Relation Results

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251242	Ser159	NNTSTDGsLPSTPPP	Mus musculus	FL5.12 Cell
pmid	sentence
16543145	MCL-1 was phosphorylated by GSK-3 at a conserved GSK-3 phosphorylation site (S159). S159 phosphorylation of MCL-1 was induced by IL-3 withdrawal or PI3K inhibition and prevented by AKT or inhibition of GSK-3, and it led to increased ubiquitinylation and degradation of MCL-1.

Publications:

1

Organism:

Mus Musculus

Pathways:

Alzheimer, Acute Myeloid Leukemia, FLT3-ITD signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-130141	Ser163	GGWDGLLsYFGTPTW	Homo sapiens	Neuron
pmid	sentence
15525785	Glycogen synthase kinase-3beta phosphorylates bax and promotes its mitochondrial localization during neuronal apoptosis. Gsk-3beta directly phosphorylated bax(alpha) on ser163

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249359	Ser163	PDKQFLIsPPASPPV	Mus musculus	C2C12 Cell
pmid	sentence
12063245	Consensus phosphorylation sites for p42/44 MAPK and GSK-3 are present in the SP repeat of MCIP1 at serine 112 and serine 108, respectively \|Several endogenous proteins are capable of inhibiting the catalytic activity of calcineurin. Modulatory calcineurin interacting protein 1 (MCIP1) is unique among these proteins on the basis of its pattern of expression and its function in a negative feedback loop to regulate calcineurin activity. Here we show that MCIP1 can be phosphorylated by MAPK and glycogen synthase kinase-3 and that phosphorylated MCIP1 is a substrate for calcineurin.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-162786	Ser17	STISDFMsPGPTDLL	Homo sapiens
pmid	sentence
20049328	Gsk3beta phosphorylates bmal1 specifically on ser 17 and thr 21 and primes it for ubiquitylation. In the absence of gsk3beta-mediated phosphorylation, bmal1 becomes stabilized and bmal1 dependent circadian gene expression is dampened.

Identifier	Residue	Sequence	Organism
SIGNOR-162790	Thr21	DFMSPGPtDLLSSSL	Homo sapiens
pmid	sentence
20049328	Gsk3beta phosphorylates bmal1 specifically on ser 17 and thr 21 and primes it for ubiquitylation. In the absence of gsk3beta-mediated phosphorylation, bmal1 becomes stabilized and bmal1 dependent circadian gene expression is dampened.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276345	Ser183	SNLLQSPsSILSTLD	Homo sapiens	HeLa Cell
pmid	sentence
21757741	Here, we demonstrate that glycogen synthase kinase-3β (GSK3β) phosphorylates securin to promote its proteolysis via SCF(βTrCP) E3 ubiquitin ligase.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276344	Ser184	NLLQSPSsILSTLDV	Homo sapiens	HeLa Cell
pmid	sentence
21757741	Here, we demonstrate that glycogen synthase kinase-3β (GSK3β) phosphorylates securin to promote its proteolysis via SCF(βTrCP) E3 ubiquitin ligase.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276354	Ser186	APRTHPYsPKSEAPR	Homo sapiens	T-98G Cell
pmid	sentence
21873430	Both MITF and USF1 were activated by glycogen synthase kinase (GSK) 3, with GSK3 phosphorylation sites on USF1 identified as the previously described activating site threonine 153 as well as serine 186.

Identifier	Residue	Sequence	Organism
SIGNOR-276355	Thr153	EALLGQAtPPGTGQF	Homo sapiens
pmid	sentence
21873430	Both MITF and USF1 were activated by glycogen synthase kinase (GSK) 3, with GSK3 phosphorylation sites on USF1 identified as the previously described activating site threonine 153 as well as serine 186.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276057	Ser188	RLQQRRGsQPETRTG	Homo sapiens	HEK-293T Cell
pmid	sentence
16982607	Protein kinase A (PKA) was found to phosphorylate Ser188 in vitro as well as in intact cells. Importantly, activation of endogenous cAMP-coupled beta-adrenergic receptors with norepinephrine stimulated the phosphorylation of FRAT1 at Ser188. GSK-3 was also able to phosphorylate FRAT1 at Ser188 and other residues in vitro or when overexpressed in intact cells. Phosphorylation of Ser188 by PKA inhibited the ability of FRAT1 to activate beta-catenin-dependent transcription.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264880	Ser191	IESFGSKsGRTSKKI	Homo sapiens	HEK-293 Cell
pmid	sentence
32814770	Phosphorylation of cyclophilin D at serine 191 regulates mitochondrial permeability transition pore opening and cell death after ischemia-reperfusion\|We conclude that CypD phosphorylation at S191 residue leads to its binding to OSCP and thus sensitizes mPTP opening for the subsequent cell death.\|Under baseline condition (WT group), the phosphorylation of CypD by a kinase (e.g. GSK3beta) at S191 induces its translocation to the OSCP, to favor mPTP opening and subsequent cell death at reperfusion.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-203011	Ser195	DQYPYAAsPATAASF	Homo sapiens
pmid	sentence
24142875	Here, we showed that rnpc1 is phosphorylated at ser195 by glycogen synthase kinase 3 (gsk3). We also provided evidence that ser195 phosphorylation converts rnpc1 from a repressor to an activator of p53.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251254	Ser2070	DEYNVTPsPPGTVLT	Homo sapiens	HEK-293 Cell
pmid	sentence
12794074	Ser-2093 is efficiently phosphorylated by GSK-3β and, to a minor extent, residues Thr-2068 and/or Ser-2070 and Thr-2074 of Notch2 are also targets for GSK-3β-dependent phosphorylation. We also find that GSK-3β-dependent phosphorylation of Notch2 is inhibiting transcriptional activation of different Notch target genes.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251253	Ser2093	GPNRSFLsLKHTPMG	Homo sapiens	HEK-293 Cell
pmid	sentence
12794074	Ser-2093 is efficiently phosphorylated by GSK-3β and, to a minor extent, residues Thr-2068 and/or Ser-2070 and Thr-2074 of Notch2 are also targets for GSK-3β-dependent phosphorylation. We also find that GSK-3β-dependent phosphorylation of Notch2 is inhibiting transcriptional activation of different Notch target genes.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-101570	Thr2068	LLDEYNVtPSPPGTV	Homo sapiens	HEK-293 Cell
pmid	sentence
12794074	We show that gsk-3beta directly binds at c-terminal of the notch2 ankyrin repeats and phosphorylates thr-2068 and/or ser-2070, thr-2074, and thr-2093.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-101574	Thr2074	VTPSPPGtVLTSALS	Homo sapiens	HEK-293 Cell
pmid	sentence
12794074	We show that gsk-3beta directly binds at c-terminal of the notch2 ankyrin repeats and phosphorylates thr-2068 and/or ser-2070, thr-2074, and thr-2093.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276163	Ser212	KLDTFCGsPPYAAPE	in vitro
pmid	sentence
18424437	MARK family kinases can be activated by phosphorylation of a conserved threonine (Thr-208 in MARK2), and inactivated by phosphorylation of a serine (Ser-212), both in the activation loop of the catalytic domain. Activation is achieved by the kinases MARKK/TAO1 or LKB1, although the inactivating kinase was unknown. We show here that GSK3beta serves the role of the inhibitory kinase.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275746	Ser226	PKPGVTPsKSTSASA	Homo sapiens	Neuron
pmid	sentence
32599005	Our laboratory has also demonstrated that FGF14 is a key accessory protein that binds to the intracellular Nav1.6 C-terminal tail, and that GSK3β can phosphorylate FGF14 both in vitro and in vivo at S226 [20] in an experimental model of Alzheimer's disease

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-156514	Ser231	LSTSSSSsPPGTPSP	Homo sapiens
pmid	sentence
17601773	Mass spectrometric analysis revealed that cdk2/cyclinA phosphorylates C/EBPbeta on Thr(188) and is required for phosphorylation (on Ser(184) or Thr(179)) of C/EBPbeta by GSK3beta and maintenance of DNA binding activity. However, the acquisition of dna binding and transactivation capacity of c/ebpbeta is delayed until further phosphorylation (on ser(184) or thr(179)) by gsk3beta occurs.

Identifier	Residue	Sequence	Organism
SIGNOR-196377	Ser231	LSTSSSSsPPGTPSP	Homo sapiens
pmid	sentence
22369944	However, the acquisition of dna binding and transactivation capacity of c/ebpbeta is delayed until further phosphorylation (on ser(184) or thr(179)) by gsk3beta occurs.

Identifier	Residue	Sequence	Organism
SIGNOR-210129	Thr226	GSSGSLStSSSSSPP	Homo sapiens
pmid	sentence
22369944	However, the acquisition of dna binding and transactivation capacity of c/ebpbeta is delayed until further phosphorylation (on ser(184) or thr(179)) by gsk3beta occurs.

Publications:

3

Organism:

Homo Sapiens

Pathways:

Adipogenesis, Acute Myeloid Leukemia, FLT3-ITD signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235892	Ser243	PGETPPLsPIDMESQ	Homo sapiens	HEK-293 Cell
pmid	sentence
16023596	The c-jun and c-myc oncogenic transcription factors are highly unstable proteins due to polyubiquitination. 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 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.Phosphorylation of Thr-239 and Ser-243 is required for Fbw7-mediated c-Jun disappearance

Identifier	Residue	Sequence	Organism
SIGNOR-18684	Ser249	LSPIDMEsQERIKAE	in vitro
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-236717	Thr239	VPEMPGEtPPLSPID	Homo sapiens	HEK-293 Cell
pmid	sentence
16023596	The c-jun and c-myc oncogenic transcription factors are highly unstable proteins due to polyubiquitination. 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 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.Phosphorylation of Thr-239 and Ser-243 is required for Fbw7-mediated c-Jun disappearance

Publications:

3

Organism:

Homo Sapiens, In Vitro

Pathways:

Acute Myeloid Leukemia, Insulin Signaling, WNT/FLT3

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276418	Ser251	QTVPEARsRDATPPV	Homo sapiens	HeLa Cell
pmid	sentence
22710716	Thus, JunB phosphorylation at S251 and T255 by GSK3β is primed by phosphorylation at S259 by a yet to-be-identified kinase.Phosphorylation at S251, T255 and S259 is required for JunB degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276417	Thr255	EARSRDAtPPVSPIN	Homo sapiens	HeLa Cell
pmid	sentence
22710716	Thus, JunB phosphorylation at S251 and T255 by GSK3β is primed by phosphorylation at S259 by a yet to-be-identified kinase.Phosphorylation at S251, T255 and S259 is required for JunB degradation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251234	Ser252	MEGYRAPsRQDVYGP	in vitro
pmid	sentence
12885254	GSK3beta selectively phosphorylates p120 on S252 and T310 in Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-251235	Thr310	GTARRTGtPSDPRRR	in vitro
pmid	sentence
12885254	GSK3beta selectively phosphorylates p120 on S252 and T310 in Vitro

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264821	Ser256	LRRAIQLsMQGSSRN	Homo sapiens	HEK-293 Cell
pmid	sentence
17434145	Phosphorylation of ataxin-3 by glycogen synthase kinase 3beta at serine 256 regulates the aggregation of ataxin-3\|

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-255566	Ser268	LPPGLSAsPQPSSVA	Mus musculus	MIN-6 Cell
pmid	sentence
19833727	We show that glucose levels modulate PDX1 protein phosphorylation at a novel C-terminal GSK3 consensus that maps to serines 268 and 272. A decrease in glucose levels triggers increased turnover of the PDX1 protein in a GSK3-dependent manner, such that PDX1 phosphomutants are refractory to the destabilizing effect of low glucose

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-255567	Ser272	LSASPQPsSVAPRRP	Mus musculus	MIN-6 Cell
pmid	sentence
19833727	We show that glucose levels modulate PDX1 protein phosphorylation at a novel C-terminal GSK3 consensus that maps to serines 268 and 272. A decrease in glucose levels triggers increased turnover of the PDX1 protein in a GSK3-dependent manner, such that PDX1 phosphomutants are refractory to the destabilizing effect of low glucose

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-255543	Ser61	LGALEQGsPPDISPY	Mus musculus	Pancreatic Beta Cell, MIN-6 Cell
pmid	sentence
16407209	Here we show that a minor portion of IPF1/PDX1 is phosphorylated on serine 61 and/or serine 66 in pancreatic beta-cells. This phosphorylated form of IPF1/PDX1 preferentially accumulates following proteasome inhibition, an effect that is prevented by inhibition of glycogen synthase kinase 3 (GSK3) activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-255544	Ser66	QGSPPDIsPYEVPPL	Mus musculus	Pancreatic Beta Cell, MIN-6 Cell
pmid	sentence
16407209	Here we show that a minor portion of IPF1/PDX1 is phosphorylated on serine 61 and/or serine 66 in pancreatic beta-cells. This phosphorylated form of IPF1/PDX1 preferentially accumulates following proteasome inhibition, an effect that is prevented by inhibition of glycogen synthase kinase 3 (GSK3) activity.

Publications:

4

Organism:

Mus Musculus

Pathways:

Insulin Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-200957	Ser270	LSTTPSEsPRAQATS	Homo sapiens
pmid	sentence
23408424	Identification of gsk3_ as the kinase targeting ser-270 /phosphorylation at ser-270 promotes gephyrin processing by calpain

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-201515	Ser274	TSPSPISsPTFSPIE	Homo sapiens
pmid	sentence
23442801	It suggests that gsk3_ activity is required for hbora-mediated mitotic entry through ser274 and ser278 phosphorylation

Identifier	Residue	Sequence	Organism
SIGNOR-201519	Ser278	PISSPTFsPIEFQIG	Homo sapiens
pmid	sentence
23442801	It suggests that gsk3_ activity is required for hbora-mediated mitotic entry through ser274 and ser278 phosphorylation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251227	Ser283	RSVPEPLsPVSSLQA	in vitro
pmid	sentence
16027724	GSK-3, p38 and CDK2 can phosphorylate Cdx2 through the 4S motif in vitro, but only CDK2 was shown to be active in vivo. the compound mutant 4S>A (serines 281, 285, 289 and 293 replaced by alanines)

Identifier	Residue	Sequence	Organism
SIGNOR-251228	Ser287	EPLSPVSsLQASVPG	in vitro
pmid	sentence
16027724	GSK-3, p38 and CDK2 can phosphorylate Cdx2 through the 4S motif in vitro, but only CDK2 was shown to be active in vivo. the compound mutant 4S>A (serines 281, 285, 289 and 293 replaced by alanines)

Identifier	Residue	Sequence	Organism
SIGNOR-251229	Ser291	PVSSLQAsVPGSVPG	in vitro
pmid	sentence
16027724	GSK-3, p38 and CDK2 can phosphorylate Cdx2 through the 4S motif in vitro, but only CDK2 was shown to be active in vivo. the compound mutant 4S>A (serines 281, 285, 289 and 293 replaced by alanines)

Identifier	Residue	Sequence	Organism
SIGNOR-251230	Ser295	LQASVPGsVPGVLGP	in vitro
pmid	sentence
16027724	GSK-3, p38 and CDK2 can phosphorylate Cdx2 through the 4S motif in vitro, but only CDK2 was shown to be active in vivo. the compound mutant 4S>A (serines 281, 285, 289 and 293 replaced by alanines)

Publications:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264857	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

Identifier	Residue	Sequence	Organism
SIGNOR-170144	Ser298	ACSSAPGsGPSSPNN	Homo sapiens
pmid	sentence
21118993	The double mutation of serines 298/302 into alanines, but also the sole mutation of serine 302, abolishes hdac4 phosphorylation by gsk3_we have shown that cells lacking gsk3_ are unable to degrade hdac4 after serum starvation

Identifier	Residue	Sequence	Organism
SIGNOR-170148	Ser302	APGSGPSsPNNSSGS	Homo sapiens
pmid	sentence
21118993	The double mutation of serines 298/302 into alanines, but also the sole mutation of serine 302, abolishes hdac4 phosphorylation by gsk3_we have shown that cells lacking gsk3_ are unable to degrade hdac4 after serum starvation

Publications:

2

Organism:

Homo Sapiens

Pathways:

IGF and Myogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-264845	Ser300	RHRDNRRsPSLERSY	in vitro
pmid	sentence
25699712	Our findings suggest that phosphorylation of Drosha at multiple sites including S300 promotes its translocation to the cytoplasm. Interestingly, GSK3beta can phosphorylate Drosha at S300 and S302 in vitro. This has been reported to promote the nuclear localization of Drosha under basal condition (Tang et al., 2011). Thus, it appears that phosphorylation of S300 by GSK3beta and p38 MAPK is involved in opposing processes.

Identifier	Residue	Sequence	Organism
SIGNOR-264846	Ser302	RDNRRSPsLERSYKK	in vitro
pmid	sentence
25699712	Our findings suggest that phosphorylation of Drosha at multiple sites including S300 promotes its translocation to the cytoplasm. Interestingly, GSK3beta can phosphorylate Drosha at S300 and S302 in vitro. This has been reported to promote the nuclear localization of Drosha under basal condition (Tang et al., 2011). Thus, it appears that phosphorylation of S300 by GSK3beta and p38 MAPK is involved in opposing processes.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-203627	Ser303	QATYFPPsPPSSEPG	Homo sapiens
pmid	sentence
24398687	Stability of the klf5 is mediated by proteasomal degradation via phosphorylation by glycogen synthase kinase 3_ (gsk3_) and recognition by f-box and wd repeat domain-containing 7 (fbw7) of a phosphodegron sequence surrounding serine 303 in klf5

Publications:

1

Organism:

Homo Sapiens

Pathways:

Adipogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-44995	Ser303	RVKEEPPsPPQSPRV	Homo sapiens
pmid	sentence
8940068	Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthase kinase 3 represses transcriptional activation by heat shock factor-1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251216	Ser303	RVKEEPPsPPQSPRV	in vitro
pmid	sentence
8940068	Ser-303 is phosphorylated by glycogen synthase kinase 3 (GSK3) through a mechanism dependent on primary phosphorylation of Ser-307 by MAPK. Secondary phosphorylation of Ser-303 by GSK3 may thus repress the activity of HSF-1, and its requirement for priming by MAPK phosphorylation of Ser-307 provides a potential link between the MAPK cascade and HSF-1.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-264822	Ser308	SAPKPQTsPSPKRAT	Homo sapiens
pmid	sentence
30123351	We found that GSK3 phosphorylates S307 and S309 by using inhibitors LiCl. Inhibition of GSK3beta can cause loss of cell polarity as well as accumulation of stress fibers. We propose that GSK3 regulates CAP1 through at least two mechanisms. First, GSK3 (and potentially other kinases) phosphorylate CAP1 at S309 and promote CAP1 localization to the cytosol. Second, phosphorylation at S309 affects protein-protein interactions with actin and cofilin. The loss of this phospho-regulation by GSK3 inhibition is expected to disrupt CAP1 function and actin dynamics.

Identifier	Residue	Sequence	Organism
SIGNOR-264823	Ser310	PKPQTSPsPKRATKK	Homo sapiens
pmid	sentence
30123351	We found that GSK3 phosphorylates S307 and S309 by using inhibitors LiCl. Inhibition of GSK3beta can cause loss of cell polarity as well as accumulation of stress fibers. We propose that GSK3 regulates CAP1 through at least two mechanisms. First, GSK3 (and potentially other kinases) phosphorylate CAP1 at S309 and promote CAP1 localization to the cytosol. Second, phosphorylation at S309 affects protein-protein interactions with actin and cofilin. The loss of this phospho-regulation by GSK3 inhibition is expected to disrupt CAP1 function and actin dynamics.

Publications:

2

Organism:

Homo Sapiens

Tissue:

Lung

Identifier	Residue	Sequence	Organism
SIGNOR-116520	Ser33	QQQSYLDsGIHSGAT	Homo sapiens
pmid	sentence
11955436	Wnt regulation of beta-catenin degradation is essential for development and carcinogenesis. beta-catenin degradation is initiated upon amino-terminal serine/threonine phosphorylation, which is believed to be performed by glycogen synthase kinase-3 (GSK-3) in complex with tumor suppressor proteins Axin and adnomatous polyposis coli (APC).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-184781	Ser33	QQQSYLDsGIHSGAT	Homo sapiens	Neuron
pmid	sentence
19303846	DISC1 inhibits GSK3beta activity through direct physical interaction, which reduces beta-catenin phosphorylation and stabilizes beta-catenin.

Identifier	Residue	Sequence	Organism
SIGNOR-199504	Ser33	QQQSYLDsGIHSGAT	Homo sapiens
pmid	sentence
23151663	Beta-catenin phosphorylation in vivo is sequentially carried out by two distinct kinases, ckialfa and gsk-3. Ckialfa phosphorylation of s45 proceeds and is required for subsequent gsk-3 phosphorylation of t41, s37, and s33 one key substrate of gsk3 is the transcriptional co-activator beta catenin, whichis inactivated by gsk3 mediated phosphorylation and targeted for proteasomal degradation in unstimulated cells.

Identifier	Residue	Sequence	Organism
SIGNOR-141799	Ser33	QQQSYLDsGIHSGAT	Homo sapiens
pmid	sentence
16293724	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.

Identifier	Residue	Sequence	Organism
SIGNOR-116524	Ser37	YLDSGIHsGATTTAP	Homo sapiens
pmid	sentence
11955436	Wnt regulation of beta-catenin degradation is essential for development and carcinogenesis. beta-catenin degradation is initiated upon amino-terminal serine/threonine phosphorylation, which is believed to be performed by glycogen synthase kinase-3 (GSK-3) in complex with tumor suppressor proteins Axin and adnomatous polyposis coli (APC).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-184785	Ser37	YLDSGIHsGATTTAP	Homo sapiens	Neuron
pmid	sentence
19303846	DISC1 inhibits GSK3beta activity through direct physical interaction, which reduces beta-catenin phosphorylation and stabilizes beta-catenin.

Identifier	Residue	Sequence	Organism
SIGNOR-141803	Ser37	YLDSGIHsGATTTAP	Homo sapiens
pmid	sentence
16293724	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.

Identifier	Residue	Sequence	Organism
SIGNOR-116528	Thr41	GIHSGATtTAPSLSG	Homo sapiens
pmid	sentence
11955436	Wnt regulation of beta-catenin degradation is essential for development and carcinogenesis. beta-catenin degradation is initiated upon amino-terminal serine/threonine phosphorylation, which is believed to be performed by glycogen synthase kinase-3 (GSK-3) in complex with tumor suppressor proteins Axin and adnomatous polyposis coli (APC).

Identifier	Residue	Sequence	Organism
SIGNOR-141807	Thr41	GIHSGATtTAPSLSG	Homo sapiens
pmid	sentence
16293724	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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-184789	Thr41	GIHSGATtTAPSLSG	Homo sapiens	Neuron
pmid	sentence
19303846	DISC1 inhibits GSK3beta activity through direct physical interaction, which reduces beta-catenin phosphorylation and stabilizes beta-catenin.

Identifier	Residue	Sequence	Organism
SIGNOR-199512	Thr41	GIHSGATtTAPSLSG	Homo sapiens
pmid	sentence
23151663	Beta-catenin phosphorylation in vivo is sequentially carried out by two distinct kinases, ckialfa and gsk-3. Ckialfa phosphorylation of s45 proceeds and is required for subsequent gsk-3 phosphorylation of t41, s37, and s33 one key substrate of gsk3 is the transcriptional co-activator beta catenin, whichis inactivated by gsk3 mediated phosphorylation and targeted for proteasomal degradation in unstimulated cells.

Identifier	Residue	Sequence	Organism
SIGNOR-260016	Thr41	GIHSGATtTAPSLSG	in vitro
pmid	sentence
11955436	β-catenin degradation is initiated upon amino-terminal serine/threonine phosphorylation, which is believed to be performed by glycogen synthase kinase-3 (GSK-3) in complex with tumor suppressor proteins Axin and adnomatous polyposis coli (APC)

Publications:

12

Organism:

Homo Sapiens, In Vitro

Tissue:

Brain, Colonic Cancer Cell

Pathways:

Acute Myeloid Leukemia, FLT3-ITD signaling, WNT/FLT3

Identifier	Residue	Sequence	Organism
SIGNOR-251258	Ser33	LPENNVLsPLPSQAM	Homo sapiens
pmid	sentence
11483158	Glycogen synthase kinase3 beta phosphorylates serine 33 of p53 and activates p53's transcriptional activity.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, AML_TRIPLETS, FLT3-ITD signaling, Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, Triple mutant AML

Identifier	Residue	Sequence	Organism
SIGNOR-170755	Ser332	STPKSKQsPISTPTS	Homo sapiens
pmid	sentence
21159948	Gsk3b phosphorylates dcx at the distinct site of ser327 and thereby contributes to dcx function in the restriction of axon branching. Together, our data define a jip3-regulated gsk3_/dcx signaling pathway that restricts axon branching in the mammalian brain.Gsk3_ induces the phosphorylation of dcx at ser327, which contributes to dcx function in the inhibition of axon branching and self-contact.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-179412	Ser346	SEEDRSKsAPTSPCD	Homo sapiens
pmid	sentence
18604201	Specifically, we have identified three phosphorylation sites within pkcepsilon that control its association with 14-3-3.kinase (ser 350), gsk3 (ser 346) and pkc itself (ser 368)

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-153627	Ser353	SHLGPHRsTPESRAA	Homo sapiens	HEK-293 Cell
pmid	sentence
17360711	We demonstrate that phosphorylation of serines 353 and 357 by glycogen synthase kinase-3beta (gsk3beta) induces a structural change of the hydrophilic loop of ps1the structural change of ps1 reduces the interaction with beta-catenin leading to decreased phosphorylation and ubiquitination of beta-catenin.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-153631	Ser357	PHRSTPEsRAAVQEL	Homo sapiens	HEK-293 Cell
pmid	sentence
17360711	We demonstrate that phosphorylation of serines 353 and 357 by glycogen synthase kinase-3beta (gsk3beta) induces a structural change of the hydrophilic loop of ps1the structural change of ps1 reduces the interaction with beta-catenin leading to decreased phosphorylation and ubiquitination of beta-catenin.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-264868	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
SIGNOR-264867	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
SIGNOR-264869	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

Identifier	Residue	Sequence	Organism
SIGNOR-158959	Ser373	VQARLERsSSKSLER	Homo sapiens
pmid	sentence
17991736	Here we report that CIITA represses collagen transcription through a phosphorylation-dependent interaction between its proline/serine/threonine domain and co-repressor molecules such as histone deacetylase (HDAC2) and Sin3B. Mutation of a serine (S373A) in CIITA, within a glycogen synthase kinase 3 (GSK3) consensus site, decreases repression of collagen transcription by blocking interaction with Sin3B

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-193450	Ser379	SQDFLLFsPEVESLP	Homo sapiens	Neuron
pmid	sentence
23623971	Glycogen synthase kinase 3 regulates expression of nuclear factor-erythroid-2 related transcription factor-1 (nrf1) and inhibits pro-survival function of nrf1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-178603	Ser389	ARIQAAAsTPTNATA	Homo sapiens
pmid	sentence
18451303	Here, we show that p38 mitogen-activated protein kinase (mapk) also inactivates gsk3beta by direct phosphorylation at its c terminus, and this inactivation can lead to an accumulation of beta-catenin.

Identifier	Residue	Sequence	Organism
SIGNOR-157548	Ser389	ARIQAAAsTPTNATA	Homo sapiens
pmid	sentence
17726008	However p38alfa also inactivates gsk3b by direct phosphorilation of the c-terminal residue ser389. this non-canonicl p38 mapk-dependent phosphorilation of gsk3b seems to occur primarily in the brain and thymocytes.

Publications:

2

Organism:

Homo Sapiens

Tissue:

Brain

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264891	Ser391	SEKGLELsPPHASEA	Homo sapiens	NCI-H1299 Cell
pmid	sentence
28581525	CK1delta and GSK3beta kinases sequentially phosphorylate ZNF322A at serine-396 and then serine-391. Moreover, the doubly phosphorylated ZNF322A protein creates a destruction motif for the ubiquitin ligase FBXW7alpha leading to ZNF322A protein destruction.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-167286	Ser396	DDKKAKTsTRSSAKT	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
20679343	Alzheimer disease neurons are characterized by extraneuronal plaques formed by aggregated amyloid-? Peptide and by intraneuronal tangles composed of fibrillar aggregates of the microtubule-associated tau protein. Tau is mostly found in a hyperphosphorylated form in these tangleswe find that three residues can be phosphorylated (ser-396, ser-400, and ser-404) by gsk3?

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-167290	Ser400	AKTSTRSsAKTLKNR	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
20679343	Alzheimer disease neurons are characterized by extraneuronal plaques formed by aggregated amyloid-? Peptide and by intraneuronal tangles composed of fibrillar aggregates of the microtubule-associated tau protein. Tau is mostly found in a hyperphosphorylated form in these tangleswe find that three residues can be phosphorylated (ser-396, ser-400, and ser-404) by gsk3?

Identifier	Residue	Sequence	Organism
SIGNOR-164651	Ser516	GDRSGYSsPGSPGTP	Homo sapiens
pmid	sentence
20308788	Abnormal hyperphosphorylation of tau appears to be crucial in neurofibrillary degeneration in alzheimer's disease (ad). Gsk-3beta phosphorylated tau at many sites, with ser199, thr205, and ser396 being the most favorable sites in cells.

Identifier	Residue	Sequence	Organism
SIGNOR-150360	Ser519	SGYSSPGsPGTPGSR	Homo sapiens
pmid	sentence
17078951	Here, we found that prephosphorylation by pka promotes gsk-3beta-catalyzed tau phosphorylation at thr181, ser199, ser202, thr205, thr217, thr231, ser396 and ser422

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-60655	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
SIGNOR-171042	Ser579	NVKSKIGsTENLKHQ	Homo sapiens
pmid	sentence
21215781	Tau pseudophosphorylation at specific sites such as s262, s293, s324 and s356 was reported to induce tau conformational change and attenuate tau binding to microtubules (fischer et al., 2009). Then, newly soluble tau proteins are targeted by post-translational modifications that directly or indirectly alter tau conformation, promoting tau dimerization in an anti-parallel manner. Stable tau dimers form tau oligomers, which continue in the aggregation process

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-167294	Ser721	PVVSGDTsPRHLSNV	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
20679343	Alzheimer disease neurons are characterized by extraneuronal plaques formed by aggregated amyloid-? Peptide and by intraneuronal tangles composed of fibrillar aggregates of the microtubule-associated tau protein. Tau is mostly found in a hyperphosphorylated form in these tangleswe find that three residues can be phosphorylated (ser-396, ser-400, and ser-404) by gsk3?

Identifier	Residue	Sequence	Organism
SIGNOR-164655	Thr522	SSPGSPGtPGSRSRT	Homo sapiens
pmid	sentence
20308788	Abnormal hyperphosphorylation of tau appears to be crucial in neurofibrillary degeneration in alzheimer's disease (ad). Gsk-3beta phosphorylated tau at many sites, with ser199, thr205, and ser396 being the most favorable sites in cells.

Identifier	Residue	Sequence	Organism
SIGNOR-150364	Thr534	SRTPSLPtPPTREPK	Homo sapiens
pmid	sentence
17078951	Here, we found that prephosphorylation by pka promotes gsk-3beta-catalyzed tau phosphorylation at thr181, ser199, ser202, thr205, thr217, thr231, ser396 and ser422

Identifier	Residue	Sequence	Organism
SIGNOR-171046	Thr548	KKVAVVRtPPKSPSS	Homo sapiens
pmid	sentence
21215781	Gsk3b phosphorylates tau at t231tau phosphorylation at t231, s235 and s262 also contributes to the dissociation of tau from microtubules

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-255486
pmid	sentence
21443865	The MAPT H1 haplotype and subhaplotypes may be associated with sporadic tauopathies including AD. And that, tau's phosphorylation is regulated by many protein kinases, including glycogen synthase kinase 3beta (GSK3B).

Publications:

11

Organism:

Homo Sapiens,

Tissue:

Brain

Pathways:

Insulin Signaling, MTOR Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-181541	Ser404	SMRPDVSsPPSSSST	Homo sapiens
pmid	sentence
18838540	We found hormone-dependent GR phosphorylation on serine 404 by GSK-3beta [ ]Cells expressing a GR that is incapable of GSK-3beta phosphorylation had a redirection of the global transcriptional response to hormone, including the activation of additional signaling pathways, in part due to the altered ability of unphosphorylatable GR to recruit transcriptional cofactors CBP/p300 and the p65 (RelA) subunit of NF-kappaB

Publications:

1

Organism:

Homo Sapiens

Pathways:

Adipogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-275967	Ser405	QARAHGLsLIPSTGL	in vitro
pmid	sentence
10587587	Here, we show that Ser298, which locates downstream of the bHLHZip and was previously found to be mutated in individuals with WS2, plays an important role in MITF function. Glycogen synthase kinase 3 (GSK3) was found to phosphorylate Ser298 in vitro, thereby enhancing the binding of MITF to the tyrosinase promoter.

Identifier	Residue	Organism	Cell Line
SIGNOR-276356		Homo sapiens	T-98G Cell
pmid	sentence
21873430	Both MITF and USF1 were activated by glycogen synthase kinase (GSK) 3, with GSK3 phosphorylation sites on USF1 identified as the previously described activating site threonine 153 as well as serine 186.

Publications:

2

Organism:

In Vitro, Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276270	Ser427	ALERFDHsPTPSASS	Homo sapiens	HEK-293T Cell
pmid	sentence
19946213	We have identified a conserved cluster of serines that include, Ser431, which is a prerequisite phosphorylation site for the generation of BMAL dependent phospho-primed CLOCK and for the potential GSK-3 phosphorylation at Ser427.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236645	Ser430	DTLTPPPsDAGSPFQ	Homo sapiens	HeLa Cell
pmid	sentence
16825193	The transcription factor SREBP1 is degraded by the ubiquitin-proteasome system following phosphorylation of Thr426 and Ser430 in its phosphodegron. We now demonstrate that the glycogen synthase kinase (GSK)-3beta-dependent phosphorylation of these residues in SREBP1 is enhanced in response to specific DNA binding

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236030	Ser430	DTLTPPPsDAGSPFQ	Homo sapiens	HEK-293 Cell
pmid	sentence
19126544	Importantly, we demonstrate that the mature form of endogenous SREBP1 is phosphorylated on Ser-434. Glycogen synthase kinase-3 phosphorylates Ser-434, and the phosphorylation of this residue is attenuated in response to insulin signaling. Interestingly, phosphorylation of Ser-434 promotes the glycogen synthase kinase-3-dependent phosphorylation of Thr-426 and Ser-430 and destabilizes SREBP1.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235797	Ser434	PPPSDAGsPFQSSPL	Homo sapiens	HEK-293 Cell
pmid	sentence
19126544	Importantly, we demonstrate that the mature form of endogenous SREBP1 is phosphorylated on Ser-434. Glycogen synthase kinase-3 phosphorylates Ser-434, and the phosphorylation of this residue is attenuated in response to insulin signaling. Interestingly, phosphorylation of Ser-434 promotes the glycogen synthase kinase-3-dependent phosphorylation of Thr-426 and Ser-430 and destabilizes SREBP1.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236649	Thr426	TEVEDTLtPPPSDAG	Homo sapiens	HeLa Cell
pmid	sentence
16825193	The transcription factor SREBP1 is degraded by the ubiquitin-proteasome system following phosphorylation of Thr426 and Ser430 in its phosphodegron. We now demonstrate that the glycogen synthase kinase (GSK)-3beta-dependent phosphorylation of these residues in SREBP1 is enhanced in response to specific DNA binding

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236667	Thr426	TEVEDTLtPPPSDAG	Homo sapiens	HEK-293 Cell
pmid	sentence
19126544	Importantly, we demonstrate that the mature form of endogenous SREBP1 is phosphorylated on Ser-434. Glycogen synthase kinase-3 phosphorylates Ser-434, and the phosphorylation of this residue is attenuated in response to insulin signaling. Interestingly, phosphorylation of Ser-434 promotes the glycogen synthase kinase-3-dependent phosphorylation of Thr-426 and Ser-430 and destabilizes SREBP1.

Publications:

5

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251245	Ser451	NGFYHFGsTSSSPPI	Homo sapiens	HEK-293 Cell
pmid	sentence
16141410	In vitro and in vivo (HEK 293 cells) kinase assays with synthetic peptides and full-length myocardin demonstrated that myocardin was a primed GSK3beta substrate, with serines 455 to 467 and 624 to 636 being the major GSK3beta phosphorylation sites. GSK3β phosphorylation at the sites identified inhibits myocardin intrinsic transcriptional activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251244	Ser455	HFGSTSSsPPISPAS	Homo sapiens	HEK-293 Cell
pmid	sentence
16141410	In vitro and in vivo (HEK 293 cells) kinase assays with synthetic peptides and full-length myocardin demonstrated that myocardin was a primed GSK3beta substrate, with serines 455 to 467 and 624 to 636 being the major GSK3beta phosphorylation sites. GSK3β phosphorylation at the sites identified inhibits myocardin intrinsic transcriptional activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251243	Ser459	TSSSPPIsPASSDLS	Homo sapiens	HEK-293 Cell
pmid	sentence
16141410	In vitro and in vivo (HEK 293 cells) kinase assays with synthetic peptides and full-length myocardin demonstrated that myocardin was a primed GSK3beta substrate, with serines 455 to 467 and 624 to 636 being the major GSK3beta phosphorylation sites. GSK3β phosphorylation at the sites identified inhibits myocardin intrinsic transcriptional activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251246	Ser463	PPISPASsDLSVAGS	Homo sapiens	HEK-293 Cell
pmid	sentence
16141410	In vitro and in vivo (HEK 293 cells) kinase assays with synthetic peptides and full-length myocardin demonstrated that myocardin was a primed GSK3beta substrate, with serines 455 to 467 and 624 to 636 being the major GSK3beta phosphorylation sites. GSK3β phosphorylation at the sites identified inhibits myocardin intrinsic transcriptional activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251247	Ser626	DQTNVLSsTFLSPQC	Homo sapiens	HEK-293 Cell
pmid	sentence
16141410	In vitro and in vivo (HEK 293 cells) kinase assays with synthetic peptides and full-length myocardin demonstrated that myocardin was a primed GSK3beta substrate, with serines 455 to 467 and 624 to 636 being the major GSK3beta phosphorylation sites. GSK3β phosphorylation at the sites identified inhibits myocardin intrinsic transcriptional activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251248	Ser630	VLSSTFLsPQCSPQH	Homo sapiens	HEK-293 Cell
pmid	sentence
16141410	In vitro and in vivo (HEK 293 cells) kinase assays with synthetic peptides and full-length myocardin demonstrated that myocardin was a primed GSK3beta substrate, with serines 455 to 467 and 624 to 636 being the major GSK3beta phosphorylation sites. GSK3β phosphorylation at the sites identified inhibits myocardin intrinsic transcriptional activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251249	Ser634	TFLSPQCsPQHSPLG	Homo sapiens	HEK-293 Cell
pmid	sentence
16141410	In vitro and in vivo (HEK 293 cells) kinase assays with synthetic peptides and full-length myocardin demonstrated that myocardin was a primed GSK3beta substrate, with serines 455 to 467 and 624 to 636 being the major GSK3beta phosphorylation sites. GSK3β phosphorylation at the sites identified inhibits myocardin intrinsic transcriptional activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251250	Ser638	PQCSPQHsPLGAVKS	Homo sapiens	HEK-293 Cell
pmid	sentence
16141410	In vitro and in vivo (HEK 293 cells) kinase assays with synthetic peptides and full-length myocardin demonstrated that myocardin was a primed GSK3beta substrate, with serines 455 to 467 and 624 to 636 being the major GSK3beta phosphorylation sites. GSK3β phosphorylation at the sites identified inhibits myocardin intrinsic transcriptional activity

Publications:

8

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-251218	Ser451	STSTPAPsRTASFSE
pmid	sentence
10653665	Thr 446 and Ser 450, which are phosphorylated by glycogen synthase kinase-3 (GSK-3)

Identifier	Residue	Sequence
SIGNOR-251219	Thr447	NASGSTStPAPSRTA
pmid	sentence
10653665	Thr 446 and Ser 450, which are phosphorylated by glycogen synthase kinase-3 (GSK-3). Phosphorylation resulted in a 6-fold increase in V(max) and the conversion of citrate dependence from sigmoidal, displaying negative cooperativity, to hyperbolic.

Publications:

2

Identifier	Residue	Sequence	Organism
SIGNOR-151422	Ser468	AVFTDLAsVDNSEFQ	Homo sapiens
pmid	sentence
17183360	Rela is phosphorylated at: ser276 by the catalytic subunit of protein kinase a (pkac), msk1 and msk2; at ser311 by the atypical pkczeta; at ser468 by ikkbeta, ikkepsilon and glycogen-synthase kinase-3beta (gsk3beta); at ser529 by ck2; and at ser536 by ikkbeta, ikkalfa, ikkepsilon, nf-kb activating kinase (nak, also known as tank-binding kinase-1 tbk1)) and rsk1 (also known as p90 ribosomal protein s6 kinase (p90s6k) .

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-143581	Ser468	AVFTDLAsVDNSEFQ	Homo sapiens	T-lymphocyte
pmid	sentence
16407239	Rela is phosphorylated at: ser276 by the catalytic subunit of protein kinase a (pkac), msk1 and msk2; at ser311 by the atypical pkczeta; at ser468 by ikkbeta, ikkepsilon and glycogen-synthase kinase-3beta (gsk3beta); at ser529 by ck2; and at ser536 by ikkbeta, ikkalfa, ikkepsilon, nf-kb activating kinase (nak, also known as tank-binding kinase-1 tbk1)) and rsk1 (also known as p90 ribosomal protein s6 kinase (p90s6k) .

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-251221	Ser486	LRTPGRQsPGPGHRS	Homo sapiens
pmid	sentence
10581160	Axin residues T609 and S614 are physiological GSK3beta targets. Axin phosphorylation in the regulation of b-catenin stability. When active (left), GSK3b phosphorylates Axin as well as APC and b-catenin. The phosphorylated form of Axin binds strongly to b-catenin and promotes the phosphorylation of b-catenin by GSK3b, leading to strong interaction with b-TrCP

Identifier	Residue	Sequence	Organism
SIGNOR-251222	Thr481	HVQRVLRtPGRQSPG	Homo sapiens
pmid	sentence
10581160	Axin residues T609 and S614 are physiological GSK3beta targets. Axin phosphorylation in the regulation of b-catenin stability. When active (left), GSK3b phosphorylates Axin as well as APC and b-catenin. The phosphorylated form of Axin binds strongly to b-catenin and promotes the phosphorylation of b-catenin by GSK3b, leading to strong interaction with b-TrCP

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-159442	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
SIGNOR-159446	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
SIGNOR-159450	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
SIGNOR-159454	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

Identifier	Residue	Sequence	Organism
SIGNOR-159458	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
SIGNOR-159462	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
SIGNOR-159466	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
SIGNOR-159470	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

Identifier	Residue	Sequence	Organism
SIGNOR-90668	Ser503	GGEEETKsPPAEEAA	Homo sapiens
pmid	sentence
12130654	Gsk3beta was shown to phosphorylate at ser-493 in vitro by phosphopeptide mapping and site-directed mutagenesis, and in vivo in hek293 cells. The role of ser-493 phosphorylation is also a question to be addressed in the future. Because the e-segment appears to be involved in filament formation (27, 42), phosphorylation in that region may also play a regulatory role in filament formation. Secondary structure prediction suggests that phosphorylation of ser-493 in combination with following the pro residue interrupts _-helix of the e-segment

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249353	Ser512	PPKSGDRsGYSSPGS	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
9771888	Sequencing of 32P-labeled trypsin phosphopeptides from tau prephosphorylated by A-kinase (using unlabeled ATP) and further phosphorylated by GSK-3 in the presence of [gamma-32P]ATP revealed that Ser-195, Ser-198, Ser-199, Ser-202, Thr-205, Thr-231, Ser-235, Ser-262, Ser-356 and Ser-404 are phosphorylated, whereas if tau is not prephosphorylated by A-kinase, GSK-3 phosphorylates it at Thr-181, Ser-184, Ser-262, Ser-356 and Ser-400. These data suggest that (i) prephosphorylation of tau by A-kinase makes additional and different sites accessible for phosphorylation by GSK-3; (ii) phosphorylation of tau at these additional sites further inhibits the biological activity of tau in its ability to bind to microtubules and promote microtubule assembly.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249354	Ser515	SGDRSGYsSPGSPGT	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
9832145	Sequencing of 32P-labeled trypsin phosphopeptides from tau prephosphorylated by A-kinase (using unlabeled ATP) and further phosphorylated by GSK-3 in the presence of [gamma-32P]ATP revealed that Ser-195, Ser-198, Ser-199, Ser-202, Thr-205, Thr-231, Ser-235, Ser-262, Ser-356 and Ser-404 are phosphorylated, whereas if tau is not prephosphorylated by A-kinase, GSK-3 phosphorylates it at Thr-181, Ser-184, Ser-262, Ser-356 and Ser-400. These data suggest that (i) prephosphorylation of tau by A-kinase makes additional and different sites accessible for phosphorylation by GSK-3; (ii) phosphorylation of tau at these additional sites further inhibits the biological activity of tau in its ability to bind to microtubules and promote microtubule assembly.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249352	Ser516	GDRSGYSsPGSPGTP	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
12387894	We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249343	Ser519	SGYSSPGsPGTPGSR	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
12387894	We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249344	Ser531	GSRSRTPsLPTPPTR	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
12387894	We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249345	Ser713	GAEIVYKsPVVSGDT	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
12387894	We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249355	Ser717	VYKSPVVsGDTSPRH	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
12387894	Sequencing of 32P-labeled trypsin phosphopeptides from tau prephosphorylated by A-kinase (using unlabeled ATP) and further phosphorylated by GSK-3 in the presence of [gamma-32P]ATP revealed that Ser-195, Ser-198, Ser-199, Ser-202, Thr-205, Thr-231, Ser-235, Ser-262, Ser-356 and Ser-404 are phosphorylated, whereas if tau is not prephosphorylated by A-kinase, GSK-3 phosphorylates it at Thr-181, Ser-184, Ser-262, Ser-356 and Ser-400. These data suggest that (i) prephosphorylation of tau by A-kinase makes additional and different sites accessible for phosphorylation by GSK-3; (ii) phosphorylation of tau at these additional sites further inhibits the biological activity of tau in its ability to bind to microtubules and promote microtubule assembly.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249346	Ser721	PVVSGDTsPRHLSNV	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
12387894	We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249351	Thr498	KTPPAPKtPPSSGEP	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
12387894	We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249347	Thr522	SSPGSPGtPGSRSRT	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
12387894	We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249348	Thr529	TPGSRSRtPSLPTPP	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
12387894	We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249349	Thr534	SRTPSLPtPPTREPK	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
12387894	We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249350	Thr548	KKVAVVRtPPKSPSS	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
12387894	We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235.

Publications:

13

Organism:

Homo Sapiens

Pathways:

Insulin Signaling, PI3K/AKT Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-133251	Ser518	KTVTPASsAKTSPAK	Rattus norvegicus	Neuron
pmid	sentence
15652488	Ser-518 is also a potential phosphorylation site of CRMP-2 by GSK-3_.

Identifier	Residue	Sequence	Organism
SIGNOR-264839	Thr509	PVCEVSVtPKTVTPA	Homo sapiens
pmid	sentence
25040932	Cdk5 and DYRK2 phosphorylate CRMP2 and CRMP4, respectively, priming these proteins at S522 before their subsequent phosphorylation by GSK-3b at T509, T516 and S518\|e CRMP2 phosphorylation by GSK-3b disrupts its interaction with tubulin (Yamashita & Goshima, 2012), leading to growth inhibition

Identifier	Residue	Sequence	Organism
SIGNOR-264840	Thr514	SVTPKTVtPASSAKT	Homo sapiens
pmid	sentence
25040932	Cdk5 and DYRK2 phosphorylate CRMP2 and CRMP4, respectively, priming these proteins at S522 before their subsequent phosphorylation by GSK-3b at T509, T516 and S518\|e CRMP2 phosphorylation by GSK-3b disrupts its interaction with tubulin (Yamashita & Goshima, 2012), leading to growth inhibition

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-133255	Thr514	SVTPKTVtPASSAKT	Rattus norvegicus	Neuron
pmid	sentence
15652488	Here, we showed that glycogen synthase kinase-3beta (gsk-3beta) phosphorylated crmp-2 at thr-514 and inactivated it

Publications:

4

Organism:

Rattus Norvegicus, Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-145991	Ser518	KYATPAPsAKSSPSK	Homo sapiens	Neuron
pmid	sentence
16611631	Using in vitro kinase assays and pharmacological inhibition of gsk3 as described above for crmp2 and crmp4, it was found that thr509 (and presumably ser518 and thr514) of human crmp1 is phosphorylated by gsk3, following priming of ser522 by cdk5

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-145995	Thr509	PVYEVPAtPKYATPA	Homo sapiens	Neuron
pmid	sentence
16611631	In summary, phosphorylation of thr509 of human crmp1 appears to be regulated by two mechanisms; direct phosphorylation by cdk5, or by priming of ser522 by cdk5 followed by sequential phosphorylation of ser518, thr514, and thr509 by gsk3.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-145999	Thr514	PATPKYAtPAPSAKS	Homo sapiens	Neuron
pmid	sentence
16611631	Using in vitro kinase assays and pharmacological inhibition of gsk3 as described above for crmp2 and crmp4, it was found that thr509 (and presumably ser518 and thr514) of human crmp1 is phosphorylated by gsk3, following priming of ser522 by cdk5

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-146003	Ser518	KGGTPAGsARGSPTR	Rattus norvegicus
pmid	sentence
16611631	Together, these results suggest that crmp4 is able to increase neurite formation and elongation in neurons, although not as potently as crmp2, and that this process is regulated by ser522/ser518/thr514/thr509 phosphorylation in both cases. We demonstrate that cdk5 primes crmp2 and crmp4 for subsequent phosphorylation by gsk3, whereas dyrk2, phosphorylates and primes only crmp4 in vitro

Identifier	Residue	Sequence	Organism
SIGNOR-146011	Thr509	PVFDLTTtPKGGTPA	Rattus norvegicus
pmid	sentence
16611631	Together, these results suggest that crmp4 is able to increase neurite formation and elongation in neurons, although not as potently as crmp2, and that this process is regulated by ser522/ser518/thr514/thr509 phosphorylation in both cases. We demonstrate that cdk5 primes crmp2 and crmp4 for subsequent phosphorylation by gsk3, whereas dyrk2, phosphorylates and primes only crmp4 in vitro

Identifier	Residue	Sequence	Organism
SIGNOR-146015	Thr514	TTTPKGGtPAGSARG	Rattus norvegicus
pmid	sentence
16611631	Together, these results suggest that crmp4 is able to increase neurite formation and elongation in neurons, although not as potently as crmp2, and that this process is regulated by ser522/ser518/thr514/thr509 phosphorylation in both cases. We demonstrate that cdk5 primes crmp2 and crmp4 for subsequent phosphorylation by gsk3, whereas dyrk2, phosphorylates and primes only crmp4 in vitro

Publications:

3

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-146007	Ser522	PAGSARGsPTRPNPP	Rattus norvegicus	Neuron
pmid	sentence
16611631	Primary rat cortical neurons were treated with purvalanol, a more potent inhibitor of cdk5 and dyrk2 than roscovitine (25). Phosphorylation was monitored using antibodies that specifically recognize crmp2 when phosphorylated at thr514/thr509, or crmp4 when phosphorylated at thr509. Loss of phosphorylation of ser522 will prevent subsequent phosphorylation of ser518/thr514/thr509 by gsk3. Together, these results suggest that crmp4 is able to increase neurite formation and elongation in neurons, although not as potently as crmp2, and that this process is regulated by ser522/ser518/thr514/thr509 phosphorylation in both cases. We demonstrate that cdk5 primes crmp2 and crmp4 for subsequent phosphorylation by gsk3, whereas dyrk2, phosphorylates and primes only crmp4 in vitro

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264825	Ser533	QGCSREAsRESSRDT	Chlorocebus aethiops	COS Cell
pmid	sentence
19638411	GSK-3beta directly phosphorylates CLASP2 at Ser533 and Ser537 within the region responsible for the IQGAP1 binding. Phosphorylation of CLASP2 results in the dissociation of CLASP2 from IQGAP1, EB1 and microtubules.\| CLASPs were originally identified as CLIP-170-interacting proteins and later found to be required for microtubule stabilisation at the cortical regions of epithelial cells

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264826	Ser537	REASRESsRDTSPVR	Chlorocebus aethiops	COS Cell
pmid	sentence
19638411	GSK-3beta directly phosphorylates CLASP2 at Ser533 and Ser537 within the region responsible for the IQGAP1 binding. Phosphorylation of CLASP2 results in the dissociation of CLASP2 from IQGAP1, EB1 and microtubules.\| CLASPs were originally identified as CLIP-170-interacting proteins and later found to be required for microtubule stabilisation at the cortical regions of epithelial cells

Publications:

2

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-251236	Ser535	ESEQSMDsEEPDSRG	in vitro
pmid	sentence
12133000	The largest (epsilon) subunit of eIF2B is a substrate for glycogen synthase kinase (GSK)-3 in vitro, and phosphorylation by GSK3 inhibits the activity of eIF2B. The site of phosphorylation has previously been identified as Ser(535).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251237	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:

2

Organism:

In Vitro, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-180022	Ser540	MDSEEPDsRGGSPQM	Homo sapiens
pmid	sentence
18701453	Gsk3_ phosphorylates eif2b_ at ser-539 (ser-535 in the rat sequence) and inactivates it

Identifier	Residue	Organism
SIGNOR-175621		Homo sapiens
pmid	sentence
21798082	Akt also promotes protein synthesis by phosphorylating and inactivating gsk3b, thus releasing the gsk3b-dependent inhibition of the eukariotic translation initiation factor 2b (eif2b).

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-144566	Ser55	CPTYFPPsPTGSLTQ	Homo sapiens
pmid	sentence
16484495	We show here that gsk3beta phosphorylates and stabilizes the orphan nuclear receptor rev-erbalpha, a negative component of the circadian clock.

Identifier	Residue	Sequence	Organism
SIGNOR-144570	Ser59	FPPSPTGsLTQDPAR	Homo sapiens
pmid	sentence
16484495	We show here that gsk3beta phosphorylates and stabilizes the orphan nuclear receptor rev-erbalpha, a negative component of the circadian clock.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-140609	Ser556	AQKSEGKsLPSSPSS	Homo sapiens
pmid	sentence
16174773	Synphilin-1 s556a mutant, which is less phosphorylated by gsk3beta, formed more inclusion bodies than wild type synphilin-1. Mutation analysis showed that ser556 is a major gsk3beta phosphorylation site in synphilin-1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276070	Ser571	RDTYSDRsGSSSPDS	Homo sapiens	HEK-293 Cell
pmid	sentence
17681942	Mutation of Ser-571 demonstrated that Ser-571 was the major site phosphorylated by GSK3 in intact human embryonic kidney 293 cells by GSK3 in vitro. Furthermore, mutation of Ser-575 prevented the phosphorylation of Ser-571, suggesting that phosphorylation of Ser-575 was necessary for priming the GSK3 phosphorylation of Ser-571. Incubation with an alkaline phosphatase increased CTPS1 activity in a time-dependent manner, demonstrating that phosphorylation inhibits CTPS1 activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276068	Ser574	YSDRSGSsSPDSEIT	Homo sapiens	HEK-293 Cell
pmid	sentence
17681942	We found that low serum conditions increased phosphorylation of endogenous CTPS1 and this phosphorylation was inhibited by the glycogen synthase kinase 3 (GSK3) inhibitor indirubin-3'-monoxime and GSK3beta short interfering RNAs, demonstrating the involvement of GSK3 in phosphorylation of endogenous human CTPS1. Separating tryptic peptides from [(32)P]orthophosphate-labeled cells and analyzing the phosphopeptides by mass spectrometry identified Ser-574 and Ser-575 as phosphorylated residues. Incubation with an alkaline phosphatase increased CTPS1 activity in a time-dependent manner, demonstrating that phosphorylation inhibits CTPS1 activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276069	Ser575	SDRSGSSsPDSEITE	Homo sapiens	HEK-293 Cell
pmid	sentence
17681942	We found that low serum conditions increased phosphorylation of endogenous CTPS1 and this phosphorylation was inhibited by the glycogen synthase kinase 3 (GSK3) inhibitor indirubin-3'-monoxime and GSK3beta short interfering RNAs, demonstrating the involvement of GSK3 in phosphorylation of endogenous human CTPS1. Separating tryptic peptides from [(32)P]orthophosphate-labeled cells and analyzing the phosphopeptides by mass spectrometry identified Ser-574 and Ser-575 as phosphorylated residues. Incubation with an alkaline phosphatase increased CTPS1 activity in a time-dependent manner, demonstrating that phosphorylation inhibits CTPS1 activity.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262743	Ser585	SEPVAKEsTEASKEP	Homo sapiens	HeLa Cell
pmid	sentence
17139249	Therefore, at least Ser585 and Thr597 in BICD1 are important phosphorylation sites for BICD1 to exert its functions, and GSK-3β-dependent phosphorylation is required for the interaction of BICD1 with dynein.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262744	Thr597	KEPSPTKtPTISPVI	Homo sapiens	HeLa Cell
pmid	sentence
17139249	Therefore, at least Ser585 and Thr597 in BICD1 are important phosphorylation sites for BICD1 to exert its functions, and GSK-3β-dependent phosphorylation is required for the interaction of BICD1 with dynein.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276392	Ser6	sTPCSSMS	in vitro
pmid	sentence
22142472	GSK-3β phosphorylated STK38 on residues S6 and T7 in vitro, depending largely on a PKA-mediated priming phosphorylation of STK38 on residues S10 and S11, respectively. Our results indicate that that GSK-3β inhibits STK38's full activation, and suggest that STK38 activation is required to prevent cell death in response to oxidative stress.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-264882	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264890	Ser638	PRVDLHTsGEHSELV	Homo sapiens	Colorectal Cancer Cell
pmid	sentence
29179460	GSK-3beta phosphorylation-dependent degradation of ZNF281 by beta-TrCP2 suppresses colorectal cancer progression\|

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264884	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-264885	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

Identifier	Residue	Sequence	Organism
SIGNOR-235793	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

Identifier	Residue	Sequence
SIGNOR-251239	Ser641	YRYPRPAsVPPSPSL
pmid	sentence
11427888	Glycogen synthase has multiple serines (residues 640, 644, 648 and 652) separated by three residues, and those Ser residues are phosphorylated sequentially by GSK3 from the C-terminal end after Ser 656 has been phosphorylated by casein kinase II.

Identifier	Residue	Sequence	Organism
SIGNOR-253005	Ser641	YRYPRPAsVPPSPSL	in vitro
pmid	sentence
6772446	Glycogen synthase kinase-3 phosphorylates three serine residues on glycogen synthase (sites 3a, 3b and 3c) which are all located in the same nine-amino-acid segment of the polypeptide chain. The sequence in this region is: Arg-Tyr-Pro-Arg-Pro-Ala-Ser(P)-Val-Pro-Pro-Ser(P)-Pro-Ser-Leu-Ser(P)-Arg-.

Identifier	Residue	Sequence
SIGNOR-251238	Ser645	RPASVPPsPSLSRHS
pmid	sentence
11427888	Glycogen synthase has multiple serines (residues 640, 644, 648 and 652) separated by three residues, and those Ser residues are phosphorylated sequentially by GSK3 from the C-terminal end after Ser 656 has been phosphorylated by casein kinase II.

Identifier	Residue	Sequence	Organism
SIGNOR-253006	Ser645	RPASVPPsPSLSRHS	in vitro
pmid	sentence
6772446	Glycogen synthase kinase-3 phosphorylates three serine residues on glycogen synthase (sites 3a, 3b and 3c) which are all located in the same nine-amino-acid segment of the polypeptide chain. The sequence in this region is: Arg-Tyr-Pro-Arg-Pro-Ala-Ser(P)-Val-Pro-Pro-Ser(P)-Pro-Ser-Leu-Ser(P)-Arg-.

Identifier	Residue	Sequence	Organism
SIGNOR-253007	Ser649	VPPSPSLsRHSSPHQ	in vitro
pmid	sentence
6772446	Glycogen synthase kinase-3 phosphorylates three serine residues on glycogen synthase (sites 3a, 3b and 3c) which are all located in the same nine-amino-acid segment of the polypeptide chain. The sequence in this region is: Arg-Tyr-Pro-Arg-Pro-Ala-Ser(P)-Val-Pro-Pro-Ser(P)-Pro-Ser-Leu-Ser(P)-Arg-.

Identifier	Residue	Sequence
SIGNOR-251240	Ser649	VPPSPSLsRHSSPHQ
pmid	sentence
11427888	Glycogen synthase has multiple serines (residues 640, 644, 648 and 652) separated by three residues, and those Ser residues are phosphorylated sequentially by GSK3 from the C-terminal end after Ser 656 has been phosphorylated by casein kinase II.

Identifier	Residue	Sequence
SIGNOR-251241	Ser653	PSLSRHSsPHQSEDE
pmid	sentence
11427888	Glycogen synthase has multiple serines (residues 640, 644, 648 and 652) separated by three residues, and those Ser residues are phosphorylated sequentially by GSK3 from the C-terminal end after Ser 656 has been phosphorylated by casein kinase II.

Publications:

8

Organism:

Homo Sapiens, , In Vitro

Tissue:

Muscle, Skeletal Muscle

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-276430	Ser693	LVGQLYKsSLLDDLL	in vitro
pmid	sentence
23185298	After identifying Ser693 as a GSK3beta phosphorylation site, we also determined that K679 is crucial for GSK3beta-binding, which strongly suggests that Drp1 is a novel substrate for GSK3beta. Our results suggest that GSK3beta-mediated phosphorylation at Ser693 does cause a dramatic decrease of GTPase activity; in contrast, GSK3beta-mediated phosphorylation at Ser693 appears not to affect Drp1 inter-/intra-molecular interactions.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264426	Ser7222	FRSRGRRsKPSSRAA	Homo sapiens	Hair Follicle Bulge Stem Cell
pmid	sentence
21295697	We discovered that GSK3β, a kinase inhibited by Wnt signaling, directly phosphorylates ACF7, a > 500 kDa microtubule-actin crosslinking protein abundant in hair follicle stem cells (HF-SCs). We map ACF7's GSK3β sites to the microtubule-binding domain and show that phosphorylation uncouples ACF7 from microtubules.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264428	Ser7230	KPSSRAAsPTRSSSS	Homo sapiens	Hair Follicle Bulge Stem Cell
pmid	sentence
21295697	We discovered that GSK3β, a kinase inhibited by Wnt signaling, directly phosphorylates ACF7, a > 500 kDa microtubule-actin crosslinking protein abundant in hair follicle stem cells (HF-SCs). We map ACF7's GSK3β sites to the microtubule-binding domain and show that phosphorylation uncouples ACF7 from microtubules.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264429	Ser7234	RAASPTRsSSSASQS	Homo sapiens	Hair Follicle Bulge Stem Cell
pmid	sentence
21295697	We discovered that GSK3β, a kinase inhibited by Wnt signaling, directly phosphorylates ACF7, a > 500 kDa microtubule-actin crosslinking protein abundant in hair follicle stem cells (HF-SCs). We map ACF7's GSK3β sites to the microtubule-binding domain and show that phosphorylation uncouples ACF7 from microtubules.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264430	Ser7310	ADPKKSAsRPGSRAG	Homo sapiens	Hair Follicle Bulge Stem Cell
pmid	sentence
21295697	We discovered that GSK3β, a kinase inhibited by Wnt signaling, directly phosphorylates ACF7, a > 500 kDa microtubule-actin crosslinking protein abundant in hair follicle stem cells (HF-SCs). We map ACF7's GSK3β sites to the microtubule-binding domain and show that phosphorylation uncouples ACF7 from microtubules.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264431	Ser7314	KSASRPGsRAGSRAG	Homo sapiens	Hair Follicle Bulge Stem Cell
pmid	sentence
21295697	We discovered that GSK3β, a kinase inhibited by Wnt signaling, directly phosphorylates ACF7, a > 500 kDa microtubule-actin crosslinking protein abundant in hair follicle stem cells (HF-SCs). We map ACF7's GSK3β sites to the microtubule-binding domain and show that phosphorylation uncouples ACF7 from microtubules.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264432	Ser7318	RPGSRAGsRAGSRAS	Homo sapiens	Hair Follicle Bulge Stem Cell
pmid	sentence
21295697	We discovered that GSK3β, a kinase inhibited by Wnt signaling, directly phosphorylates ACF7, a > 500 kDa microtubule-actin crosslinking protein abundant in hair follicle stem cells (HF-SCs). We map ACF7's GSK3β sites to the microtubule-binding domain and show that phosphorylation uncouples ACF7 from microtubules.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264433	Ser7322	RAGSRAGsRASSRRG	Homo sapiens	Hair Follicle Bulge Stem Cell
pmid	sentence
21295697	We discovered that GSK3β, a kinase inhibited by Wnt signaling, directly phosphorylates ACF7, a > 500 kDa microtubule-actin crosslinking protein abundant in hair follicle stem cells (HF-SCs). We map ACF7's GSK3β sites to the microtubule-binding domain and show that phosphorylation uncouples ACF7 from microtubules.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264434	Ser7326	RAGSRASsRRGSDAS	Homo sapiens	Hair Follicle Bulge Stem Cell
pmid	sentence
21295697	We discovered that GSK3β, a kinase inhibited by Wnt signaling, directly phosphorylates ACF7, a > 500 kDa microtubule-actin crosslinking protein abundant in hair follicle stem cells (HF-SCs). We map ACF7's GSK3β sites to the microtubule-binding domain and show that phosphorylation uncouples ACF7 from microtubules.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264435	Ser7330	RASSRRGsDASDFDL	Homo sapiens	Hair Follicle Bulge Stem Cell
pmid	sentence
21295697	We discovered that GSK3β, a kinase inhibited by Wnt signaling, directly phosphorylates ACF7, a > 500 kDa microtubule-actin crosslinking protein abundant in hair follicle stem cells (HF-SCs). We map ACF7's GSK3β sites to the microtubule-binding domain and show that phosphorylation uncouples ACF7 from microtubules.

Publications:

9

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-164742	Ser76	SNLQRMGsSESTDSG	Homo sapiens	HeLa Cell
pmid	sentence
20348946	Here, we report that casein kinase 1 alpha (ck1alpha) phosphorylates cdc25a on both s79 and s82 in a hierarchical manner requiring prior phosphorylation of s76 by chk1 or gsk-3beta. This facilitates beta-trcp binding and ubiquitin-mediated proteolysis of cdc25a

Publications:

1

Organism:

Homo Sapiens

Pathways:

Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism
SIGNOR-203657	Ser77	ADRLRAEsPSPPRLL	Homo sapiens
pmid	sentence
24425879	Here we show that gsk-3_ inactivates the proapoptotic activity of hlxb9 by phosphorylating hlxb9 at ser-78/ser-80 (phlxb9).

Identifier	Residue	Sequence	Organism
SIGNOR-203661	Ser79	RLRAESPsPPRLLAA	Homo sapiens
pmid	sentence
24425879	Here we show that gsk-3_ inactivates the proapoptotic activity of hlxb9 by phosphorylating hlxb9 at ser-78/ser-80 (phlxb9).

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276071	Ser789	VSAGPRPsPLPSPQP	Homo sapiens	HEK-293 Cell
pmid	sentence
17711861	The activation of MLK3 by GSK-3beta occurred via phosphorylation of MLK3 on two amino acid residues, Ser(789) and Ser(793), that are located within the C-terminal regulatory domain of MLK3.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276072	Ser793	PRPSPLPsPQPAPRR	Homo sapiens	HEK-293 Cell
pmid	sentence
17711861	The activation of MLK3 by GSK-3beta occurred via phosphorylation of MLK3 on two amino acid residues, Ser(789) and Ser(793), that are located within the C-terminal regulatory domain of MLK3.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-148472	Ser820	VSSAYTVsRRSSGIS	Homo sapiens	HEK-293 Cell
pmid	sentence
16611981	The degradation of Gli2 requires the phosphorylation of a cluster of numerous serine residues in its carboxyl terminus by protein kinase A and subsequently by casein kinase 1 and glycogen synthase kinase 3.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249589	Ser832	GISPYFSsRRSSEAS	Homo sapiens	HEK-293 Cell
pmid	sentence
16611981	The degradation of Gli2 requires the phosphorylation of a cluster of numerous serine residues in its carboxyl terminus by protein kinase A and subsequently by casein kinase 1 and glycogen synthase kinase 3.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249590	Ser863	DPISTDAsRRSSEAS	Homo sapiens	HEK-293 Cell
pmid	sentence
16611981	The degradation of Gli2 requires the phosphorylation of a cluster of numerous serine residues in its carboxyl terminus by protein kinase A and subsequently by casein kinase 1 and glycogen synthase kinase 3.

Publications:

3

Organism:

Homo Sapiens

Pathways:

Sonic Hedgehog

Identifier	Residue	Sequence	Organism
SIGNOR-116140	Ser83	DEGHSNSsPRHSEAA	Homo sapiens
pmid	sentence
11903055	In kinase assays pka phosphorylated ser-87 of hnrnp d, whereas glycogen synthase kinase-3 beta (gsk-3 beta) phosphorylated ser-83, but only if ser-87 had been pre-phosphorylated by pka. Phosphorylation of ser-87 enhanced, whereas phosphorylation of ser-83 repressed, transactivation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-102582	Ser83	DEGHSNSsPRHSEAA	Homo sapiens	Leukemia Cell
pmid	sentence
11903055	In kinase assays pka phosphorylated ser-87 of hnrnp d, whereas glycogen synthase kinase-3 beta (gsk-3 beta) phosphorylated ser-83, but only if ser-87 had been pre-phosphorylated by pka. Phosphorylation of ser-87 enhanced, whereas phosphorylation of ser-83 repressed, transactivation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251225	Ser847	SEAASLSsLNSSESD	in vitro
pmid	sentence
10671552	Phosphorylation of the E-cadherin Cytoplasmic Domain by CKII and GSK-3β Increases the Binding to β-catenin. pre-phosphorylation by CKII at Ser-855 and/or Ser-853 of E-cadherin is required before GSK-3β can phosphorylate at Ser-849.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-174049	Ser86	TKNGLPGsRPGSPER	Homo sapiens
pmid	sentence
21658600	We demonstrate that gsk-3 phosphorylates serine 86 of the p53-acetyltransferase tip60. A tip60(s86a) mutant was less active to induce p53 k120 acetylation, histone 4 acetylation, and expression of puma

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, AML_TRIPLETS, FLT3-ITD signaling, Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, Insulin Signaling, MTOR Signaling, Triple mutant AML, PI3K/AKT Signaling, WNT/FLT3

Identifier	Residue	Sequence	Organism
SIGNOR-169642	Ser864	PKPSSHHsGSGSTST	Homo sapiens
pmid	sentence
21078818	We identify ror2 ser 864 as a critical residue phosphorylated by gsk3 and required for noncanonical receptor activation by wnt5a, analogous to the priming phosphorylation of low-density receptor-related protein 6 (lrp6) in response to wnt3a.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-245428	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-242578	Ser9	SGRPRTTsFAESCKP	Homo sapiens	HEK-293 Cell
pmid	sentence
9373175	Evidence that the inhibition of glycogen synthase kinase-3_ by IGF-1 is mediated by PDK1/PKB-induced phosphorylation of Ser-9

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-245416	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 3beta (GSK3B). The AKT-mediated phosphorylation of glycogen synthase kinase 3b 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-252546	Ser9	SGRPRTTsFAESCKP	Homo sapiens	HEK-293 Cell
pmid	sentence
9373175	Evidence that the inhibition of glycogen synthase kinase-3beta by IGF-1 is mediated by PDK1/PKB-induced phosphorylation of Ser-9

Identifier	Residue	Organism
SIGNOR-255109		Homo sapiens
pmid	sentence
15829723	GSK-3beta activity can be inhibited by Akt phosphorylation (12), which may provide a mechanism for Akt to promote muscle growth through inhibition of the negative regulator GSK-3beta.

Publications:

3

Organism:

Homo Sapiens

Tissue:

Skeletal Muscle

Pathways:

Adipogenesis, FLT3-ITD signaling, IGF and Myogenesis

Identifier	Residue	Sequence
SIGNOR-264819	Ser9	SGRPRTTsFAESCKP
pmid	sentence
26088133	Interestingly, GSK3beta can be released from the multienzyme complex in response to PKA phosphorylation on serine 9, which suppresses GSK3beta activity.

Publications:

1

Pathways:

FLT3-ITD signaling, PI3K/AKT Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-148908	Ser9	SGRPRTTsFAESCKP	Homo sapiens	B-lymphocyte
pmid	sentence
16914735	Gckr can phosphorylate an n-terminal recombinant fusion protein of gsk3_ and enhance the in vivo phosphorylation of gsk3_ on serine 9reduction of gckr expression inhibits wnt3a-induced phosphorylation of gsk3_ at serine 9 and decreases the accumulation of cytosolic _-catenin.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-119889	Ser9	SGRPRTTsFAESCKP	Homo sapiens
pmid	sentence
14657655	Phospho-gsk3b-specific antibodies also revolved that lkb1 regulates gsk3b phosphorylation at a known inhibitory site, serine-9. This localized phosphorylation is cdc42 and pkc-zeta-dependent.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262524	Ser9	SGRPRTTsFAESCKP	Mus musculus	MEF Cell
pmid	sentence
28646232	We demonstrate that insulin-mediated activation of ERK1/2 results in phosphorylation of GSK3β at S9 independently of Akt/mTORC1 activity in Tsc2 null mouse embryonic fibroblasts. In addition, we show that inhibition of ERK1/2 rescues GSK3β activity and restores protein synthesis in Tsc2 −/− MEFs to normal levels

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262523	Ser9	SGRPRTTsFAESCKP	Mus musculus	MEF Cell
pmid	sentence
28646232	We demonstrate that insulin-mediated activation of ERK1/2 results in phosphorylation of GSK3β at S9 independently of Akt/mTORC1 activity in Tsc2 null mouse embryonic fibroblasts. In addition, we show that inhibition of ERK1/2 rescues GSK3β activity and restores protein synthesis in Tsc2 −/− MEFs to normal levels

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-188581	Ser9	SGRPRTTsFAESCKP	Homo sapiens	T-lymphocyte
pmid	sentence
19836308	Gsk3 is different from most kinases in that it is constitutively partially active and the most common regulatory mechanism is inhibition by phosphorylation of ser21 in gsk3_ or ser9 in gsk3_. This inhibitory phosphorylation can be mediated by several kinases, such as akt/protein kinase b (pkb), protein kinase c (pkc) and protein kinase a (pka).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249166	Ser9	SGRPRTTsFAESCKP	Homo sapiens	HEK-293 Cell
pmid	sentence
12054501	Human serum and glucocorticoid-inducible kinase-like kinase (SGKL) phosphorylates glycogen syntheses kinase 3 beta (GSK-3beta) at serine-9 through direct interaction

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249167	Ser9	SGRPRTTsFAESCKP	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:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252788	Ser9	SGRPRTTsFAESCKP	Homo sapiens
pmid	sentence
11584304	S6k then phosphorylates the same serine residue on gsk3 that is targeted by pkb/akt (fig. 1), thereby inhibiting its activity.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-188577	Ser9	SGRPRTTsFAESCKP	Homo sapiens	T-lymphocyte
pmid	sentence
19836308	Gsk3 is different from most kinases in that it is constitutively partially active and the most common regulatory mechanism is inhibition by phosphorylation of ser21 in gsk3alpha or ser9 in gsk3beta. This inhibitory phosphorylation can be mediated by several kinases, such as akt/protein kinase b (pkb), protein kinase c (pkc) and protein kinase a (pka).

Publications:

1

Organism:

Homo Sapiens

Pathways:

Sonic Hedgehog, WNT/FLT3

Identifier	Residue	Sequence
SIGNOR-275801	Ser9	SGRPRTTsFAESCKP
pmid	sentence
32396532	Moreover, RSK4 stabilized Beta-catenin in the presence of GSK-3Beta WT but not RSK4 stabilizes Beta-catenin through phosphorylation of GSK-3Beta (Ser9) in ESCC cells\|GSK-3Beta S9A in ESCC cells, which was similar to overexpression of GSK3Beta S9D\|

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-254754	Ser9	SGRPRTTsFAESCKP	Homo sapiens	HEK-293 Cell
pmid	sentence
20080667	DAB2IP interacts via its C2 domain with GSK3β, recruiting phosphatase PP2A for S9 de-phosphorylation and leading to GSK3β activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-188585	Ser9	SGRPRTTsFAESCKP	Homo sapiens
pmid	sentence
19836308	Gsk3 is different from most kinases in that it is constitutively partially active and the most common regulatory mechanism is inhibition by phosphorylation of ser21 in gsk3_ or ser9 in gsk3_. This inhibitory phosphorylation can be mediated by several kinases, such as akt/protein kinase b (pkb), protein kinase c (pkc) and protein kinase a (pka).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248345	Ser9	SGRPRTTsFAESCKP	Mus musculus
pmid	sentence
16959610	Epm2a-encoded laforin is a phosphatase for GSK-3beta and an important repressor in the Wnt signaling pathway\| only GSK-3β phosphorylation on Ser9 was affected by overexpression of laforin\|Although GSK-3β is inactivated by phosphorylation at the Ser9 position, it is unclear if the inactivated enzyme can be reactivated by dephosphorylation.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence
SIGNOR-264820	Ser9	SGRPRTTsFAESCKP
pmid	sentence
26088133	Anchored PP1 may relieve PKA-mediated inhibition of GSK3beta by dephosphorylating Ser-9, providing bi-directional control of AKAP220 complex formation in response to cAMP.

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262522	Ser9	SGRPRTTsFAESCKP	Mus musculus	MEF Cell
pmid	sentence
28646232	We demonstrate that insulin-mediated activation of ERK1/2 results in phosphorylation of GSK3β at S9 independently of Akt/mTORC1 activity in Tsc2 null mouse embryonic fibroblasts. In addition, we show that inhibition of ERK1/2 rescues GSK3β activity and restores protein synthesis in Tsc2 −/− MEFs to normal levels

Publications:

1

Organism:

Mus Musculus

Pathways:

Adipogenesis, Acute Myeloid Leukemia, AML_TRIPLETS, FLT3-ITD signaling, Insulin Signaling, MTOR Signaling, Triple mutant AML, PI3K/AKT Signaling, WNT/FLT3

Identifier	Residue	Sequence	Organism
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	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

Identifier	Residue	Sequence	Organism
SIGNOR-110917	Ser9	SGRPRTTsFAESCKP	Homo sapiens
pmid	sentence
11584304	S6k then phosphorylates the same serine residue on gsk3 that is targeted by pkb/akt (fig. 1), thereby inhibiting its activity.

Publications:

1

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling, MTOR Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251251	Ser903	KTTSQAHsLPLSPAS	Mus musculus	Fibroblast
pmid	sentence
12871932	GSK-3 beta forms an in vivo complex with and specifically phosphorylates NF-kappa B1/p105 at Ser-903 and Ser-907 in vitro. GSK-3 beta has a dual effect on p105: it stabilizes p105 under resting conditions and primes p105 for degradation upon tumor necrosis factor (TNF)-alpha treatment. Indeed, constitutive processing of p105 to p50 occurs at a higher rate in cells lacking GSK-3 beta with respect to wild-type cells and can be reduced upon reintroduction of GSK-3 beta by transfection. S903A and S907A point mutations impair p105 proteolysis in response to TNF-α.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251252	Ser907	QAHSLPLsPASTRQQ	Mus musculus	Fibroblast
pmid	sentence
12871932	GSK-3 beta forms an in vivo complex with and specifically phosphorylates NF-kappa B1/p105 at Ser-903 and Ser-907 in vitro. GSK-3 beta has a dual effect on p105: it stabilizes p105 under resting conditions and primes p105 for degradation upon tumor necrosis factor (TNF)-alpha treatment. Indeed, constitutive processing of p105 to p50 occurs at a higher rate in cells lacking GSK-3 beta with respect to wild-type cells and can be reduced upon reintroduction of GSK-3 beta by transfection. S903A and S907A point mutations impair p105 proteolysis in response to TNF-α.

Publications:

2

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-159574	Ser974	EESLAEMsIMTTELQ	Homo sapiens
pmid	sentence
18055457	Astrin acts as a substrate for gsk3beta and is phosphorylated at thr-111, thr-937 ((s/t)p motif) and ser-974/thr-978 ((s/t)xxx(s/t)-p motif;p is a phosphorylatable residue). Inhibition of gsk3beta impairs spindle and kinetochore accumulation of astrin and spindle formation at mitosis, suggesting that astrin association with the spindle microtubule and kinetochore may be dependent on phosphorylation by gsk3beta

Identifier	Residue	Sequence	Organism
SIGNOR-159578	Thr111	PIPQISStPKTSEEA	Homo sapiens
pmid	sentence
18055457	Astrin acts as a substrate for gsk3beta and is phosphorylated at thr-111, thr-937 ((s/t)p motif) and ser-974/thr-978 ((s/t)xxx(s/t)-p motif;p is a phosphorylatable residue). Inhibition of gsk3beta impairs spindle and kinetochore accumulation of astrin and spindle formation at mitosis, suggesting that astrin association with the spindle microtubule and kinetochore may be dependent on phosphorylation by gsk3beta

Identifier	Residue	Sequence	Organism
SIGNOR-159582	Thr937	ADEEPEStPVPLLGS	Homo sapiens
pmid	sentence
18055457	Astrin acts as a substrate for gsk3beta and is phosphorylated at thr-111, thr-937 ((s/t)p motif) and ser-974/thr-978 ((s/t)xxx(s/t)-p motif;p is a phosphorylatable residue). Inhibition of gsk3beta impairs spindle and kinetochore accumulation of astrin and spindle formation at mitosis, suggesting that astrin association with the spindle microtubule and kinetochore may be dependent on phosphorylation by gsk3beta

Identifier	Residue	Sequence	Organism
SIGNOR-159586	Thr978	AEMSIMTtELQSLCS	Homo sapiens
pmid	sentence
18055457	Astrin acts as a substrate for gsk3beta and is phosphorylated at thr-111, thr-937 ((s/t)p motif) and ser-974/thr-978 ((s/t)xxx(s/t)-p motif;p is a phosphorylatable residue). Inhibition of gsk3beta impairs spindle and kinetochore accumulation of astrin and spindle formation at mitosis, suggesting that astrin association with the spindle microtubule and kinetochore may be dependent on phosphorylation by gsk3beta

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-183325	Thr11	TAPAETAtPAPVEKS	Homo sapiens	HeLa Cell
pmid	sentence
19136008	We found that threonine 10 of h1.5 can be phosphorylated by glycogen synthase kinase-3 in vitro. We have generated an antiserum specific for human h1.5 phosphorylated at threonine 10. Immunofluorescence labeling of hela cells with this antiserum revealed that the phosphorylation at this site appears in prometaphase and disappears in telophase, and that this hyperphosphorylated form of h1.5 is mainly chromatin-bound in metaphase when chromatin condensation is maximal.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264816	Thr1136	AKEFAPAtPPSTPHN	Homo sapiens	HEK-293 Cell
pmid	sentence
26088133	A-kinase anchoring protein 220 (AKAP220) is a multivalent anchoring protein that can sequester a variety of signal transduction enzymes. These include protein kinase A (PKA) and glycogen synthase kinase 3beta (GSK3beta). Using a combination of molecular and cellular approaches we show that GSK3beta phosphorylation of Thr-1132 on AKAP220 initiates recruitment of this kinase into the enzyme scaffold. We also find that AKAP220 anchors GSK3beta and its substrate beta-catenin in membrane ruffles.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275763	Thr1938	HREKKEStPSTASLP	Rattus norvegicus	Neuron
pmid	sentence
29642012	In vivo genetic manipulations demonstrate that GSK3β and Nav1.6 are molecular determinants of MSN excitability and that silencing of GSK3β prevents maladaptive plasticity of IC MSNs. In vitro studies reveal direct interaction of GSK3β with Nav1.6 and phosphorylation at Nav1.6T1936 by GSK3β. A GSK3β-Nav1.6T1936 competing peptide reduces MSNs excitability in IC, but not EC rats. These results identify GSK3β regulation of Nav1.6 as a biosignature of MSNs maladaptive plasticity.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275748	Thr1966	TPEKTDMtPSTTSPP	Homo sapiens	Neuron
pmid	sentence
32599005	Glycogen synthase kinase 3β (GSK3beta) phosphorylates the Nav1.2C-terminal tail at T1966, suppressing Na+ currents and channel trafficking to the plasma membrane

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-123262	Thr2022	NIQENTQtPTVQEES	Homo sapiens	HEK-293 Cell
pmid	sentence
15005626	Gsk3 beta-dependent phosphorylation of the alpha nac coactivator regulates its nuclear translocation and proteasome-mediated degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251231	Thr226	HLQPGHPtPPPTPVP	Mus musculus	NIH-3T3 Cell
pmid	sentence
10567568	Glycogen synthase kinase 3 (GSK3) phosphorylates T222 and T226, causing a conformational change in C/EBPα. GSK3-mediated phosphorylation does not, in itself, dramatically alter the activity of C/EBPα in our assays. phosphorylation of C/EBPalpha and other substrates by GSK3 may be required for adipogenesis, since treatment of differentiating preadipocytes with lithium inhibits their conversion to adipocytes.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251232	Thr230	GHPTPPPtPVPSPHP	Mus musculus	NIH-3T3 Cell
pmid	sentence
10567568	Glycogen synthase kinase 3 (GSK3) phosphorylates T222 and T226, causing a conformational change in C/EBPα. GSK3-mediated phosphorylation does not, in itself, dramatically alter the activity of C/EBPα in our assays. phosphorylation of C/EBPalpha and other substrates by GSK3 may be required for adipogenesis, since treatment of differentiating preadipocytes with lithium inhibits their conversion to adipocytes.

Publications:

2

Organism:

Mus Musculus

Pathways:

Adipogenesis, Acute Myeloid Leukemia, AML_TRIPLETS, Triple mutant AML

Identifier	Residue	Sequence	Organism
SIGNOR-262698	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251644	Thr235	SSSSPPGtPSPADAK	Mus musculus	3T3-F442A Cell
pmid	sentence
22355693	We found that expression of srebf1a depended on GSK3β activity and that GSK3β activity was necessary for C/EBPβ phosphorylation at Thr188

Publications:

1

Organism:

Mus Musculus

Pathways:

Adipogenesis, Acute Myeloid Leukemia, FLT3-ITD signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-255828	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

Pathways:

Acute Myeloid Leukemia, AML_TRIPLETS, Triple mutant AML

Identifier	Residue	Sequence	Organism
SIGNOR-154668	Thr280	DELDQAStPTDVRDI	Homo sapiens
pmid	sentence
17486076	Glycogen synthase kinase-3beta and p38 phosphorylate cyclin d2 on thr280 to trigger its ubiquitin/proteasome-dependent degradation in hematopoietic cells

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-142880	Thr283	QGPSQTStPTDVTAI	Homo sapiens
pmid	sentence
16331257	We have previously shown that both basal and camp-induced degradation of cyclin d3 in reh cells is dependent on thr-283 phosphorylation by glycogen synthase kinase-3beta (gsk-3beta).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-62265	Thr286	EEVDLACtPTDVRDV	Homo sapiens
pmid	sentence
9832503	Phosphorylation of cyclin d1 on a single threonine residue near the carboxyl terminus (thr-286) positively regulates proteasomal degradation of d1. Now, we demonstrate that glycogen synthase kinase-3beta (gsk-3beta) phosphorylates cyclin d1 specifically on thr-286, thereby triggering rapid cyclin d1 turnover now, we demonstrate that glycogen synthase kinase-3beta (gsk-3beta) phosphorylates cyclin d1 specifically on thr-286, thereby triggering rapid cyclin d1 turnover.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-144818	Thr286	EEVDLACtPTDVRDV	Homo sapiens	Breast Cancer Cell
pmid	sentence
16504004	Phosphorylation of cyclin d1 on a single threonine residue near the carboxyl terminus (thr-286) positively regulates proteasomal degradation of d1. Now, we demonstrate that glycogen synthase kinase-3beta (gsk-3beta) phosphorylates cyclin d1 specifically on thr-286, thereby triggering rapid cyclin d1 turnover now, we demonstrate that glycogen synthase kinase-3beta (gsk-3beta) phosphorylates cyclin d1 specifically on thr-286, thereby triggering rapid cyclin d1 turnover.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-245437	Thr286	EEVDLACtPTDVRDV	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

Pathways:

Acute Myeloid Leukemia, AML_TRIPLETS, Triple mutant AML

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264851	Thr33	FYSSLNQtHTHTVLL	Homo sapiens	HEK-293 Cell
pmid	sentence
32937135	GSK-3beta phosphorylates FBXL21 and TCAP to activate FBXL21-mediated, phosphodegron-dependent TCAP degradation.\|These results show direct GSK-3beta phosphorylation of TCAP S157 and FBXL21 T33 sites.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-236641	Thr366	ASSSTSVtPDVSDNE	Homo sapiens
pmid	sentence
16107342	Gsk3beta Phosphorylates pten at thr-366 in intact cells phosphorylation of pten at thr-366 reduces the activity of pten in cells

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, Insulin Signaling, MTOR Signaling, PI3K/AKT Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-236026	Thr37	PPGDYSTtPGGTLFS	Homo sapiens
pmid	sentence
18701453	We found that gsk-3Beta phosphorylates and inactivates 4e-bp1, thereby increasing eif4e-dependent protein synthesis. upon stimulation, 4e-bp1 is phosphorylated on several threonine and serine residues, including thr-37/46 (36). This results in dissolution of the complex, freeing eif4e to bind with mrna cap to promote translation initiation.

Identifier	Residue	Sequence	Organism
SIGNOR-201699	Thr46	GGTLFSTtPGGTRII	Homo sapiens
pmid	sentence
23584478	Glycogen synthase kinase-3_ positively regulates protein synthesis and cell proliferation through the regulation of translation initiation factor 4E-binding protein 1We found that GSK-3_ phosphorylates and inactivates 4E-BP1, thereby increasing eIF4E-dependent protein synthesis.

Identifier	Residue	Sequence	Organism
SIGNOR-236660	Thr46	GGTLFSTtPGGTRII	Homo sapiens
pmid	sentence
18701453	We found that gsk-3Beta phosphorylates and inactivates 4e-bp1, thereby increasing eif4e-dependent protein synthesis. upon stimulation, 4e-bp1 is phosphorylated on several threonine and serine residues, including thr-37/46 (36). This results in dissolution of the complex, freeing eif4e to bind with mrna cap to promote translation initiation.

Publications:

3

Organism:

Homo Sapiens

Tissue:

Kidney

Pathways:

Insulin Signaling, MTOR Signaling, PI3K/AKT Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-118559	Thr395	PLPSGLLtPPQSGKK	Homo sapiens
pmid	sentence
14536078	Our experiments suggest that gsk3 is the kinase primarily responsible for phosphorylation of cyclin e on t380

Identifier	Residue	Sequence	Organism
SIGNOR-118563	Thr77	DPCSLIPtPDKEDDD	Homo sapiens
pmid	sentence
14536078	Our experiments suggest that gsk3 is the kinase primarily responsible for phosphorylation of cyclin e on t380

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-138898	Thr43	KVTTVVAtPGQGPDR	Homo sapiens	Breast Cancer Cell, Kidney Cancer Cell
pmid	sentence
16039586	Erk, which is activated by hbx, associates with gsk-3beta through a docking motif ((291)fkfp) of gsk-3beta and phosphorylates gsk-3beta at the (43)thr residue, which primes gsk-3beta for its subsequent phosphorylation at ser9 by p90rsk, resulting in inactivation of gsk-3beta and upregulation of beta-catenin.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-138894	Thr43	KVTTVVAtPGQGPDR	Homo sapiens	Breast Cancer Cell, Kidney Cancer Cell
pmid	sentence
16039586	Erk, which is activated by hbx, associates with gsk-3beta through a docking motif ((291)fkfp) of gsk-3beta and phosphorylates gsk-3beta at the (43)thr residue, which primes gsk-3beta for its subsequent phosphorylation at ser9 by p90rsk, resulting in inactivation of gsk-3beta and upregulation of beta-catenin.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264835	Thr516	TPLADTPtRPVTRHG	Homo sapiens	Neuron
pmid	sentence
25040932	The T516 phosphorylation was achieved by the glycogen synthase kinase-3beta (GSK-3beta), which can phosphorylate the wildtype protein but not the non-phosphorylatable mutant. Furthermore, we have shown that T516 phosphorylation is essential for the tubulin-binding property of CRMP5. Therefore, CRMP5-induced growth inhibition is dependent on T516 phosphorylation through the GSK-3beta pathway.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-118844	Thr58	KKFELLPtPPLSPSR	Homo sapiens
pmid	sentence
14563837	Conversely, overexpression of gsk-3 alpha or gsk-3 beta enhances thr-58 phosphorylation and ubiquitination of c-myc

Identifier	Residue	Sequence	Organism
SIGNOR-138603	Thr58	KKFELLPtPPLSPSR	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.

Identifier	Residue	Sequence	Organism
SIGNOR-252080	Thr58	KKFELLPtPPLSPSR	Rattus norvegicus
pmid	sentence
11018017	Phosphorylation of Thr 58, likely mediated by GSK-3 but dependent on the prior phosphorylation of Ser 62, is associated with degradation of Myc.

Publications:

3

Organism:

Homo Sapiens, Rattus Norvegicus

Pathways:

Acute Myeloid Leukemia, AML_TRIPLETS, FLT3-ITD signaling, Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, Triple mutant AML, WNT/FLT3

Identifier	Residue	Sequence	Organism
SIGNOR-261795	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

Identifier	Residue	Sequence	Organism
SIGNOR-160318	Thr66	NVNTKCItIPRSLDG	Homo sapiens
pmid	sentence
18172167	Mechanistically, axin facilitates gsk3-beta-mediated phosphorylation of smad3 at thr66, which triggers smad3 ubiquitination and degradation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Adipogenesis, Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276303	Thr67	KKKVERLtMQVSSLQ	Homo sapiens	HEK-293T Cell
pmid	sentence
21282377	These data suggest that the E3 ligase SCFFbxw7-α degrades p-DEK in a GSK-3β–dependent manner.Therefore, the phosphorylation of DEK by GSK-3β is a crucial step to mediate Tpm RNA splicing.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-168389	Thr687	PRGMGPGtPAGYGRG	Homo sapiens
pmid	sentence
20932480	We conclude that t687 is the primary site of threonine phosphorylation in psf. Gsk3 directly phosphorylates the splicing regulatory protein psf. In this phosphorylated form, psf is sequestered in a complex with trap150, precluding it from binding the ess1 sequence in cd45 alternatively spliced exons. Upon t?_Cell stimulation, reduced gsk3 activity leads to reduced psf phosphorylation, thereby releasing psf from trap150 and allowing it to participate in activation-induced cd45 exon skipping

Identifier	Residue	Organism
SIGNOR-168392		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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251257	Thr73	MKIDEPStPYHSMMG	Bos taurus	Brain
pmid	sentence
11320080	Protein phosphatase 1 (PP1) is complexed with inhibitor 2 (I-2) in the cytosol. In rabbit muscle extract PP1.I-2 is activated upon preincubation with ATP/Mg. This activation is caused by phosphorylation of I-2 on Thr(72) by glycogen synthase kinase 3 (GSK3).

Publications:

1

Organism:

Bos Taurus

Identifier	Residue	Sequence	Organism
SIGNOR-251220	Thr743	VEVDAAVtPEERHLS	in vitro
pmid	sentence
8764598	The sole site of phosphorylation in APPcyt by GSK-3beta was determined by phosphoamino acid analysis and phosphorylation of APPcyt mutant peptides to be Thr743 (numbering as for APP770).

Publications:

1

Organism:

In Vitro

Pathways:

Adipogenesis, Alzheimer, Acute Myeloid Leukemia, AML_TRIPLETS, FLT3-ITD signaling, Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, Sonic Hedgehog, Insulin Signaling, MTOR Signaling, IGF and Myogenesis, Triple mutant AML, PI3K/AKT Signaling, WNT/FLT3

Identifier	Residue	Sequence
SIGNOR-275528	Thr783	IAAPTHStLPTAHTC
pmid	sentence
27162139	These experiments suggested that GSK3beta phosphorylation of FIEL1 is required for PIAS4 targeting, and FIEL1 residues P779 and phosphorylated T783 are both required for PIAS4 interaction \|FIEL1 T783A mutant overexpression completely failed to decrease PIAS4 protein level.

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262879	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

Identifier	Residue	Sequence	Organism
SIGNOR-217865	Tyr216	RGEPNVSyICSRYYR	Homo sapiens
pmid	sentence
20331603	Phosphorylation of the residue Tyrosine in 216 position results in the constitutive activity of GSK-3beta and believed to be important target for signal transduction.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236564	Tyr216	RGEPNVSyICSRYYR	Homo sapiens	HEK-293 Cell
pmid	sentence
14570592	However, in the present study, we clearly demonstrate that GSK3_ is capable of catalysing the autophosphorylation of Tyr216 in vitro.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-236622	Tyr216	RGEPNVSyICSRYYR	Homo sapiens
pmid	sentence
15020233	In vitro kinase assay was carried out using a recombinant human active mek1 and we found that gsk-3beta was phosphorylated on tyr(216) by this kinase in a dose- and time-dependent manner. Further, the pretreatment of fibroblasts with u0126 inhibited serum-induced nuclear translocation of gsk-3beta. These results suggested that mek1/2 induces tyrosine phosphorylation of gsk-3beta and this cellular event might induce nuclear translocation of gsk-3beta.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Skin

Identifier	Residue	Sequence	Organism
SIGNOR-244780	Tyr216	RGEPNVSyICSRYYR	Homo sapiens
pmid	sentence
15020233	In vitro kinase assay was carried out using a recombinant human active mek1 and we found that gsk-3beta was phosphorylated on tyr(216) by this kinase in a dose- and time-dependent manner. Further, the pretreatment of fibroblasts with u0126 inhibited serum-induced nuclear translocation of gsk-3beta. These results suggested that mek1/2 induces tyrosine phosphorylation of gsk-3beta and this cellular event might induce nuclear translocation of gsk-3beta.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Skin

Pathways:

Adipogenesis, Acute Myeloid Leukemia, AML_TRIPLETS, FLT3-ITD signaling, Insulin Signaling, PI3K/AKT Signaling

Identifier	Residue	Organism
SIGNOR-193402		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-270059		Homo sapiens	Breast Cancer Cell, Kidney Cancer Cell
pmid	sentence
16039586	Erk, which is activated by hbx, associates with gsk-3beta through a docking motif ((291)fkfp) of gsk-3beta and phosphorylates gsk-3beta at the (43)thr residue, which primes gsk-3beta for its subsequent phosphorylation at ser9 by p90rsk, resulting in inactivation of gsk-3beta and upregulation of beta-catenin.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-58219		Homo sapiens
pmid	sentence
9635432	The frat family consists of three members: frat-1, -2, and -3. It has been shown that different sites of frat-1 interact with gsk-3 and dvl-1 and that wnt-1 disintegrates the complex formation of frat-1, dvl-1, and axin, resulting in the activation of the wnt signaling pathway

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-201683		Homo sapiens
pmid	sentence
23579495	Phosphorylation by GSK3 kept Axin activated (open) for _-catenin interaction and poised for engagement of LRP6.

Identifier	Residue	Organism
SIGNOR-67438		Homo sapiens
pmid	sentence
10318824	From the binding experiments, we defined the domains of Axin that bind glycogen synthase kinase-3beta (GSK-3beta) and beta-catenin. We also examined the ability of each Axin mutant to inhibit lymphoid enhancer factor-1 (Lef-1) reporter activity in a cell line expressing high levels of beta-catenin.

Identifier	Residue	Organism
SIGNOR-60046		Homo sapiens
pmid	sentence
9734785	Interaction with beta-catenin and GSK-3beta was required for the Axin-mediated beta-catenin reduction.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-264817		Homo sapiens	HEK-293 Cell
pmid	sentence
26088133	A-kinase anchoring protein 220 (AKAP220) is a multivalent anchoring protein that can sequester a variety of signal transduction enzymes. These include protein kinase A (PKA) and glycogen synthase kinase 3beta (GSK3beta). Using a combination of molecular and cellular approaches we show that GSK3beta phosphorylation of Thr-1132 on AKAP220 initiates recruitment of this kinase into the enzyme scaffold. We also find that AKAP220 anchors GSK3beta and its substrate beta-catenin in membrane ruffles.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-184696		Homo sapiens
pmid	sentence
19293931	In the absence of secreted wnt ligands, cytosolic beta-catenin is phosphorylated at ser45 by the priming kinase casein kinase 1 (ck1). Consequently, glycogen synthase kinase 3 (gsk3), in complex with axin and adenomatous polyposis coli (apc), phosphorylates beta-catenin at thr41, ser37, and ser33 apc cooperates with axin to promote the phosphorylation of b-catenin by gsk3 [which requires priming phosphorylation by casein kinase 1, alpha-isoform (ck1alpha)]

Identifier	Residue	Organism
SIGNOR-177233		Homo sapiens
pmid	sentence
22083140	In the absence of secreted wnt ligands, cytosolic beta-catenin is phosphorylated at ser45 by the priming kinase casein kinase 1 (ck1). Consequently, glycogen synthase kinase 3 (gsk3), in complex with axin and adenomatous polyposis coli (apc), phosphorylates beta-catenin at thr41, ser37, and ser33 apc cooperates with axin to promote the phosphorylation of b-catenin by gsk3 [which requires priming phosphorylation by casein kinase 1, alpha-isoform (ck1alpha)]

Publications:

2

Organism:

Homo Sapiens

Pathways:

WNT/FLT3

Identifier	Residue	Organism
SIGNOR-179784		Homo sapiens
pmid	sentence
15276472	Gsk3 was previously shown to directly phosphorylate the n-terminal regulatory domain of nfatc1, thus antagonizing the action of calcineurin and inhibiting nuclear shuttling of nfat.

Publications:

1

Organism:

Homo Sapiens

Pathways:

IGF and Myogenesis

Identifier	Residue	Organism
SIGNOR-261903		Homo sapiens
pmid	sentence
21821001	Our study also showed that a number of K562 cells survived despite the apoptotic stimuli. Within these surviving cells, galectin-3 was upregulated through newly synthesized protein. Notably, inducible galectin-3, which stabilized the pro-survival Bcl-2 family proteins Mcl-1, Bcl-xL, and Bcl-2, was essential for anti-apoptosis. Unpredictably, GSK-3β was critical for inducible galectin-3 expression as well as for cell survival. As summarized in Fig. 4C, we not only found inducible galectin-3 has an anti-apoptotic effect, but we also identified a GSK-3β-regulated mechanism for apoptotic resistance in K562 cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-187896		Homo sapiens
pmid	sentence
19740771	We found that gsk3beta inhibits maml1 transcriptional activity by directly targeting the n-terminal domain of maml1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-255110		Homo sapiens
pmid	sentence
15829723	GSK-3beta is a serine/threonine kinase that can block translation that is initiated by eukaryotic initiation factor-2B (24) and may thereby reduce protein synthesis.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Skeletal Muscle

Pathways:

Insulin Signaling, MTOR Signaling, PI3K/AKT Signaling

Identifier	Residue	Organism
SIGNOR-167957		Homo sapiens
pmid	sentence
20837657	In canonical wnt signaling, dsh phosphorylation inhibits the apcaxingsk3 complex, leading to beta-catenin stabilization.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, WNT/FLT3

Identifier	Residue	Organism
SIGNOR-159476		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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-255485
pmid	sentence
25309941	Following GSK3β activation, NF-κB is translocated from the cytoplasm to the nucleus and binds transcriptional sites with CBP leading to an increase in the transcription of pro-inflammatory cytokines (IL-1β, TNF-α, and IL-6).

Publications:

1

Pathways:

Acute Myeloid Leukemia, FLT3-ITD signaling

Identifier	Residue	Organism
SIGNOR-75366		Homo sapiens
pmid	sentence
10698523	Gsk-3beta-dependent phosphorylation of apc.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-175436		Homo sapiens
pmid	sentence
21798082	Akt also promotes protein synthesis by phosphorylating and inactivating gsk3b, thus releasing the gsk3b-dependent inhibition of the eukariotic translation initiation factor 2b (eif2b).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-79950		Homo sapiens
pmid	sentence
10911903	It has been found that a multiprotein complex assembled by the cytoplasmic component conductin induces degradation of cytoplasmic beta-catenin. The complex includes apc, the serine/threonine kinase gsk3 beta, and beta-catenin, which bind to conductin at distinct domains.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain, Kidney, Lung

Identifier	Residue	Organism	Cell Line
SIGNOR-262539		Homo sapiens	Pancreatic Cell Line
pmid	sentence
31562256	Indeed, we demonstrated that the selective GSK3 inhibitor LY2090314 significantly reduced cell proliferation in control pancreatic cancer cell lines

Publications:

1

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling, PI3K/AKT Signaling

Identifier	Residue	Organism
SIGNOR-148475		Mus musculus
pmid	sentence
16885213	Gli2 and Gli3 (in vertebrates) are phosphorylated by protein kinase A and glycogen synthase kinase-3_ and are proteolytically processed

Identifier	Residue	Organism
SIGNOR-219231		Drosophila melanogaster
pmid	sentence
11955435	We show that these phosphoserines prime further phosphorylation at adjacent Glycogen Synthase Kinase 3 (GSK3) and Casein Kinase I (CK1) sites. Alteration of the GSK3 or CK1 sites prevents Ci-155 proteolysis and activates Ci in the absence of Hedgehog.

Publications:

2

Organism:

Mus Musculus, Drosophila Melanogaster

Pathways:

Sonic Hedgehog

Identifier	Residue	Organism
SIGNOR-159473		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

Identifier	Residue	Organism
SIGNOR-175659		Homo sapiens
pmid	sentence
21798082	Gsk3b is able to phosphorylate nebulin at two ser sites in the c-terminal region of nebulin localized to the z-disk, thus preventing the interaction of nebulin with neuronal wiscott-aldrich syndrome protein (nwasp), a ubiquitously expressed member of the wasp family, which is involved in actin assembly.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-171892		Homo sapiens	HEK-293 Cell
pmid	sentence
21304492	Amer1 binds ck1gamma, recruits axin and gsk3beta to the plasma membrane and promotes complex formation between axin and lrp6.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-159438		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

Identifier	Residue	Organism
SIGNOR-169669		Homo sapiens
pmid	sentence
21078818	We demonstrate here that prototype canonical wnt3a and noncanonical wnt5a ligands specifically trigger completely unrelated endogenous coreceptors-lrp5/6 and ror1/2, respectively-through a common mechanism that involves their wnt-dependent coupling to the frizzled (fzd) coreceptor and recruitment of shared components, including dishevelled (dvl), axin, and glycogen synthase kinase 3 (gsk3)

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-159435		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

Identifier	Residue	Organism
SIGNOR-251607		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

Identifier	Residue	Organism
SIGNOR-263513		Homo sapiens
pmid	sentence
33081032	GSK3β regulates S6K1 activity positively through modulating phosphorylation of S6K1 at p.Ser371.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-255488
pmid	sentence
28712664	AKT phosphorylates and inhibits GSK3 in addition to many other substrates including TSC2, FOXO proteins, TBC1D4.

Publications:

1

Pathways:

Acute Myeloid Leukemia, AML_TRIPLETS, FLT3-ITD signaling, Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, Insulin Signaling, MTOR Signaling, Triple mutant AML, PI3K/AKT Signaling, WNT/FLT3

Identifier	Residue	Organism	Cell Line
SIGNOR-141783		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

Pathways:

Acute Myeloid Leukemia, FLT3-ITD signaling

Identifier	Residue	Organism
SIGNOR-90608		Homo sapiens
pmid	sentence
12123574	Here, we observed that gsk3beta was able to bind and phosphorylate notch1ic in vitro, and attenuation of gsk3beta activity reduced phosphorylation of notchic in vivo.Functionally, ligand-activated signaling through the endogenous notch1 receptor was reduced in gsk3beta fibroblasts, implying a positive role for gsk3beta in mammalian notch signaling.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism	Cell Line
SIGNOR-217430		Homo sapiens	T-lymphocyte
pmid	sentence
16407239	Rela is phosphorylated at: ser276 by the catalytic subunit of protein kinase a (pkac), msk1 and msk2; at ser311 by the atypical pkczeta; at ser468 by ikkbeta, ikkepsilon and glycogen-synthase kinase-3beta (gsk3beta); at ser529 by ck2; and at ser536 by ikkbeta, ikkalfa, ikkepsilon, nf-kb activating kinase (nak, also known as tank-binding kinase-1 tbk1)) and rsk1 (also known as p90 ribosomal protein s6 kinase (p90s6k) .

Identifier	Residue	Organism
SIGNOR-217367		Homo sapiens
pmid	sentence
17183360	Rela is phosphorylated at: ser276 by the catalytic subunit of protein kinase a (pkac), msk1 and msk2; at ser311 by the atypical pkczeta; at ser468 by ikkbeta, ikkepsilon and glycogen-synthase kinase-3beta (gsk3beta); at ser529 by ck2; and at ser536 by ikkbeta, ikkalfa, ikkepsilon, nf-kb activating kinase (nak, also known as tank-binding kinase-1 tbk1)) and rsk1 (also known as p90 ribosomal protein s6 kinase (p90s6k) .

Publications:

2

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3-ITD signaling

Identifier	Residue	Organism
SIGNOR-175475		Homo sapiens
pmid	sentence
21798082	Akt also promotes protein synthesis by phosphorylating and inactivating gsk3b, thus releasing the gsk3b-dependent inhibition of the eukariotic translation initiation factor 2b (eif2b).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-264843		Homo sapiens	Neuron
pmid	sentence
25040932	GSK-3beta phosphorylates MAP1B and the adenomatous polyposis coil gene product (APC; Grimes and Jope 2001; Frame and Cohen 2001). The phosphorylation of MAP1B by GSK-3beta suppresses detyrosination of microtubules and decreases the numbers of stable microtubules

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-262113		Homo sapiens	MHCC97-L Cell
pmid	sentence
PMC7642658	Importantly, we found that TDP-43 protein could interact with GSK3β mRNA and regulate the level of GSK3β protein translation. Taken together, our findings suggest that TDP-43 may activate the Wnt/β-catenin pathway by targeting the inhibition of GSK3β protein translation\|TDP-43 activates Wnt/β-catenin pathway probably by inhibiting the GSK3β protein translation. A. Interaction between TDP-43 protein and GSK3β mRNA was analyzed using RIP assay.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-251613		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

Identifier	Residue	Organism
SIGNOR-244030		in vitro
pmid	sentence
11738041	The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-245432		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

Pathways:

Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, IGF and Myogenesis

Identifier	Residue	Organism	Cell Line
SIGNOR-147451		Homo sapiens	Neuron
pmid	sentence
16815997	In the absence of wnt, macf1 associated with a complex that contained axin, betBeta-catenin, gsk3beta, and apc. Upon wnt stimulation, macf1 appeared to be involved in the translocation and subsequent binding of the axin complex to lrp6 at the cell membrane. Macf1 is involved in the translocation of the complex containing axin, Beta-catenin, and gsk3_ but not apc from the cytosol to the cell membrane, where axin and macf1 bind to lrp-5/6. Subsequently, gsk3_ is inactivated by phosphorylation, axin is degraded, and Beta-catenin is released and enters the nucleus, where it can activate the wnt-responsive genes.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-191000		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-157544		Homo sapiens
pmid	sentence
17726008	Here we show that similar to the interaction with traf4 and axin, the kinase domain of mekk4 interacts with the multifunctional serine/threonine kinase gsk3beta. Gsk3beta binding to mekk4 blocks mekk4 dimerization that is required for mekk4 activation, effectively inhibiting mekk4 stimulation of the jnk and p38 mapk pathways

Publications:

1

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling, Cell cycle: G2/M phase transition

Identifier	Residue	Organism
SIGNOR-207474		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-263050		Mus musculus
pmid	sentence
24260231	Involvement of GSK3 Inhibition by the PI3K/Akt Pathway in Regulation of Etoposide-induced Chk1 Activation. GSK3ß regulates etoposide-induced Chk1 activation. GSK3 inhibitors, including LiCl and SB216763, restored the sustained Chk1 activation and mitigated apoptosis in cells treated with etoposide and the inhibitors for aberrant kinases, PI3K, or Akt. Thus, proteasomal degradation of Chk1 as well as GSK3 activation may be involved in negative regulation of etoposide-induced Chk1 by imatinib in these cells.

Publications:

1

Organism:

Mus Musculus

Pathways:

Identifier	Residue	Organism
SIGNOR-175572		Homo sapiens
pmid	sentence
21798082	Akt also promotes protein synthesis by phosphorylating and inactivating gsk3b, thus releasing the gsk3b-dependent inhibition of the eukariotic translation initiation factor 2b (eif2b).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-255484
pmid	sentence
15229249	We speculate that DKK1 produced by βAP-treated neurons suppresses the canonical Wnt signaling pathway by interacting with LRP5/6 and therefore facilitates GSK3β activation.

Publications:

1

Pathways:

WNT/FLT3

Identifier	Residue	Organism
SIGNOR-159484		Homo sapiens
pmid	sentence
18045539	Phosphorylation at the gsk3 sites represses the transcriptional activity of smad1 by enhancing proteasomal degradation of psmad1cter

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-175520		Homo sapiens
pmid	sentence
21798082	Akt also promotes protein synthesis by phosphorylating and inactivating gsk3b, thus releasing the gsk3b-dependent inhibition of the eukariotic translation initiation factor 2b (eif2b).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-119892		Homo sapiens
pmid	sentence
14657655	Phospho-gsk3b-specific antibodies also revolved that lkb1 regulates gsk3b phosphorylation at a known inhibitory site, serine-9. This localized phosphorylation is cdc42 and pkc-zeta-dependent.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism	Cell Line
SIGNOR-149380		Rattus norvegicus	Rat-1 Cell
pmid	sentence
16959574	Gsk3 inhibits the mtor pathway by phosphorylating tsc2 in a manner dependent on ampk-priming phosphorylation.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Organism
SIGNOR-157541		Homo sapiens
pmid	sentence
17726008	Gsk3beta binding to mekk4 blocks mekk4 dimerization that is required for mekk4 activation, effectively inhibiting mekk4 stimulation of the jnk and p38 mapk pathways

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-254752		Homo sapiens	HEK-293 Cell
pmid	sentence
20080667	DAB2IP activates GSK-3β and antagonizes Wnt-mediated EMT. GSK-3β appears to directly associate with DAB2IP. Because DAB2IP is not a phosphatase, the mechanism of GSK-3β activation by DAB2IP is likely mediated by a separate phosphatase associated within this complex. PP2A is critical for DAB2IP-mediated GSK-3β activation and MET responses.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264874
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

Identifier	Residue	Organism	Cell Line
SIGNOR-251586		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: