+ |
GSK3A | down-regulates activity
phosphorylation
|
ANKRD28 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264792 |
Ser1007 |
INRYTNTsKTVSFEA |
in vitro |
|
pmid |
sentence |
17023142 |
We provide evidence for a dual kinase-mediated regulation of the PITK holoenzyme whereby PITK phosphorylation at S1017 is catalyzed by calcium/calmodulin-dependent kinase II-delta (CaMKIIdelta), promoting the subsequent phosphorylation of S1013 by glycogen synthase kinase-3 (GSK3) in vitro.|the phosphorylation of PITK at these specific residues altered PP1 binding and subsequent PITK-directed dephosphorylation of hnRNP K |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
GSK3A | down-regulates
phosphorylation
|
CAMKK2 |
0.272 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-198122 |
Ser129 |
ICPSLPYsPVSSPQS |
Homo sapiens |
|
pmid |
sentence |
22778263 |
Cdk5 and gsk3 phosphorylate ser-129, ser-133, and ser-137. Mutation of ser-129, ser-133, and ser-137 increases autonomous activity with little change in ca2 /cam-dependent activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-198126 |
Ser133 |
LPYSPVSsPQSSPRL |
Homo sapiens |
|
pmid |
sentence |
22778263 |
Cdk5 and gsk3 phosphorylate ser-129, ser-133, and ser-137. Mutation of ser-129, ser-133, and ser-137 increases autonomous activity with little change in ca2 /cam-dependent activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-198130 |
Ser137 |
PVSSPQSsPRLPRRP |
Homo sapiens |
|
pmid |
sentence |
22778263 |
Cdk5 and gsk3 phosphorylate ser-129, ser-133, and ser-137. Mutation of ser-129, ser-133, and ser-137 increases autonomous activity with little change in ca2 /cam-dependent activity. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
GSK3A | up-regulates activity
phosphorylation
|
LRP6 |
0.616 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275398 |
Ser1490 |
AILNPPPsPATERSH |
Homo sapiens |
|
pmid |
sentence |
35487243 |
Central to WNT signalosome formation is phosphorylation of LRP6 at multiple sites, with GSK3β phosphorylating LRP6 at S1490 and CK1 family members phosphorylating LRP6 at T1479 and T1493 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | down-regulates quantity by destabilization
phosphorylation
|
MCL1 |
0.469 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251217 |
Ser159 |
NNTSTDGsLPSTPPP |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
16543145 |
MCL-1 was phosphorylated by GSK-3 at a conserved GSK-3 phosphorylation site (S159). Glycogen Synthase Kinase-3 Regulates Mitochondrial Outer Membrane Permeabilization and Apoptosis by Destabilization of MCL-1. threonine 163, which represents the GSK-3 priming phosphorylation in this protein |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCG | down-regulates
phosphorylation
|
GSK3A |
0.329 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-115726 |
Ser21 |
SGRARTSsFAEPGGG |
Homo sapiens |
|
pmid |
sentence |
11884598 |
Convergence of multiple signaling cascades at glycogen synthase kinase 3: edg receptor-mediated phosphorylation and inactivation by lysophosphatidic acid through a protein kinase c-dependent intracellular pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCA | down-regulates
phosphorylation
|
GSK3A |
0.352 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-115714 |
Ser21 |
SGRARTSsFAEPGGG |
Homo sapiens |
|
pmid |
sentence |
11884598 |
Convergence of multiple signaling cascades at glycogen synthase kinase 3: edg receptor-mediated phosphorylation and inactivation by lysophosphatidic acid through a protein kinase c-dependent intracellular pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CAMK2B | down-regulates
phosphorylation
|
GSK3A |
0.295 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167962 |
Ser21 |
SGRARTSsFAEPGGG |
Homo sapiens |
Neuron |
pmid |
sentence |
20841359 |
Inhibitory phosphorylation of gsk-3 by camkii couples depolarization to neuronal survival. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SGK3 | down-regulates activity
phosphorylation
|
GSK3A |
0.361 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249165 |
Ser21 |
SGRARTSsFAEPGGG |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16543730 |
Phosphorylation of GSK3 by PKB or SGK1 inhibits GSK3 activity|estern blotting using an antibody specific for the PKB/SGK1 consensus phosphorylation site in GSK3a/beta (serine 21 and 9 respectively) revealed an increase in GSK3a/beta phosphorylation in human embryonic kidney 293 (HEK293) cells overexpressing wild type SGK1, constitutively active SGK1, but not catalytically inactive SGK1.|The effect of SGK1 was mimicked by PKB and SGK3. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCH | down-regulates
phosphorylation
|
GSK3A |
0.326 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-115730 |
Ser21 |
SGRARTSsFAEPGGG |
Homo sapiens |
|
pmid |
sentence |
11884598 |
Furthermore, several pkc isotypes phosphorylate gsk-3 in vitro and in vivo. in the presence of atp, several isoforms (?, ___, _, ?, And of pkc phosphorylated both gsk-3? At ser 21 and gsk-3_ at ser 9 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT | down-regulates
phosphorylation
|
GSK3A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-83217 |
Ser21 |
SGRARTSsFAEPGGG |
Homo sapiens |
|
pmid |
sentence |
11035810 |
In response to insulin, gsk3a inhibited by phosphorylation at ser-21 by pkb/akt1;phosphorylation at this site causes a conformational change, preventing access of substrates to the active site. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKACA | down-regulates
phosphorylation
|
GSK3A |
0.378 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-83221 |
Ser21 |
SGRARTSsFAEPGGG |
Homo sapiens |
|
pmid |
sentence |
11035810 |
Phosphorylation of ser21 and inactivation of glycogen synthase kinase 3 by protein kinase a. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | down-regulates activity
phosphorylation
|
GSK3A |
0.268 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-110827 |
Ser21 |
SGRARTSsFAEPGGG |
Homo sapiens |
Neutrophil |
pmid |
sentence |
11583116 |
P90-rsk and akt may promote rapid phosphorylation/inactivation of glycogen synthase kinase 3 in chemoattractant-stimulated neutrophils. These reactions were monitored with a phosphospecific antibody that only recognized the alpha- or beta-isoforms of GSK-3 when these proteins were phosphorylated on serine residues 21 and 9, respectively. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCB | down-regulates
phosphorylation
|
GSK3A |
0.333 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-115718 |
Ser21 |
SGRARTSsFAEPGGG |
Homo sapiens |
|
pmid |
sentence |
11884598 |
Convergence of multiple signaling cascades at glycogen synthase kinase 3: edg receptor-mediated phosphorylation and inactivation by lysophosphatidic acid through a protein kinase c-dependent intracellular pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCD | down-regulates
phosphorylation
|
GSK3A |
0.348 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-115722 |
Ser21 |
SGRARTSsFAEPGGG |
Homo sapiens |
|
pmid |
sentence |
11884598 |
Convergence of multiple signaling cascades at glycogen synthase kinase 3: edg receptor-mediated phosphorylation and inactivation by lysophosphatidic acid through a protein kinase c-dependent intracellular pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT1 | down-regulates
phosphorylation
|
GSK3A |
0.62 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252589 |
Ser21 |
SGRARTSsFAEPGGG |
Homo sapiens |
|
pmid |
sentence |
11035810 |
In response to insulin, gsk3a inhibited by phosphorylation at ser-21 by pkb/akt1;phosphorylation at this site causes a conformational change, preventing access of substrates to the active site. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | down-regulates
phosphorylation
|
JUN |
0.338 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-21776 |
Ser243 |
PGETPPLsPIDMESQ |
Homo sapiens |
|
pmid |
sentence |
1846781 |
Phosphorylation of recombinant human c-jun proteins in vitro by gsk-3 decreases their dna-binding activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-21780 |
Ser249 |
LSPIDMEsQERIKAE |
Homo sapiens |
|
pmid |
sentence |
1846781 |
Phosphorylation of recombinant human c-jun proteins in vitro by gsk-3 decreases their dna-binding activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-21784 |
Thr239 |
VPEMPGEtPPLSPID |
Homo sapiens |
|
pmid |
sentence |
1846781 |
Phosphorylation of recombinant human c-jun proteins in vitro by gsk-3 decreases their dna-binding activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-138592 |
|
|
Homo sapiens |
|
pmid |
sentence |
16023596 |
Similar to c-myc, we report here that phosphorylation of c-jun by gsk3 creates a high-affinity binding site for the e3 ligase fbw7, which targets c-jun for polyubiquitination and proteasomal degradation. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
GSK3A | down-regulates quantity by destabilization
phosphorylation
|
CD274 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277552 |
Ser279 |
CGIQDTNsKKQSDTH |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
33879767 |
We find EGFR inhibitors promote PD-L1 ubiquitination and proteasomal degradation following GSK3α-mediated phosphorylation of Ser279/Ser283. We identify ARIH1 as the E3 ubiquitin ligase responsible for targeting PD-L1 to degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | up-regulates activity
phosphorylation
|
PPARA |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277431 |
Ser280 |
FHCCQCTsVETVTEL |
Rattus norvegicus |
Cardiomyocyte Cell Line |
pmid |
sentence |
30745182 |
Fatty acids (FAs) upregulate GSK-3α, which phosphorylates PPARα at Ser280 in the ligand-binding domain (LBD). This modification ligand independently enhances transcription of a subset of PPARα targets, selectively stimulating FA uptake and storage, but not oxidation, thereby promoting lipid accumulation. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
GSK3A | down-regulates activity
phosphorylation
|
FCAR |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264856 |
Ser284 |
LTFARTPsVCK |
Mus musculus |
BA/F3 Cell |
pmid |
sentence |
30766540 |
GSK-3 is constitutively active in the absence of cytokine stimulation and can phosphorylate S263, keeping FcalphaRI in the inactive state. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
GSK3A | down-regulates quantity by destabilization
phosphorylation
|
GPSM3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264863 |
Ser35 |
STTRPWRsAPPSPPP |
Homo sapiens |
Monocyte |
pmid |
sentence |
22843681 |
Co-immunoprecipitation of endogenous GPSM3 and 14-3-3 proteins from the human monocytic cell line THP-1 suggests basal phosphorylation of GPSM3 at serine 35 as potentially mediated by GSK3alpha. The GPSM3/14-3-3 interaction is seen to stabilize GPSM3 from degradation and also support the nuclear exclusion of both proteins. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | down-regulates activity
phosphorylation
|
GRB14 |
0.267 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264871 |
Ser358 |
MHPYQGRsGCSSQSI |
in vitro |
|
pmid |
sentence |
28130417 |
Phosphorylation of clustered serine residues in the N-terminus of BPS domain negatively regulates formation of the complex between human Grb14 and insulin receptor| In vitro kinase assay using the motif-derived peptides showed that the serine residues located in N-terminal (Ser358, Ser362 and Ser366) and C-terminal (Ser419 and Ser423) regions of the BPS domain were phosphorylated by GSK-3. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264870 |
Ser362 |
QGRSGCSsQSISPMR |
in vitro |
|
pmid |
sentence |
28130417 |
Phosphorylation of clustered serine residues in the N-terminus of BPS domain negatively regulates formation of the complex between human Grb14 and insulin receptor| In vitro kinase assay using the motif-derived peptides showed that the serine residues located in N-terminal (Ser358, Ser362 and Ser366) and C-terminal (Ser419 and Ser423) regions of the BPS domain were phosphorylated by GSK-3. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264872 |
Ser366 |
GCSSQSIsPMRSISE |
in vitro |
|
pmid |
sentence |
28130417 |
Phosphorylation of clustered serine residues in the N-terminus of BPS domain negatively regulates formation of the complex between human Grb14 and insulin receptor| In vitro kinase assay using the motif-derived peptides showed that the serine residues located in N-terminal (Ser358, Ser362 and Ser366) and C-terminal (Ser419 and Ser423) regions of the BPS domain were phosphorylated by GSK-3. |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
GSK3A | down-regulates quantity by destabilization
phosphorylation
|
GATA6 |
0.268 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253156 |
Ser37 |
REPSTPPsPISSSSS |
Homo sapiens |
HT-29 Cell |
pmid |
sentence |
27273097 |
Through bioinformatics and cell-based experiments, we identified the AKT-repressed signal as glycogen synthase kinase 3 (GSK3)-catalyzed phosphorylation of Ser(37) on the long form of the transcription factor GATA6. Phosphorylation of GATA6 on Ser(37) promoted its degradation, thereby preventing GATA6 from repressing transcripts that are induced by TNF and attenuated by insulin |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | down-regulates quantity by destabilization
phosphorylation
|
STAT2 |
0.266 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276760 |
Ser381 |
RKFNILTsNQKTLTP |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
31843895 |
GSK3α/β are critical kinases to regulate STAT2 protein stability mediated by FBXW7.The 4-point mutant (STAT2-4A) of STAT2 at S381A/T385A/E389A/S393A inhibited GSK3α/β-mediated STAT2 phosphorylation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276762 |
Ser393 |
LTPEKGQsQGLIWDF |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
31843895 |
GSK3α/β are critical kinases to regulate STAT2 protein stability mediated by FBXW7.The 4-point mutant (STAT2-4A) of STAT2 at S381A/T385A/E389A/S393A inhibited GSK3α/β-mediated STAT2 phosphorylation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276761 |
Thr385 |
ILTSNQKtLTPEKGQ |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
31843895 |
GSK3α/β are critical kinases to regulate STAT2 protein stability mediated by FBXW7.The 4-point mutant (STAT2-4A) of STAT2 at S381A/T385A/E389A/S393A inhibited GSK3α/β-mediated STAT2 phosphorylation. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
GSK3A | down-regulates quantity by destabilization
phosphorylation
|
BCL3 |
0.401 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276011 |
Ser402 |
LSASPSSsPSQSPPR |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
15469820 |
In this report, we show that BCL-3 is a substrate for the protein kinase GSK3 and that GSK3-mediated BCL-3 phosphorylation, which is inhibited by Akt activation, targets its degradation through the proteasome pathway. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276012 |
Ser406 |
PSSSPSQsPPRDPPG |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
15469820 |
In this report, we show that BCL-3 is a substrate for the protein kinase GSK3 and that GSK3-mediated BCL-3 phosphorylation, which is inhibited by Akt activation, targets its degradation through the proteasome pathway. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
GSK3A | up-regulates
phosphorylation
|
MITF |
0.299 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-72878 |
Ser405 |
QARAHGLsLIPSTGL |
Homo sapiens |
|
pmid |
sentence |
10587587 |
Glycogen synthase kinase 3 (gsk3) was found to phosphorylate ser298 in vitro, thereby enhancing the binding of mitf to the tyrosinase promoter |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | up-regulates activity
phosphorylation
|
MAFA |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159365 |
Ser49 |
CHRLPPGsLSSTPLS |
Homo sapiens |
|
pmid |
sentence |
18042454 |
We also demonstrate that gsk-3 triggers mafa sequential phosphorylation on residues s61, t57, t53, and s49 /we demonstrated that phosphorylation by gsk-3 is conserved among the large maf proteins. It couples ubiquitination/degradation and transcriptional activation and modulates maf biological activity./ Taken together, these results suggest that, in contrast to what can be expected from ubiquitination/degradation, gsk-3-mediated mafa phosphorylation increases its transactivating ability, thereby controlling its biological activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159369 |
Ser61 |
PLSTPCSsVPSSPSF |
Homo sapiens |
|
pmid |
sentence |
18042454 |
We also demonstrate that gsk-3 triggers mafa sequential phosphorylation on residues s61, t57, t53, and s49 /we demonstrated that phosphorylation by gsk-3 is conserved among the large maf proteins. It couples ubiquitination/degradation and transcriptional activation and modulates maf biological activity./ Taken together, these results suggest that, in contrast to what can be expected from ubiquitination/degradation, gsk-3-mediated mafa phosphorylation increases its transactivating ability, thereby controlling its biological activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159373 |
Thr53 |
PPGSLSStPLSTPCS |
Homo sapiens |
|
pmid |
sentence |
18042454 |
We also demonstrate that gsk-3 triggers mafa sequential phosphorylation on residues s61, t57, t53, and s49 /we demonstrated that phosphorylation by gsk-3 is conserved among the large maf proteins. It couples ubiquitination/degradation and transcriptional activation and modulates maf biological activity./ Taken together, these results suggest that, in contrast to what can be expected from ubiquitination/degradation, gsk-3-mediated mafa phosphorylation increases its transactivating ability, thereby controlling its biological activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159377 |
Thr57 |
LSSTPLStPCSSVPS |
Homo sapiens |
|
pmid |
sentence |
18042454 |
We also demonstrate that gsk-3 triggers mafa sequential phosphorylation on residues s61, t57, t53, and s49 /we demonstrated that phosphorylation by gsk-3 is conserved among the large maf proteins. It couples ubiquitination/degradation and transcriptional activation and modulates maf biological activity./ Taken together, these results suggest that, in contrast to what can be expected from ubiquitination/degradation, gsk-3-mediated mafa phosphorylation increases its transactivating ability, thereby controlling its biological activity. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
GSK3A | down-regulates quantity by destabilization
phosphorylation
|
MAFA |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159381 |
Ser49 |
CHRLPPGsLSSTPLS |
Homo sapiens |
|
pmid |
sentence |
18042454 |
We also demonstrate that gsk-3 triggers mafa sequential phosphorylation on residues s61, t57, t53, and s49 /we demonstrated that phosphorylation by gsk-3 is conserved among the large maf proteins. It couples ubiquitination/degradation and transcriptional activation and modulates maf biological activity./ Taken together, these results suggest that, in contrast to what can be expected from ubiquitination/degradation, gsk-3-mediated mafa phosphorylation increases its transactivating ability, thereby controlling its biological activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159390 |
Ser61 |
PLSTPCSsVPSSPSF |
Homo sapiens |
|
pmid |
sentence |
18042454 |
We also demonstrate that gsk-3 triggers mafa sequential phosphorylation on residues s61, t57, t53, and s49 /we demonstrated that phosphorylation by gsk-3 is conserved among the large maf proteins. It couples ubiquitination/degradation and transcriptional activation and modulates maf biological activity./ Taken together, these results suggest that, in contrast to what can be expected from ubiquitination/degradation, gsk-3-mediated mafa phosphorylation increases its transactivating ability, thereby controlling its biological activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159394 |
Thr53 |
PPGSLSStPLSTPCS |
Homo sapiens |
|
pmid |
sentence |
18042454 |
We also demonstrate that gsk-3 triggers mafa sequential phosphorylation on residues s61, t57, t53, and s49 /we demonstrated that phosphorylation by gsk-3 is conserved among the large maf proteins. It couples ubiquitination/degradation and transcriptional activation and modulates maf biological activity./ Taken together, these results suggest that, in contrast to what can be expected from ubiquitination/degradation, gsk-3-mediated mafa phosphorylation increases its transactivating ability, thereby controlling its biological activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159398 |
Thr57 |
LSSTPLStPCSSVPS |
Homo sapiens |
|
pmid |
sentence |
18042454 |
We also demonstrate that gsk-3 triggers mafa sequential phosphorylation on residues s61, t57, t53, and s49 /we demonstrated that phosphorylation by gsk-3 is conserved among the large maf proteins. It couples ubiquitination/degradation and transcriptional activation and modulates maf biological activity./ Taken together, these results suggest that, in contrast to what can be expected from ubiquitination/degradation, gsk-3-mediated mafa phosphorylation increases its transactivating ability, thereby controlling its biological activity. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
GSK3A | down-regulates quantity by destabilization
phosphorylation
|
NCOA3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276067 |
Ser509 |
GVHSPMAsSGNTGNH |
Homo sapiens |
MCF-7 Cell |
pmid |
sentence |
17574025 |
GSK3 Phosphorylates SRC-3 on S505.In this report, we identified GSK3 as a kinase that phosphorylates SRC-3 on S505 and demonstrated that this phosphorylation modulates SRC-3 transcriptional function and turnover. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | down-regulates activity
phosphorylation
|
EIF2B5 |
0.375 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251215 |
Ser540 |
MDSEEPDsRGGSPQM |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
11500362 |
We identify multiple phosphorylation sites in the largest, catalytic, subunit (epsilon) of mammalian eIF2B. Glycogen synthase kinase 3 (GSK3) is responsible for phosphorylating Ser535. This regulatory phosphorylation event requires both the fourth site (Ser539) and a distal region, which acts to recruit GSK3 to eIF2Bepsilon in vivo. eIF2Bϵ from mammals or insects is a substrate for glycogen synthase kinase 3 (GSK3), and this inhibits the activity of eIF2B |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | down-regulates
phosphorylation
|
MAPT |
0.44 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-60651 |
Ser579 |
NVKSKIGsTENLKHQ |
Homo sapiens |
Neuron |
pmid |
sentence |
9771888 |
Tau is phosphorylated by gsk-3 at several sites found in alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by a-kinase. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-29364 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
7566348 |
The ability of p42 map and p44 map kinases, glycogen synthase kinases 3 alpha and 3 beta (gsk-3 alpha and gsk-3 beta) to phosphorylate tau in transfected cos cells was investigated. Both gsk-3 alpha and gsk-3 beta phosphorylated tau to produce a phf-like state of phosphorylation but the map kinases failed to induce such a transformation in tau. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | Alzheimer |
+ |
GSK3A | up-regulates activity
phosphorylation
|
STMN3 |
0.254 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264883 |
Ser60 |
SFEVILKsPSDLSPE |
in vitro |
|
pmid |
sentence |
22577147 |
Altogether, these results indicate that CDK5 phosphorylates similarly serines 68 and 73, whereas ERK2 targets mostly serine 68 and GSK-3beta mostly serine 60.|This observation may support the hypothesis of a specific localization of stathmin 3 depending on its phosphorylation by GSK-3beta |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
GSK3A | down-regulates quantity by destabilization
phosphorylation
|
UNG |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264886 |
Ser64 |
EPGTPPSsPLSAEQL |
Homo sapiens |
OVCAR-3 Cell |
pmid |
sentence |
27875297 |
Here we show that glycogen synthase kinase 3 (GSK-3) interacts with and phosphorylates UNG2 at Thr60 and that Thr60 phosphorylation requires a Ser64 priming phosphorylation event.|phosphorylation of Thr60 and Ser64 creates a cyclin E/c-Myc-like phosphodegron that promotes polyubiquitylation and proteasome-mediated degradation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264887 |
Thr60 |
AGQEEPGtPPSSPLS |
Homo sapiens |
OVCAR-3 Cell |
pmid |
sentence |
27875297 |
Here we show that glycogen synthase kinase 3 (GSK-3) interacts with and phosphorylates UNG2 at Thr60 and that Thr60 phosphorylation requires a Ser64 priming phosphorylation event.|phosphorylation of Thr60 and Ser64 creates a cyclin E/c-Myc-like phosphodegron that promotes polyubiquitylation and proteasome-mediated degradation |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
GSK3A | down-regulates
phosphorylation
|
GYS1 |
0.422 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-118927 |
Ser641 |
YRYPRPAsVPPSPSL |
Homo sapiens |
|
pmid |
sentence |
14593110 |
Glycogen synthase kinase-3 (gsk-3) phosphorylates four serine residues in the cooh terminus of glycogen synthase. Phosphorylation of one of these residues, ser640 (site 3a), causes strong inactivation of glycogen synthase |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle, Skeletal Muscle |
+ |
GSK3A | down-regulates activity
phosphorylation
|
MAPT |
0.44 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249342 |
Ser641 |
KVTSKCGsLGNIHHK |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
pmid |
sentence |
7706316 |
Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Alzheimer |
+ |
GSK3A |
phosphorylation
|
PKD2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145306 |
Ser76 |
AGAAASPsPPLSSCS |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16551655 |
We report the identification of a new phosphorylation site for pc2 within its n-terminal domain (ser(76)) and demonstrate that this residue is phosphorylated by glycogen synthase kinase 3 (gsk3). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Kidney |
+ |
GSK3A | down-regulates quantity by destabilization
phosphorylation
|
RICTOR |
0.395 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276899 |
Thr1695 |
EAEAVLAtPPKQPIV |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
25897075 |
We show that this process is dependent on glycogen synthase kinase 3 (GSK3): GSK3 was associated with rictor and directly phosphorylated the Thr-1695 site in a putative CDC4 phospho-degron motif of rictor; mutation of this site impaired the interaction between rictor and FBXW7, decreased rictor ubiquitination, and increased rictor stability. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | up-regulates activity
phosphorylation
|
NIFK |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262697 |
Thr234 |
TVDSQGPtPVCTPTF |
in vitro |
|
pmid |
sentence |
16244663 |
The forkhead-associated (FHA) domain of human Ki67 interacts with the human nucleolar protein hNIFK, recognizing a 44-residue fragment, hNIFK226-269, phosphorylated at Thr234. Here we show that high-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230. phosphorylation of Thr234 by GSK3 proceeds only after Thr238 is already phosphorylated by CDK1. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
GSK3A | up-regulates activity
phosphorylation
|
RELA |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255827 |
Thr254 |
RQVAIVFRtPPYADPS |
Mus musculus |
Chondrocyte |
pmid |
sentence |
22761446 |
Redundant functions of GSK-3_ and GSK-3_ through phosphorylation of RelA at Thr-254 play a crucial role in early stages of chondrocyte differentiation |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
GSK3A | down-regulates activity
phosphorylation
|
AKT |
0.621 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252455 |
Thr312 |
TMKTFCGtPEYLAPE |
Mus musculus |
Th17 Cell |
pmid |
sentence |
23142783 |
GSK3_ negatively regulates AKT activation by phosphorylating AKT at T312 in the substrate binding site, which inhibited IL-1-induced AKT activation and function. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
GSK3A | down-regulates activity
phosphorylation
|
AKT1 |
0.62 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252434 |
Thr312 |
TMKTFCGtPEYLAPE |
Mus musculus |
Th17 Cell |
pmid |
sentence |
23142783 |
GSK3_ negatively regulates AKT activation by phosphorylating AKT at T312 in the substrate binding site, which inhibited IL-1-induced AKT activation and function. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
GSK3A | down-regulates quantity by destabilization
phosphorylation
|
MYC |
0.415 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-138596 |
Thr58 |
KKFELLPtPPLSPSR |
Homo sapiens |
|
pmid |
sentence |
16023596 |
Similar to c-myc, similar to c-myc, we report here that phosphorylation of c-jun by gsk3 creates a high-affinity binding site for the e3 ligase fbw7, which targets c-jun for polyubiquitination and proteasomal degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | down-regulates activity
phosphorylation
|
NBR1 |
0.327 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261794 |
Thr586 |
HNTPVDVtPCMSPLP |
in vitro |
|
pmid |
sentence |
24879152 |
The autophagy receptor NBR1 (neighbor of BRCA1 gene 1) binds UB/ubiquitin and the autophagosome-conjugated MAP1LC3/LC3 (microtubule-associated protein 1 light chain 3) proteins, thereby ensuring ubiquitinated protein degradation|Here we show that NBR1 is a substrate of GSK3. NBR1 phosphorylation by GSK3 at Thr586 prevents the aggregation of ubiquitinated proteins and their selective autophagic degradation. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
GSK3A | down-regulates
phosphorylation
|
SFPQ |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-168382 |
Thr687 |
PRGMGPGtPAGYGRG |
Homo sapiens |
|
pmid |
sentence |
20932480 |
Here we demonstrate that in resting tcells psf is directly phosphorylated by gsk3, thus promoting interaction of psf with trap150, which prevents psf from binding cd45 pre-mrna. Upon tcell activation, reduced gsk3 activity leads to reduced psf phosphorylation, releasing psf from trap150 and allowing it to bind cd45 splicing regulatory elements and repress exon inclusion. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-168385 |
|
|
Homo sapiens |
|
pmid |
sentence |
20932480 |
Psf is directly phosphorylated by gsk3, thus promoting interaction of psf with trap150, which prevents psf from binding cd45 pre-mrna. / threonine phosphorylation of psf by gsk3 primarily occurs on residue t687 |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
GSK3A | down-regulates quantity by destabilization
phosphorylation
|
IL17RA |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277206 |
Thr780 |
MVLTDPHtPYEEEQR |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
26871944 |
Glycogen synthase kinase 3 (GSK3) constitutively bound to and phosphorylated IL-17RA at T780, leading to ubiquitination and proteasome-mediated degradation of IL-17RA, thus inhibiting IL-17-mediated inflammation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | up-regulates activity
phosphorylation
|
ARHGAP31 |
0.344 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262878 |
Thr789 |
PPAPPPPtPLEESTP |
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
17158447 |
We show that GSK-3alpha and -beta interact with CdGAP in mammalian cells. We also demonstrate that GSK-3 phosphorylates CdGAP both in vitro and in vivo on Thr-776, which we have previously shown to be an ERK 1/2 phosphorylation site involved in CdGAP regulation. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
GSK3A | up-regulates
phosphorylation
|
GSK3A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-180035 |
Tyr279 |
RGEPNVSyICSRYYR |
Homo sapiens |
Glioblastoma Cell |
pmid |
sentence |
18701488 |
Gsk3a is activated by phosphorylation at tyr-279. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Alzheimer |
+ |
CHIR-98014 | down-regulates
chemical inhibition
|
GSK3A |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-190985 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CAPN2 | up-regulates activity
cleavage
|
GSK3A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251612 |
|
|
Homo sapiens |
|
pmid |
sentence |
25969760 |
Thus, it has been shown that calpain cleaves the inhibitory domain of GSK3 generating two fragments of 40 and 30 kDa. This cleavage enhanced activity of the kinase |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT2 | down-regulates
phosphorylation
|
GSK3A |
0.538 |
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 |
+ |
CAPN1 | up-regulates activity
cleavage
|
GSK3A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251585 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
pmid |
sentence |
25969760 |
Thus, it has been shown that calpain cleaves the inhibitory domain of GSK3 generating two fragments of 40 and 30 kDa. This cleavage enhanced activity of the kinase |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Alzheimer |
+ |
CAPN3 | up-regulates activity
cleavage
|
GSK3A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251606 |
|
|
Homo sapiens |
|
pmid |
sentence |
25969760 |
Thus, it has been shown that calpain cleaves the inhibitory domain of GSK3 generating two fragments of 40 and 30 kDa. This cleavage enhanced activity of the kinase |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | down-regulates
phosphorylation
|
MAFB |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159432 |
|
|
Homo sapiens |
|
pmid |
sentence |
18042454 |
We showed that c-maf and mafb, like mafa, are indeed phosphorylated by gsk-3/ we demonstrated that phosphorylation by gsk-3 is conserved among the large maf proteins. It couples ubiquitination/degradation and transcriptional activation and modulates maf biological activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | up-regulates
phosphorylation
|
TSC2 |
0.37 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-149377 |
|
|
Homo sapiens |
|
pmid |
sentence |
16959574 |
Gsk3 inhibits the mtor pathway by phosphorylating tsc2 in a manner dependent on ampk-priming phosphorylation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164098 |
|
|
Homo sapiens |
|
pmid |
sentence |
20226003 |
Gsk3 inhibits the mtor pathway by phosphorylating tsc2 in a manner dependent on ampk-priming phosphorylation. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
GSK3A | up-regulates
phosphorylation
|
MAFB |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159429 |
|
|
Homo sapiens |
|
pmid |
sentence |
18042454 |
We showed that c-maf and mafb, like mafa, are indeed phosphorylated by gsk-3/ we demonstrated that phosphorylation by gsk-3 is conserved among the large maf proteins. It couples ubiquitination/degradation and transcriptional activation and modulates maf biological activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
APP | up-regulates
|
GSK3A |
0.419 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-144057 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
16446437 |
These results suggest a direct relationship between app proteolytic processing, but not amyloid-_, in gsk-3_ activation and tau phosphorylation in human neurons. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Alzheimer |
+ |
CHIR 99021 | down-regulates
chemical inhibition
|
GSK3A |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-190997 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | up-regulates activity
phosphorylation
|
OSBP2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264875 |
|
|
|
|
pmid |
sentence |
30925160 |
CK1a1, JNK1 and CDK1 had the highest site-specific activity for ORP4L, while CDK1, GSK3a, CK1a1 and GSK3b showed the highest specificity for the site when corrected for background activity with ORP4L-S4A. Because of the complexity of the serine/proline-rich site, we did not determine which serine(s) in ORP4L were phosphorylated by candidate kinases.|We conclude that phosphorylation of a unique serine/proline motif in the ORD induces a conformation change in ORP4L that enhances interaction with vimentin and cholesterol extraction from membranes. |
|
Publications: |
1 |
+ |
SB 415286 | down-regulates
chemical inhibition
|
GSK3A |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-206751 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | up-regulates
phosphorylation
|
MAF |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159358 |
|
|
Homo sapiens |
|
pmid |
sentence |
18042454 |
We showed that c-maf and mafb, like mafa, are indeed phosphorylated by gsk-3/ we demonstrated that phosphorylation by gsk-3 is conserved among the large maf proteins. It couples ubiquitination/degradation and transcriptional activation and modulates maf biological activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | down-regulates
phosphorylation
|
MAF |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159361 |
|
|
Homo sapiens |
|
pmid |
sentence |
18042454 |
We showed that c-maf and mafb, like mafa, are indeed phosphorylated by gsk-3/ we demonstrated that phosphorylation by gsk-3 is conserved among the large maf proteins. It couples ubiquitination/degradation and transcriptional activation and modulates maf biological activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | down-regulates
phosphorylation
|
NOTCH1 |
0.325 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-183969 |
|
|
Homo sapiens |
|
pmid |
sentence |
19214430 |
Taken together, our results indicate that gsk-3alfa is a negative regulator of notch1/nicd. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |