1 on thr24, ser256 and ser319. Foxo 3alfa and foxo4 are phosphorylated on equivalent sites. In addition, phosphorylation of afx by protein kinase b inhibits its transcriptional activity. |
|
| Publications: |
8 |
Organism: |
Homo Sapiens, Mus Musculus |
| + |
AKT2 | down-regulates activity
phosphorylation
|
FOXO3 |
0.741 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236671 |
Ser253 |
APRRRAVsMDNSNKY |
Homo sapiens |
|
| pmid |
sentence |
| 19188143 |
Akt-dependent phosphorylation of foxo3a (thr32, ser253, and ser315 for human foxo3) enhances foxo3a/14-3-3 Interaction and promotes foxo3a nuclear export to the cytoplasm, resulting in the repression of foxo3a transcriptional function akt phosphorylates members of the foxo factors (forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localisation. In particular, akt phosphorylates foxo1 on thr24, ser256 and ser319. Foxo 3alfa and foxo4 are phosphorylated on equivalent sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235960 |
Ser315 |
DFRSRTNsNASTVSG |
Homo sapiens |
|
| pmid |
sentence |
| 19188143 |
Akt-dependent phosphorylation of foxo3a (thr32, ser253, and ser315 for human foxo3) enhances foxo3a/14-3-3 Interaction and promotes foxo3a nuclear export to the cytoplasm, resulting in the repression of foxo3a transcriptional function akt phosphorylates members of the foxo factors (forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localisation. In particular, akt phosphorylates foxo1 on thr24, ser256 and ser319. Foxo 3alfa and foxo4 are phosphorylated on equivalent sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236675 |
Thr32 |
QSRPRSCtWPLQRPE |
Homo sapiens |
|
| pmid |
sentence |
| 19188143 |
Akt-dependent phosphorylation of foxo3a (thr32, ser253, and ser315 for human foxo3) enhances foxo3a/14-3-3 Interaction and promotes foxo3a nuclear export to the cytoplasm, resulting in the repression of foxo3a transcriptional function akt phosphorylates members of the foxo factors (forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localisation. In particular, akt phosphorylates foxo1 on thr24, ser256 and ser319. Foxo 3alfa and foxo4 are phosphorylated on equivalent sites. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates activity
phosphorylation
|
FOXO1 |
0.643 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-68652 |
Ser256 |
SPRRRAAsMDNNSKF |
Homo sapiens |
|
| pmid |
sentence |
| 10377430 |
Our results demonstrate that pkb/akt directly phosphorylates fkhr1, a member of the closely related fkhr subclass of the forkhead family of transcription factors, on at least two residues (threonine-24 and serine-253). These results indicate that phosphorylation by pkbyakt negatively regulates fkhr1 by promoting export from the nucleus. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-68656 |
Thr24 |
LPRPRSCtWPLPRPE |
Homo sapiens |
|
| pmid |
sentence |
| 10377430 |
Our results demonstrate that pkb/akt directly phosphorylates fkhr1, a member of the closely related fkhr subclass of the forkhead family of transcription factors, on at least two residues (threonine-24 and serine-253). These results indicate that phosphorylation by pkbyakt negatively regulates fkhr1 by promoting export from the nucleus. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates
phosphorylation
|
SH3RF1 |
0.397 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-155233 |
Ser304 |
KNTKKRHsFTSLTMA |
Homo sapiens |
|
| pmid |
sentence |
| 17535800 |
Overexpression of posh induces apoptosis in a variety of cell types, but apoptosis can be prevented by co-expressing the pro-survival protein kinase akt. We report here that posh is a direct substrate for phosphorylation by akt in vivo and in vitro, and we identify a major site of akt phosphorylation as serine 304 of posh, which lies within the rac-binding domain. We further show that phosphorylation of posh results in a decreased ability to bind activated rac |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | up-regulates activity
phosphorylation
|
PPIF |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276875 |
Ser31 |
LPAARACsKGSGDPS |
Homo sapiens |
LN-229 Cell |
| pmid |
sentence |
| 25650317 |
In turn, mitochondrial Akt2 phosphorylates Ser31 in cyclophilin D (CypD), a regulator of organelle functions. Akt2-phosphorylated CypD supports mitochondrial bioenergetics and opposes tumor cell death, conferring resistance to PI3K therapy. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | up-regulates activity
phosphorylation
|
BMI1 |
0.296 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249582 |
Ser316 |
ANRPRKSsVNGSSAT |
|
|
| pmid |
sentence |
| 22505453 |
the polycomb group silencing protein Bmi1 can be phosphorylated by AKT, which enhances its oncogenic potential in PCa. Overexpression of Bmi1 can act in combination with PTEN haploinsufficiency to induce invasive carcinogenic formation in the prostate |
|
| Publications: |
1 |
| + |
AKT2 | down-regulates
phosphorylation
|
BRAF |
0.275 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78681 |
Ser364 |
FGQRDRSsSAPNVHI |
Homo sapiens |
|
| pmid |
sentence |
| 10869359 |
We show that phosphorylation of b-raf by akt occurs at multiple residues within its amino terminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity b-raf contains three akt consensus sites, table i. One site, ser364 is conserved with c-raf;however, two sites, ser428 and thr439, are unique to b-raf |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78685 |
Ser428 |
GPQRERKsSSSSEDR |
Homo sapiens |
|
| pmid |
sentence |
| 10869359 |
We show that phosphorylation of b-raf by akt occurs at multiple residues within its amino terminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity b-raf contains three akt consensus sites, table i. One site, ser364 is conserved with c-raf;however, two sites, ser428 and thr439, are unique to b-raf |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78689 |
Thr440 |
EDRNRMKtLGRRDSS |
Homo sapiens |
|
| pmid |
sentence |
| 10869359 |
We show that phosphorylation of b-raf by akt occurs at multiple residues within its amino terminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity b-raf contains three akt consensus sites, table i. One site, ser364 is conserved with c-raf;however, two sites, ser428 and thr439, are unique to b-raf |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
AKT2 | up-regulates quantity by stabilization
phosphorylation
|
BCL3 |
0.273 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277359 |
Ser41 |
KRPLRAPsPEPAAPR |
in vitro |
|
| pmid |
sentence |
| 28689659 |
Here we show that Akt, Erk2, and IKK1/2 phosphorylate Bcl3. Phosphorylation of Ser33 by Akt induces switching of K48 ubiquitination to K63 ubiquitination and thus promotes nuclear localization and stabilization of Bcl3. Phosphorylation by Erk2 and IKK1/2 of Ser114 and Ser446 converts Bcl3 into a transcriptional coregulator by facilitating its recruitment to DNA. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AKT2 | down-regulates activity
phosphorylation
|
PCBP1 |
0.439 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262625 |
Ser43 |
VKRIREEsGARINIS |
Mus musculus |
NMuMg Cell |
| pmid |
sentence |
| 20154680 |
We show that heterogeneous nuclear ribonucleoprotein E1 (hnRNP E1) binds a structural, 33-nucleotide TGF-beta-activated translation (BAT) element in the 3' untranslated region of disabled-2 (Dab2) and interleukin-like EMT inducer (ILEI) transcripts, and represses their translation.TGF-beta activation leads to phosphorylation at Ser 43 of hnRNP E1 by protein kinase Bbeta/Akt2, inducing its release from the BAT element and translational activation of Dab2 and ILEI messenger RNAs. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
AKT2 |
phosphorylation
|
ACLY |
0.29 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245263 |
Ser455 |
PAPSRTAsFSESRAD |
Rattus norvegicus |
Adipocyte |
| pmid |
sentence |
| 12107176 |
Taken together, these results demonstrate that serine 454 of ATP-citrate lyase is a novel and major in vivo substrate for protein kinase B. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PDPK1 | up-regulates activity
phosphorylation
|
AKT2 |
0.722 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134481 |
Ser474 |
RTHFPQFsYSASIRE |
Homo sapiens |
|
| pmid |
sentence |
| 15743829 |
Akt1 and akt2 are phosphorylated and activated by the protein kinase pdk1 at thr-308 or thr-309, respectively, in the activation t-loop, and further activation occurs through phosphorylation at ser-473 or ser-474, respectively. Pdk1 phosphorylates akt-2 at thr 309 in the catalytic domain, leading to enzymatic activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236785 |
Thr309 |
SDGATMKtFCGTPEY |
Homo sapiens |
|
| pmid |
sentence |
| 9512493 |
The activation of pkbbeta and pkbgamma by pdk1 was accompanied by the phosphorylation of the residues equivalent to thr308 in pkbalpha, namely thr309 (pkbbeta) and thr305 (pkbgamma) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134485 |
Thr309 |
SDGATMKtFCGTPEY |
Homo sapiens |
|
| pmid |
sentence |
| 15743829 |
Akt1 and akt2 are phosphorylated and activated by the protein kinase pdk1 at thr-308 or thr-309, respectively, in the activation t-loop, and further activation occurs through phosphorylation at ser-473 or ser-474, respectively. Pdk1 phosphorylates akt-2 at thr 309 in the catalytic domain, leading to enzymatic activation. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle, Myotube |
| + |
PHLPP1 | down-regulates activity
dephosphorylation
|
AKT2 |
0.605 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248328 |
Ser474 |
RTHFPQFsYSASIRE |
Homo sapiens |
Chronic Myeloid Leukemia Cell |
| pmid |
sentence |
| 19261608 |
The Abl kinase inhibitors and depletion of Bcr-Abl induced the expression of PHLPP1 and PHLPP2, which dephosphorylated Ser-473 on Akt1, -2, and -3, resulting in inhibited proliferation of CML cells.|Thus, Bcr-Abl represses the expression of PHLPP1 and PHLPP2 and continuously activates Akt1, -2, and -3 via phosphorylation on Ser-473, resulting in the proliferation of CML cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK14 | up-regulates activity 
phosphorylation
|
AKT2 |
0.414 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91408 |
Ser474 |
RTHFPQFsYSASIRE |
Homo sapiens |
|
| pmid |
sentence |
| 12181443 |
We show [] that the kinase activity and s473 phosphorylation of akt induced by lpa and s1p requires both mitogen-activated protein (map) kinase kinase (mek) and p38 map kinase. [] among different stimuli tested, platelet-derived growth factor stimulates s473 phosphorylation of akt in a mek- and p38-dependent manner. However, epidermal growth factor, thrombin, and endothelin-1?stimulated Akt s473 phosphorylation require p38 but not mek. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | P38 Signaling and Myogenesis |
| + |
ACP1 | down-regulates activity
dephosphorylation
|
AKT2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248456 |
Ser474 |
RTHFPQFsYSASIRE |
Mus musculus |
|
| pmid |
sentence |
| 17353188 |
Reduction in the levels of both LMW-PTP isoforms in vitro and in vivo increased tyrosine phosphorylation of IR and AktSer473 and increased IRS-1- and IRS-2-associated PI3-K activities in both liver and fat.|Activated PI3-K stimulates Akt (or protein kinase B) that in turn phosphorylates and inactivates glycogen synthase kinase-3 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PHLPP2 | down-regulates activity
dephosphorylation
|
AKT2 |
0.588 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248729 |
Ser474 |
RTHFPQFsYSASIRE |
Homo sapiens |
Chronic Myeloid Leukemia Cell |
| pmid |
sentence |
| 19261608 |
The Abl kinase inhibitors and depletion of Bcr-Abl induced the expression of PHLPP1 and PHLPP2, which dephosphorylated Ser-473 on Akt1, -2, and -3, resulting in inhibited proliferation of CML cells.|Thus, Bcr-Abl represses the expression of PHLPP1 and PHLPP2 and continuously activates Akt1, -2, and -3 via phosphorylation on Ser-473, resulting in the proliferation of CML cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CA | down-regulates activity
dephosphorylation
|
AKT2 |
0.739 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248632 |
Ser474 |
RTHFPQFsYSASIRE |
Homo sapiens |
|
| pmid |
sentence |
| 18160256 |
Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248631 |
Ser474 |
RTHFPQFsYSASIRE |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 15367694 |
Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248630 |
Thr309 |
SDGATMKtFCGTPEY |
Homo sapiens |
|
| pmid |
sentence |
| 18160256 |
Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248633 |
Thr309 |
SDGATMKtFCGTPEY |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 15367694 |
Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes |
|
| Publications: |
4 |
Organism: |
Homo Sapiens, Mus Musculus |
| + |
AKT2 | down-regulates activity
phosphorylation
|
RALGAPA2 |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269797 |
Ser486 |
SSWGRTYsFTSAMSR |
Mus musculus |
|
| pmid |
sentence |
| 21148297 |
RGC2 is an endogenous substrate for Akt2 downstream of PI 3-kinase. kt2 directly phosphorylated all three sites on RGC2 (Figure 5A). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269798 |
Ser696 |
TTVGRSFsLSWRSHP |
Mus musculus |
|
| pmid |
sentence |
| 21148297 |
RGC2 is an endogenous substrate for Akt2 downstream of PI 3-kinase |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269799 |
Thr715 |
PMRFRSAtTSGAPGV |
Mus musculus |
|
| pmid |
sentence |
| 21148297 |
RGC2 is an endogenous substrate for Akt2 downstream of PI 3-kinase |
|
| Publications: |
3 |
Organism: |
Mus Musculus |
| + |
AKT2 | down-regulates activity
phosphorylation
|
PTPN1 |
0.379 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235491 |
Ser50 |
RNRYRDVsPFDHSRI |
Mus musculus |
|
| pmid |
sentence |
| 11579209 |
We conclude that ptp1b is a novel substrate for akt and that phosphorylation of ptp1b by akt at ser(50) may negatively modulate its phosphatase activity creating a positive feedback mechanism forinsulin signaling |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
AKT2 | up-regulates
phosphorylation
|
CTNNB1 |
0.552 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152958 |
Ser552 |
QDTQRRTsMGGTQQQ |
Homo sapiens |
|
| pmid |
sentence |
| 17287208 |
Phosphorylation of beta-catenin by akt promotes beta-catenin transcriptional activitywe have demonstrated that akt phosphorylates beta-catenin at ser552 in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates
phosphorylation
|
PPARGC1A |
0.355 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-155536 |
Ser571 |
RMRSRSRsFSRHRSC |
Homo sapiens |
|
| pmid |
sentence |
| 17554339 |
Here we describe a mechanism by which insulin, through the intermediary protein kinase akt2/protein kinase b (pkb)-beta, elicits the phosphorylation and inhibition of the transcriptional coactivator peroxisome proliferator-activated receptor-coactivator 1alpha (pgc-1alpha), a global regulator of hepatic metabolism during fasting / phosphorylation of pgc-1? At ser?570 Is required for akt to inhibit recruitment of pgc-1? To chromatin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates activity
phosphorylation
|
PPARGC1A |
0.355 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262626 |
Ser571 |
RMRSRSRsFSRHRSC |
Mus musculus |
|
| pmid |
sentence |
| 17554339 |
Here we describe a mechanism by which insulin, through the intermediary protein kinase Akt2/protein kinase B (PKB)-beta, elicits the phosphorylation and inhibition of the transcriptional coactivator peroxisome proliferator-activated receptor-coactivator 1alpha (PGC-1alpha), a global regulator of hepatic metabolism during fasting. Akt phosphorylates PGC-1α at Ser 570. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
AKT2 | up-regulates activity
phosphorylation
|
NOS3 |
0.483 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251624 |
Ser615 |
SYKIRFNsISCSDPL |
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates
phosphorylation
|
HSPB1 |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186776 |
Ser82 |
RALSRQLsSGVSEIR |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
First, the akt1, akt2, and akt3 isoforms can bind directly to hsp27 and can be found in a complex with p38 mapk, mk2, and hsp27 [98_100]. Second, rane and colleagues showed that akt could phosphorylate hsp27 at ser-82, but not ser-15 or ser-78, in vitro, while co-expression of an active akt mutant and hsp27 in hek cells resulted in hsp27 phosphorylation at the same residue. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates activity
phosphorylation
|
MAP3K5 |
0.636 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100588 |
Ser83 |
ATRGRGSsVGGGSRR |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 12697749 |
Akt2 interacts with and phosphorylates ask1 at ser-83 resulting in inhibition of its kinase activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | P38 Signaling and Myogenesis |
| + |
AKT2 | up-regulates activity
phosphorylation
|
SRSF5 |
0.369 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262633 |
Ser86 |
GRGRGRYsDRFSSRR |
Rattus norvegicus |
|
| pmid |
sentence |
| 15684423 |
Here we show that Akt2 kinase phosphorylated SRp40 in vivo and in vitro. Mutation of Ser86 on SRp40 blocked in vitro phosphorylation. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
AKT2 | up-regulates
phosphorylation
|
XIAP |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119492 |
Ser87 |
VGRHRKVsPNCRFIN |
Homo sapiens |
|
| pmid |
sentence |
| 14645242 |
Here, we demonstrate that akt, including akt1 and akt2, interacts with and phosphorylates x-linked inhibitor of apoptosis protein (xiap) at residue serine-87 in vitro and in vivo. Phosphorylation of xiap by akt protects xiap from ubiquitination and degradation in response to cisplatin. Moreover, autoubiquitination of xiap is also inhibited by akt. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates activity
phosphorylation
|
GSK3B |
0.608 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245420 |
Ser9 |
SGRPRTTsFAESCKP |
Homo sapiens |
|
| pmid |
sentence |
| 23552696 |
Active AKT, a common mediator of cell survival signals induced by radiation through multiple intracellular signaling pathways,11, 12 suppresses apoptosis. AKT positively regulates cyclin D1 expression through inactivation of glycogen synthase kinase 3_ (GSK3_). The AKT-mediated phosphorylation of glycogen synthase kinase 3_ on serine9 decreases its kinase activity for Thr286 of cyclin D1, which inhibits the nuclear export and the cytoplasmic proteasomal degradation of cyclin D1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235718 |
|
|
Homo sapiens |
Colonic Cancer Cell |
| pmid |
sentence |
| 16293724 |
We show that PGE2 stimulates colon cancer cell growth through its heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptor, EP2, by a signaling route that involves the activation of phosphoinositide 3-kinase and the protein kinase Akt by free G protein betagamma subunits and the direct association of the G protein alphas subunit with the regulator of G protein signaling (RGS) domain of axin. This leads to the inactivation and release of glycogen synthase kinase 3beta from its complex with axin, thereby relieving the inhibitory phosphorylation of beta-catenin and activating its signaling pathway. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates
phosphorylation
|
TSC2 |
0.718 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183636 |
Ser939 |
SFRARSTsLNERPKS |
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
We demonstrate here that tuberin is phosphorylated on s939 and t1462 in response to pi3k activation. Our results are consistent with akt being the pi3k-depen-dent tuberin kinase. The pi3k-akt-mediated phosphorylation of tuberin would inhibit the function of the tuberin-hamartin complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91388 |
Ser939 |
SFRARSTsLNERPKS |
Homo sapiens |
|
| pmid |
sentence |
| 12172553 |
We demonstrate here that tuberin is phosphorylated on s939 and t1462 in response to pi3k activation. Our results are consistent with akt being the pi3k-depen-dent tuberin kinase. The pi3k-akt-mediated phosphorylation of tuberin would inhibit the function of the tuberin-hamartin complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91041 |
Ser939 |
SFRARSTsLNERPKS |
Homo sapiens |
|
| pmid |
sentence |
| 12150915 |
We demonstrate here that tuberin is phosphorylated on s939 and t1462 in response to pi3k activation. Our results are consistent with akt being the pi3k-depen-dent tuberin kinase. The pi3k-akt-mediated phosphorylation of tuberin would inhibit the function of the tuberin-hamartin complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91045 |
Thr1462 |
GLRPRGYtISDSAPS |
Homo sapiens |
|
| pmid |
sentence |
| 12150915 |
We demonstrate here that tuberin is phosphorylated on s939 and t1462 in response to pi3k activation. Our results are consistent with akt being the pi3k-depen-dent tuberin kinase. The pi3k-akt-mediated phosphorylation of tuberin would inhibit the function of the tuberin-hamartin complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91392 |
Thr1462 |
GLRPRGYtISDSAPS |
Homo sapiens |
|
| pmid |
sentence |
| 12172553 |
We demonstrate here that tuberin is phosphorylated on s939 and t1462 in response to pi3k activation. Our results are consistent with akt being the pi3k-depen-dent tuberin kinase. The pi3k-akt-mediated phosphorylation of tuberin would inhibit the function of the tuberin-hamartin complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183640 |
Thr1462 |
GLRPRGYtISDSAPS |
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
We demonstrate here that tuberin is phosphorylated on s939 and t1462 in response to pi3k activation. Our results are consistent with akt being the pi3k-depen-dent tuberin kinase. The pi3k-akt-mediated phosphorylation of tuberin would inhibit the function of the tuberin-hamartin complex. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates activity
phosphorylation
|
STXBP4 |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262635 |
Ser99 |
GAKLRLEsAWEIAFI |
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 15753124 |
Akt2 phosphorylates Synip to regulate docking and fusion of GLUT4-containing vesicles. These data demonstrate that insulin activation of Akt2 specifically regulates the docking/fusion step of GLUT4-containing vesicles at the plasma membrane through the regulation of Synip phosphorylation and Synip-Syntaxin4 interaction.Thus, our data demonstrate that insulin-stimulated Akt2-dependent phosphorylation of Synip on serine residue 99 results in reduced binding interactions between Synip and Syntaxin4. |
|
| Publications: |
1 |
Organism: |
Cricetulus Griseus |
| + |
AKT2 | up-regulates
phosphorylation
|
ANKRD2 |
0.423 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236978 |
Ser99 |
QERVRKTsLDLRREI |
Mus musculus |
C2C12 Cell, Myoblast |
| pmid |
sentence |
| 21737686 |
In vitro and in vivo studies confirmed that akt phosphorylates ankrd2 at ser-99. moreover, the forced expression of a phosphorylation-defective mutant form of ankrd2 in c2c12 myoblasts promoted a faster differentiation program, implicating akt-dependent phosphorylation at ser-99 in the negative regulation of myogenesis in response to stress conditions. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
AKT2 | down-regulates activity
phosphorylation
|
ADAR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276192 |
Thr1033 |
RLGERLRtMSCSDKI |
in vitro |
|
| pmid |
sentence |
| 31095429 |
AKT-dependent phosphorylation of the adenosine deaminases ADAR-1 and -2 inhibits deaminase activity. Coimmunoprecipitation studies and in vitro kinase assays revealed that AKT-1, -2, and -3 interact with both ADAR1p110 and ADAR2 and phosphorylate these RNA editases. Using site-directed mutagenesis of suspected AKT phosphorylation sites, AKT was found to primarily phosphorylate ADAR1p110 and ADAR2 on T738 and T553, respectively |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AKT2 | down-regulates
phosphorylation
|
STK3 |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164302 |
Thr117 |
IIRLRNKtLIEDEIA |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 20231902 |
Akt phosphorylates mst2 at thr117 in vitro and in vivo, which leads to mst2 cleavage and kinase activity as well as nuclear translocation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | up-regulates activity
phosphorylation
|
UPF1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277595 |
Thr151 |
FCNGRGNtSGSHIVN |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 35675814 |
AKT-Mediated UPF1 Phosphorylation at T151 Promotes UPF1 Helicase Activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates
phosphorylation
|
CDKN1B |
0.51 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93122 |
Thr157 |
GIRKRPAtDDSSTQN |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 12244303 |
Akt-induced t157 phosphorylation causes retention of p27(kip1) in the cytoplasm, precluding p27(kip1)-induced g1 arrest.[__]Thus, cytoplasmic relocalization of p27(kip1), secondary to akt-mediated phosphorylation, is a novel mechanism whereby the growth inhibitory properties of p27(kip1) are functionally inactivated and the proliferation of breast cancer cells is sustained. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | up-regulates activity
phosphorylation
|
MYO5A |
0.435 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262632 |
Thr1650 |
PTGLRKRtSSIADEG |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 17515613 |
Here we identify an Akt consensus phosphorylation motif in the actin-based motor protein myosin 5a and show that insulin stimulation leads to phosphorylation of myosin 5a at serine 1650. This Akt-mediated phosphorylation event enhances the ability of myosin 5a to interact with the actin cytoskeleton.Taken together, these data indicate that myosin 5a is a newly identified direct substrate of Akt2 and, upon insulin stimulation, phosphorylated myosin 5a facilitates anterograde movement of GLUT4 vesicles along actin to the cell surface. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
AKT2 | up-regulates
phosphorylation
|
CHUK |
0.51 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187010 |
Thr23 |
EMRERLGtGGFGNVC |
Homo sapiens |
|
| pmid |
sentence |
| 19609947 |
Although there are likely to be multiple levels of crosstalk between the pi3k-akt and nf-kb pathways, one mechanism has been attributed to direct phosphorylation of the amino acid residue t23 on ikb kinase alfa (ikkalfa) by akt, thereby leading to activation of this kinase upstream of nf-kb akt mediates ikkalpha phosphorylation at threonine 23 akt transiently associates in vivo with ikk and induces ikk activation. Akt mediates ikkalfa phosphorylation at threonine 23.Akt phosphorylates ikkalpha on t23, and this phosphorylation event is a prerequisite for the phosphorylation of p65 at s534 by ikkalpha and beta |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | up-regulates quantity by stabilization
phosphorylation
|
POU5F1 |
0.257 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242097 |
Thr235 |
QARKRKRtSIENRVR |
Homo sapiens |
NCCIT Cell |
| pmid |
sentence |
| 23041284 |
Here we show that in ECCs, Akt phosphorylated the master pluripotency factor Oct4 at threonine 235, and that the levels of phosphorylated Oct4 in ECCs correlated with resistance to apoptosis and tumorigenic potential. Phosphorylation of Oct4 increased its stability and facilitated its nuclear localization and its interaction with Sox2, which promoted the transcription of the core stemness genes POU5F1 and NANOG. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates activity
phosphorylation
|
AKT1S1 |
0.66 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248046 |
Thr246 |
LPRPRLNtSDFQKLK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12524439 |
1) PRAS40 was phosphorylated in vitro by purified Akt on the same site that was phosphorylated in insulin-treated cells; 2) activation of an inducible Akt was alone sufficient to stimulate the phosphorylation of PRAS40; and 3) cells lacking Akt1 and Akt2 exhibit a diminished ability to phosphorylate this protein |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
AKT2 |
0.481 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248997 |
Thr309 |
SDGATMKtFCGTPEY |
in vitro |
|
| pmid |
sentence |
| 9512493 |
The activation of PKBbeta and PKBgamma by PDK1 was accompanied by the phosphorylation of the residues equivalent to Thr308 in PKBalpha, namely Thr309 (PKBbeta) and Thr305 (PKBgamma). PKBgamma which had been activated by PDK1 possessed a substrate specificity identical with that of PKBalpha and PKBbeta towards a range of peptides. The activation of PKBgamma and its phosphorylation at Thr305 was triggered by insulin-like growth factor-1 in 293 cells. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AKT2 | down-regulates activity
phosphorylation
|
FOXO4 |
0.593 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251491 |
Thr32 |
QSRPRSCtWPLPRPE |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 11313479 |
Phosphorylation of AFX by PKB occurs in the nucleus. Phosphorylation of S193 reduces the rate of nuclear import. PKB-mediated phosphorylation of AFX, therefore, attenuates the import of the transcription factor, which shifts the localization of the protein from the nucleus to the cytoplasm and results in the inhibition of AFX transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248055 |
Thr32 |
QSRPRSCtWPLPRPE |
Homo sapiens |
|
| pmid |
sentence |
| 16272144 |
FOXO4 transcription factor, also referred to AFX, contains three putative phosphorylation motif sites for protein kinase B (PKB), Thr32, Ser197, and Ser262, and it is proposed that phosphorylated FOXO4 stays in the cytosol and is imported to the nucleus through dephosphorylation to induce target gene expression.[...]These results indicate that phosphorylation at Thr32 and Ser197 is indispensable, whereas that at Ser262 is not critical, for regulation of the nuclear localization and transcriptional activity of FOXO4 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-233529 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21620960 |
Akt phosphorylates members of the foxo factors (forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localisation. In particular, akt phosphorylates foxo1 on thr24, ser256 and ser319. Foxo 3alfa and foxo4 are phosphorylated on equivalent sites. In addition, phosphorylation of afx by protein kinase b inhibits its transcriptional activity. |
|
| Publications: |
3 |
Organism: |
Mus Musculus, Homo Sapiens |
| + |
AKT2 | up-regulates activity
phosphorylation
|
PDK1 |
0.383 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277271 |
Thr346 |
APRPRVEtSRAVPLA |
in vitro |
|
| pmid |
sentence |
| 27505672 |
Using a phosphoproteomics screen, we now show that active Akt accumulates in the mitochondria during hypoxia and phosphorylates pyruvate dehydrogenase kinase 1 (PDK1) on Thr346 to inactivate the pyruvate dehydrogenase complex. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AKT2 | down-regulates
phosphorylation
|
STK4 |
0.264 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201125 |
Thr387 |
TMKRRDEtMQPAKPS |
Homo sapiens |
|
| pmid |
sentence |
| 23431053 |
Full activation of mst1 requires an activation cleavage that is prevented by the phosphorylation of thr-387 by akt. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates activity
phosphorylation
|
ADARB1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276196 |
Thr553 |
LQGERLLtMSCSDKI |
in vitro |
|
| pmid |
sentence |
| 31095429 |
AKT-dependent phosphorylation of the adenosine deaminases ADAR-1 and -2 inhibits deaminase activity. Coimmunoprecipitation studies and in vitro kinase assays revealed that AKT-1, -2, and -3 interact with both ADAR1p110 and ADAR2 and phosphorylate these RNA editases. Using site-directed mutagenesis of suspected AKT phosphorylation sites, AKT was found to primarily phosphorylate ADAR1p110 and ADAR2 on T738 and T553, respectively |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AKT2 | up-regulates
phosphorylation
|
EZR |
0.382 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-130260 |
Thr567 |
QGRDKYKtLRQIRQG |
Homo sapiens |
|
| pmid |
sentence |
| 15531580 |
Purified akt directly phosphorylates recombinant ezrin at threonine 567 in vitro in an atp-dependent manner. ezrin activation after initiation of na+-glucose cotransport requires akt2 expression |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates activity
phosphorylation
|
CYCS |
0.296 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277236 |
Tyr47 |
KTGQAPGySYTAANK |
in vitro |
|
| pmid |
sentence |
| 32781572 |
Finally, we propose that pro-survival kinase Akt (protein kinase B) is a likely mediator of the S47 phosphorylation of Cytc in the brain. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AKT2 | up-regulates activity
phosphorylation
|
mTORC1 |
0.568 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236705 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17386266 |
Insulin-stimulated phosphorylation of pras40 by akt/pkb suppresses its mtorc1 inhibitory activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235967 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17277771 |
Furthermore, pras40 phosphorylation by akt and association with 14-3-3, a cytosolic anchor protein, are crucial for insulin to stimulate mtor. These findings identify pras40 as an important regulator of insulin sensitivity of the akt-mtor pathway and a potential target for the treatment of cancers, insulin resistance and hamartoma syndromes. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AKT2 | up-regulates quantity by expression
transcriptional regulation
|
JAG1 |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277223 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 38402584 |
Jagged1 is upregulated by Akt upon activation by R-Ras. All three Akt isoforms influence Jagged1 expression in ECs, but Akt3 is the most prominent Akt isoform in this role, despite its low expression level compared with Akt1. Jagged1 then activates Notch to upregulate Hey1, Hes1, p21, p53, and Unc5b in adjacent cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TCL1B | up-regulates
binding
|
AKT2 |
0.546 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81716 |
|
|
Homo sapiens |
T-lymphocyte, Leukemia Cell |
| pmid |
sentence |
| 10983986 |
In vivo, tcl1 forms trimers, which associate with akt. Tcl1 facilitates the oligomerization and activation of akt. Our data show that tcl1 is a novel akt kinase coactivator, which promotes akt-induced cell survival and proliferation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TNF | up-regulates
|
AKT2 |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106596 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11287630 |
Tumor necrosis factor (tnf) inhibited insulin-promoted tyrosine phosphorylation of irs-1 and activated the akt/protein kinase b serine-threonine kinase, a downstream target for phosphatidylinositol 3-kinase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | P38 Signaling and Myogenesis |
| + |
AKT2 | up-regulates
|
GLI1 |
0.278 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157770 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17845852 |
Ras and akt signaling enhances the nuclear localization of gli1, counteracting its suppression by other modifiers that retain it in the cytoplasm, such as suppressor of fused (sufu). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates activity
phosphorylation
|
RAF1 |
0.431 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235678 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10576742 |
Akt (protein kinase b), a member of a different signaling pathway that also regulates these responses, interacted with raf and phosphorylated this protein at a highly conserved serine residue in its regulatory domain in vivo. This phosphorylation of raf by akt inhibited activation of the raf-mek-erk signaling pathway and shifted the cellular response in a human breast cancer cell line from cell cycle arrest to proliferation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GSK690693 | down-regulates
chemical inhibition
|
AKT2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-193003 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
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 |
| + |
AKT2 | up-regulates
|
MTOR |
0.623 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101324 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12782654 |
It was shown recently that akt activates mtor through direct phosphorylation of tsc2 the serine/threonine kinase akt is an upstream positive regulator of the mammalian target of rapamycin (mtor). However, the mechanism by which akt activates mtor is not fully understood. The known pathway by which akt activates mtor is via direct phosphorylation and tuberous sclerosis complex 2 (tsc2), which is a negative regulator of mtor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
AKT2 | down-regulates activity
binding
|
CDKN1A |
0.669 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149705 |
|
|
Homo sapiens |
Myoblast |
| pmid |
sentence |
| 16982699 |
Whereas akt1 phosphorylates p21, inducing its release from cdk2 and cytoplasmic localization as previously described for akt, akt2 binds p21 in the region spanning the t145 site of p21, thus competing with phosphorylation by akt1 and inducing its accumulation in the nucleus. These distinct roles of akt/pkb isoforms in modulating proliferation and p21 have important implications for the development of drugs aimed at inhibiting cancer cell proliferation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK14 | down-regulates activity 
|
AKT2 |
0.414 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166591 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20626350 |
On the other hand, p38 alfa may negatively modulate akt activity, indipendently of pi3k by regulating the interaction between caveolin 1 and pp2a through a mechanism dependent on cell attachment. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | P38 Signaling and Myogenesis |
| + |
PI3K | up-regulates
|
AKT2 |
0.63 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252716 |
|
|
Homo sapiens |
Colonic Cancer Cell |
| pmid |
sentence |
| 16293724 |
We show that pge2 stimulates colon cancer cell growth through its heterotrimeric guanine nucleotide-binding protein (g protein)coupled receptor, ep2, by a signaling route that involves the activation of phosphoinositide 3-kinase and the protein kinase akt by free g protein bg subunits and the direct association of the g protein as subunit with the regulator of g protein signaling (rgs) domain of axin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | up-regulates
|
NFKB1 |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156530 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17604717 |
Several studies have demonstrated that akt signaling can activate the nf-kb transcription factor downstream of a variety of stimuli, such as tumor necrosis factor (tnfalfa) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FHIT | down-regulates
|
AKT2 |
0.251 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143703 |
|
|
Homo sapiens |
Lung Cancer Cell |
| pmid |
sentence |
| 16407838 |
Fhit inhibited activity of akt, a key effector in the phosphatidylinositol 3-oh kinase (pi3k) pathway;loss of endogenous fhit expression caused increased akt activity in vitro and in vivo, and overexpression of constitutively active akt inhibited fhit-induced apoptosis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
3-[1-[[4-(7-phenyl-3H-imidazo[4,5-g]quinoxalin-6-yl)phenyl]methyl]-4-piperidinyl]-1H-benzimidazol-2-one | down-regulates activity
chemical inhibition
|
AKT2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262011 |
|
|
|
|
| pmid |
sentence |
| 25309440 |
Different agents were used to inhibit either the PI3K/Akt or MEK/ERK pathways. The PI3K inhibitor, LY294002, and the Akt inhibitor, Akt inhibitor VIII, were used to inhibit the PI3K/Akt pathway. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262228 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 25336630 |
stimulations were performed in the presence or absence of Akt inhibitor VIII, which selectively inhibits Akt1/Akt2 activity. |
|
| Publications: |
2 |
Organism: |
, Homo Sapiens |
| + |
AKT2 | up-regulates
phosphorylation
|
IKK-complex |
0.439 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217463 |
|
|
Homo sapiens |
Thymoma Cell |
| pmid |
sentence |
| 19609947 |
Although there are likely to be multiple levels of crosstalk between the pi3k-akt and nf-kb pathways, one mechanism has been attributed to direct phosphorylation of the amino acid residue t23 on ikb kinase alfa (ikkalfa) by akt, thereby leading to activation of this kinase upstream of nf-kb akt mediates ikkalpha phosphorylation at threonine 23 akt transiently associates in vivo with ikk and induces ikk activation. Akt mediates ikkalfa phosphorylation at threonine 23.Akt phosphorylates ikkalpha on t23, and this phosphorylation event is a prerequisite for the phosphorylation of p65 at s534 by ikkalpha and beta |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MK-2206 | down-regulates
chemical inhibition
|
AKT2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176046 |
|
|
Homo sapiens |
Skin Cancer Cell |
| pmid |
sentence |
| 21841310 |
Treatment with the pi3k inhibitor ly294002 or the akt inhibitor mk2206 diminished s473 phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
17beta-estradiol | up-regulates
|
AKT2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97798 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 12554767 |
Treatment of cells with estradiol resulted in phosphorylation of akt and a 9-fold increase in akt activity in 10 min. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates
phosphorylation
|
GSK3A |
0.539 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138179 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16023596 |
Activated pi3k/akt pathway results in inhibitory phosphorylation of gsk3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates
phosphorylation
|
AKT1S1 |
0.66 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152936 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17277771 |
Furthermore, pras40 phosphorylation by akt and association with 14-3-3, a cytosolic anchor protein, are crucial for insulin to stimulate mtor. These findings identify pras40 as an important regulator of insulin sensitivity of the akt-mtor pathway and a potential target for the treatment of cancers, insulin resistance and hamartoma syndromes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153931 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17386266 |
Insulin-stimulated phosphorylation of pras40 by akt/pkb suppresses its mtorc1 inhibitory activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
NUDT3 | up-regulates
binding
|
AKT2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81759 |
|
|
Homo sapiens |
T-lymphocyte, Leukemia Cell |
| pmid |
sentence |
| 10983986 |
Full-length tcl1 and its isoforms bind to akt / in in vitro kinase assays using gsk-3_ as a substrate, we found that the presence of any of the tcl1 family proteins (tcl1, mtcp1, or tcl1b) as gst fusion proteins significantly enhanced akt-induced gsk-3_ phosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MTCP1 | up-regulates
binding
|
AKT2 |
0.433 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81674 |
|
|
Homo sapiens |
T-lymphocyte, Leukemia Cell |
| pmid |
sentence |
| 10983986 |
Full-length tcl1 and its isoforms bind to akt / in in vitro kinase assays using gsk-3_ as a substrate, we found that the presence of any of the tcl1 family proteins (tcl1, mtcp1, or tcl1b) as gst fusion proteins significantly enhanced akt-induced gsk-3_ phosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | up-regulates activity
|
CTNNB1 |
0.552 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141655 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16293724 |
We show that pge2 stimulates colon cancer cell growth through its heterotrimeric guanine nucleotide-binding protein (g protein) coupled receptor, ep2, by a signaling route that involves the activation of phosphoinositide 3-kinase and the protein kinase akt by free g protein bg subunits and the direct association of the g protein as subunit with the regulator of g protein signaling (rgs) domain of axin. This leads to the inactivation and release of glycogen synthase kinase 3b from its complex with axin, thereby relieving the inhibitory phosphorylation of b-catenin and activating its signaling pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates activity
|
MAPK14 |
0.414 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100591 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 12697749 |
Our data indicate that akt2 inhibits cisplatin-induced jnk/p38 and bax activation through phosphorylation of ask1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | P38 Signaling and Myogenesis |
| + |
AKT2 | down-regulates activity
phosphorylation
|
TSC |
0.665 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235852 |
|
|
Mus musculus |
3T3-L1 Cell |
| pmid |
sentence |
| 19593385 |
In examining the requirements for different Akt-mediated phosphorylation sites on TSC2, we find that only TSC2 mutants lacking all five previously identified Akt sites fully block insulin-stimulated mTORC1 signaling in reconstituted Tsc2 null cells, and this mutant also inhibits adipogenesis |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
TCL1A | up-regulates
binding
|
AKT2 |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81683 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10983986 |
Full-length tcl1 and its isoforms bind to akt / in in vitro kinase assays using gsk-3_ as a substrate, we found that the presence of any of the tcl1 family proteins (tcl1, mtcp1, or tcl1b) as gst fusion proteins significantly enhanced akt-induced gsk-3_ phosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRIM13 | down-regulates quantity by destabilization
polyubiquitination
|
AKT2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271853 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21333377 |
Here, we demonstrate that overexpression of RFP2 in cells induced apoptosis through proteasomal degradation of MDM2 and AKT. We observed that RFP2 formed a complex with MDM2, a negative regulator of the p53 tumor suppressor, and AKT, a regulator of apoptosis inhibition at the cellular level. Additionally, we found that the interaction of RFP2 with MDM2 and AKT resulted in ubiquitination and proteasomal degradation of MDM2 and AKT in vivo and in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIP3 | up-regulates activity
chemical activation
|
AKT2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-175247 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21779497 |
When active, pi3k converts phosphatidylinositol (4,5)-bisphosphate (pip2) into phosphatidylinositol (3,4,5)-trisphosphate (pip3). Pip3, in turn, binds the pleckstrin homology (ph) domain of akt/pkb, stimulating its kinase activity, resulting in the phosphorylation of a host of other proteins that affect cell growth, cell cycle entry, and cell survival. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PHLPP1 | down-regulates
dephosphorylation
|
AKT2 |
0.605 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153935 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17386267 |
These data are consistent with phlpp terminating akt signaling by directly dephosphorylating and inactivating akt / phlpp1 specifically modulates the phosphorylation of hdm2 and gsk-3alpha through akt2, whereas phlpp2 specifically modulates the phosphorylation of p27 through akt3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CCT128930 | down-regulates
chemical inhibition
|
AKT2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190868 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | up-regulates
phosphorylation
|
P300/PCAF |
0.306 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217673 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17964260 |
Akt1 and 2 promote the association of myod with p300 and pcaf acetyltransferases, via direct phosphorylation of p300. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| Pathways: | P38 Signaling and Myogenesis |
| + |
PPP2CB | down-regulates
dephosphorylation
|
AKT2 |
0.459 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-42123 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8650155 |
These results confirm that the activity changes observed are achieved by a reversible phosphorylation mechanism, and also argue that pp2a may negatively regulate rac-pk activity in vivo. Dephosphorylation of the activated rac-pk in itro by pp2ac resulted in an 87% reduction of kinase activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIK3CA | up-regulates
|
AKT2 |
0.657 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141814 |
|
|
Homo sapiens |
Colonic Cancer Cell |
| pmid |
sentence |
| 16293724 |
We show that pge2 stimulates colon cancer cell growth through its heterotrimeric guanine nucleotide-binding protein (g protein)coupled receptor, ep2, by a signaling route that involves the activation of phosphoinositide 3-kinase and the protein kinase akt by free g protein bg subunits and the direct association of the g protein as subunit with the regulator of g protein signaling (rgs) domain of axin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GNG12 | up-regulates
binding
|
AKT2 |
0.388 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141792 |
|
|
Homo sapiens |
Colonic Cancer Cell |
| pmid |
sentence |
| 16293724 |
We show that pge2 stimulates colon cancer cell growth through its heterotrimeric guanine nucleotide-binding protein (g protein) coupled receptor, ep2, by a signaling route that involves the activation of phosphoinositide 3-kinase and the protein kinase akt by free g protein bg subunits and the direct association of the g protein as subunit with the regulator of g protein signaling (rgs) domain of axin. This leads to the inactivation and release of glycogen synthase kinase 3b from its complex with axin, thereby relieving the inhibitory phosphorylation of b-catenin and activating its signaling pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PHLPP1 |
dephosphorylation
|
AKT2 |
0.605 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135008 |
|
|
Homo sapiens |
Glioblastoma Cell |
| pmid |
sentence |
| 15808505 |
These data are consistent with phlpp terminating akt signaling by directly dephosphorylating and inactivating akt / phlpp1 specifically modulates the phosphorylation of hdm2 and gsk-3alpha through akt2, whereas phlpp2 specifically modulates the phosphorylation of p27 through akt3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates
phosphorylation
|
STK3/4 |
0.264 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269937 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 20231902 |
Akt phosphorylates mst2 at thr117 in vitro and in vivo, which leads to mst2 cleavage and kinase activity as well as nuclear translocation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
AKT2
- 
- 