| + |
AKT3 | down-regulates 
phosphorylation
|
BAD |
0.517 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81118 |
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-81122 |
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 |
| + |
AKT3 | up-regulates 
phosphorylation
|
CREB1 |
0.472 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-62257 |
Ser119 |
EILSRRPsYRKILND |
Homo sapiens |
|
| pmid |
sentence |
| 9829964 |
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 |
| + |
AKT3 | down-regulates
phosphorylation
|
CASP9 |
0.494 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-61565 |
Ser196 |
KLRRRFSsLHFMVEV |
Homo sapiens |
|
| pmid |
sentence |
| 9812896 |
Akt phosphorylated recombinant casp9 in vitro on serine-196 and inhibited its protease activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT3 | down-regulates
phosphorylation
|
FOXO3 |
0.697 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183644 |
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183648 |
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183652 |
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 |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
AKT3 | down-regulates quantity by destabilization
phosphorylation
|
FOXO |
0.697 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252874 |
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-252875 |
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-252876 |
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 |
| + |
AKT3 | down-regulates
phosphorylation
|
FOXO |
0.697 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252877 |
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252878 |
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252879 |
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 |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
AKT3 | down-regulates quantity by destabilization
phosphorylation
|
FOXO3 |
0.697 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249643 |
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-249644 |
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-249642 |
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 |
| + |
AKT3 | up-regulates activity
phosphorylation
|
BMI1 |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249583 |
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 |
| + |
AKT3 | down-regulates
phosphorylation
|
BRAF |
0.295 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78693 |
Ser364 |
FGQRDRSsSAPNVHI |
Homo sapiens |
|
| pmid |
sentence |
| 10869359 |
We show that phosphorylation of b-raf by akt occurs at multiple residues within its aminoterminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78697 |
Ser428 |
GPQRERKsSSSSEDR |
Homo sapiens |
|
| pmid |
sentence |
| 10869359 |
We show that phosphorylation of b-raf by akt occurs at multiple residues within its aminoterminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AKT3 | up-regulates
phosphorylation
|
AGO2 |
0.44 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201918 |
Ser387 |
SKLMRSAsFNTDPYV |
Homo sapiens |
|
| pmid |
sentence |
| 23603119 |
Phosphorylation of argonaute 2 at serine-387 facilitates its localization to processing bodies. , akt3-mediated phosphorylation of ago2 is a molecular switch between target mrna cleavage and translational repression activities of ago2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178416 |
Ser387 |
SKLMRSAsFNTDPYV |
Homo sapiens |
|
| pmid |
sentence |
| 18476811 |
Phosphorylation of argonaute 2 at serine-387 facilitates its localization to processing bodies, akt3-mediated phosphorylation of ago2 is a molecular switch between target mrna cleavage and translational repression activities of ago2 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PHLPP2 | down-regulates activity
dephosphorylation
|
AKT3 |
0.673 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-237439 |
Ser472 |
RPHFPQFsYSASGRE |
Homo sapiens |
|
| pmid |
sentence |
| 17386267 |
Knockdown studies reveal that PHLPP1 specifically modulates the phosphorylation of HDM2 and GSK-3alpha through Akt2, whereas PHLPP2 specifically modulates the phosphorylation of p27 through Akt3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248731 |
Ser472 |
RPHFPQFsYSASGRE |
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: |
2 |
Organism: |
Homo Sapiens |
| + |
PHLPP1 | down-regulates activity
dephosphorylation
|
AKT3 |
0.637 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248330 |
Ser472 |
RPHFPQFsYSASGRE |
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 |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
AKT3 |
0.467 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248610 |
Ser472 |
RPHFPQFsYSASGRE |
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-248609 |
Ser474 |
HFPQFSYsASGRE |
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-248611 |
Thr305 |
TDAATMKtFCGTPEY |
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-248612 |
Thr309 |
TMKTFCGtPEYLAPE |
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. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
AKT3 |
0.523 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249153 |
Ser472 |
RPHFPQFsYSASGRE |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 12162751 |
Full activation of the PKB enzyme requires phosphorylation of a threonine in the activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248996 |
Thr305 |
TDAATMKtFCGTPEY |
Homo sapiens |
HEK-293 Cell |
| 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: |
2 |
Organism: |
Chlorocebus Aethiops, Homo Sapiens |
| + |
PPP2CA | down-regulates activity
dephosphorylation
|
AKT3 |
0.718 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248653 |
Ser472 |
RPHFPQFsYSASGRE |
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-248652 |
Ser472 |
RPHFPQFsYSASGRE |
Mus musculus |
|
| 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-248651 |
Thr305 |
TDAATMKtFCGTPEY |
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-248654 |
Thr305 |
TDAATMKtFCGTPEY |
Mus musculus |
|
| 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 |
| + |
ACP1 | down-regulates activity
dephosphorylation
|
AKT3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248457 |
Ser472 |
RPHFPQFsYSASGRE |
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 |
| + |
AKT3 | up-regulates activity
phosphorylation
|
NOS3 |
0.459 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251626 |
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 |
| + |
AKT3 | up-regulates activity
phosphorylation
|
TBX3 |
0.368 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-223534 |
Ser719 |
AEKEAATsELQSIQR |
Homo sapiens |
|
| pmid |
sentence |
| 25595898 |
We have identified TBX3 as a key substrate of AKT3 in melanomagenesis. we have identified the AKT3 target site at serine residue 720 in the TBX3 protein and show that this site is phosphorylated in vivo. the phosphorylation at S720 promotes TBX3 protein stability, nuclear localization, transcriptional repression of E-cadherin, and its role in cell migration and invasion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT3 | up-regulates activity
phosphorylation
|
IWS1 |
0.397 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273496 |
Ser720 |
PQRRRMNsTGGQTPR |
Homo sapiens |
NCI-H522 Cell |
| pmid |
sentence |
| 24462114 |
The data presented in this report confirmed the differential phosphorylation of IWS1 at Ser720/Thr721 by Akt3 and Akt1 and showed that its phosphorylation at this site is required for the recruitment of SetD2 to the Spt6-IWS1-Aly/REF complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273495 |
Thr721 |
QRRRMNStGGQTPRR |
Homo sapiens |
NCI-H522 Cell |
| pmid |
sentence |
| 24462114 |
The data presented in this report confirmed the differential phosphorylation of IWS1 at Ser720/Thr721 by Akt3 and Akt1 and showed that its phosphorylation at this site is required for the recruitment of SetD2 to the Spt6-IWS1-Aly/REF complex. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AKT3 | down-regulates
phosphorylation
|
HSPB1 |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186780 |
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 |
| + |
AKT3 | down-regulates activity
phosphorylation
|
GSK3B |
0.717 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245424 |
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 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT3 | down-regulates activity
phosphorylation
|
ADAR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276191 |
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 |
| + |
AKT3 | down-regulates
phosphorylation
|
STK3 |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164306 |
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 |
| + |
AKT3 | up-regulates
phosphorylation
|
CHUK |
0.383 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187062 |
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 |
| + |
AKT3 | up-regulates quantity by stabilization
phosphorylation
|
POU5F1 |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242107 |
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 |
| + |
PDPK1 | up-regulates
phosphorylation
|
AKT3 |
0.629 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-55937 |
Thr305 |
TDAATMKtFCGTPEY |
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) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle, Myotube |
| + |
AKT3 | down-regulates
phosphorylation
|
STK4 |
0.265 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201129 |
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 |
| + |
AKT3 | down-regulates activity
phosphorylation
|
ADARB1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276195 |
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 |
| + |
FHIT | down-regulates 
|
AKT3 |
0.253 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143706 |
|
|
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 |
| + |
MTCP1 | up-regulates
binding
|
AKT3 |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81677 |
|
|
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 |
| + |
TCL1A | up-regulates
binding
|
AKT3 |
0.48 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81434 |
|
|
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 |
| + |
MK-2206 | down-regulates
chemical inhibition
|
AKT3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176049 |
|
|
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 |
| + |
GFs | up-regulates activity 
|
AKT3 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245408 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23300340 |
Akt normally resides in the cytosol under serum-starved conditions, but translocates to the plasma membrane where it is subsequently phosphorylated and activated in response to growth factor treatment. Phosphorylation of Akt at Thr308 by phosphoinositide-dependent kinase-1 (PDK1) and at Ser473 by mammalian target of rapamycin (mTOR) complex 2 (mTORC2) is required for full Akt activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT3 | up-regulates
phosphorylation
|
IKK-complex |
0.391 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217466 |
|
|
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 |
| + |
PIP3 | up-regulates
chemical activation
|
AKT3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-175250 |
|
|
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 |
| + |
FAM107A | up-regulates
binding
|
AKT3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81800 |
|
|
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 |
| + |
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
|
AKT3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262012 |
|
|
|
|
| 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. |
|
| Publications: |
1 |
| + |
GSK690693 | down-regulates
chemical inhibition
|
AKT3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-193006 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT3 | down-regulates
phosphorylation
|
STK3/4 |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269941 |
|
|
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
AKT3
- 
- 