Relation Results

Adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252549	Ser119	EILSRRPsYRKILND	Homo sapiens	HEK-293 Cell
pmid	sentence
9829964	When overexpressed in serum-stimulated cells, Akt/PKB potently induced Ser-133 phosphorylation of CREB and promoted recruitment of CBP. Correspondingly, Akt/PKB stimulated target gene expression via CREB in a phospho(Ser-133)-dependent manner.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence
SIGNOR-275666	Ser1194	GQRSRLAsMLDSDTE
pmid	sentence
23462102	Akt and PP2A reciprocally regulate the guanine nucleotide exchange factor Dock6 to control axon growth of sensory neurons\|At later developmental stages, the abundance of the kinase Akt increased, resulting in the binding of Akt to Dock6 and the phosphorylation of Dock6 at Ser(1194). \| In dorsal root ganglion neurons from mice lacking Dock6, reintroduction of Dock6 with a nonphosphorylatable S1194A mutation rescued axon extension but not branch number, whereas reintroduction of Dock6 with a phosphomimetic S1194E mutation resulted in premature branching

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-274059	Ser1255	CLTERAMsWQDRARQ	in vitro
pmid	sentence
27292631	We immunoprecipitated ectopically expressed wild-type KDM5A or KDM5Amut5A and performed an in vitro kinase assay using recombinant AKT1 in the presence or absence of AKT inhibition.Wild-type KDM5A is phosphorylated by AKT1 and this modification is sensitive to AKT inhibition, whereas KDM5Amut5A is not phosphorylated in the presence of AKT1 (Figure 3C).These results suggest that AKT-mediated KDM5A phosphorylation enhances KDM5A promoter recruitment.

Identifier	Residue	Sequence	Organism
SIGNOR-274060	Ser225	TRRVKTQsESGDVSR	in vitro
pmid	sentence
27292631	We immunoprecipitated ectopically expressed wild-type KDM5A or KDM5Amut5A and performed an in vitro kinase assay using recombinant AKT1 in the presence or absence of AKT inhibition.Wild-type KDM5A is phosphorylated by AKT1 and this modification is sensitive to AKT inhibition, whereas KDM5Amut5A is not phosphorylated in the presence of AKT1 (Figure 3C).These results suggest that AKT-mediated KDM5A phosphorylation enhances KDM5A promoter recruitment.

Identifier	Residue	Sequence	Organism
SIGNOR-274062	Ser287	RQRKGTLsVNFVDLY	in vitro
pmid	sentence
27292631	We immunoprecipitated ectopically expressed wild-type KDM5A or KDM5Amut5A and performed an in vitro kinase assay using recombinant AKT1 in the presence or absence of AKT inhibition.Wild-type KDM5A is phosphorylated by AKT1 and this modification is sensitive to AKT inhibition, whereas KDM5Amut5A is not phosphorylated in the presence of AKT1 (Figure 3C).These results suggest that AKT-mediated KDM5A phosphorylation enhances KDM5A promoter recruitment.

Identifier	Residue	Sequence	Organism
SIGNOR-274063	Thr1225	SRRPRLEtILSLLVS	in vitro
pmid	sentence
27292631	We immunoprecipitated ectopically expressed wild-type KDM5A or KDM5Amut5A and performed an in vitro kinase assay using recombinant AKT1 in the presence or absence of AKT inhibition.Wild-type KDM5A is phosphorylated by AKT1 and this modification is sensitive to AKT inhibition, whereas KDM5Amut5A is not phosphorylated in the presence of AKT1 (Figure 3C).These results suggest that AKT-mediated KDM5A phosphorylation enhances KDM5A promoter recruitment.

Identifier	Residue	Sequence	Organism
SIGNOR-274061	Thr285	QMRQRKGtLSVNFVD	in vitro
pmid	sentence
27292631	We immunoprecipitated ectopically expressed wild-type KDM5A or KDM5Amut5A and performed an in vitro kinase assay using recombinant AKT1 in the presence or absence of AKT inhibition.Wild-type KDM5A is phosphorylated by AKT1 and this modification is sensitive to AKT inhibition, whereas KDM5Amut5A is not phosphorylated in the presence of AKT1 (Figure 3C).These results suggest that AKT-mediated KDM5A phosphorylation enhances KDM5A promoter recruitment.

Publications:

5

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-252504	Ser126	VKRERTSsLTQFPPS	Homo sapiens
pmid	sentence
18280241	Akt regulates ranbp3 phosphorylation in vitro and in vivo

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252593	Ser127	PQHVRAHsSPASLQL	Homo sapiens
pmid	sentence
12535517	One protein that associates with 14-3-3 in an akt-dependent manner is shown here to be the yes-associated protein (yap), which is phosphorylated by akt at serine 127, leading to binding to 14-3-3. Akt promotes yap localization to the cytoplasm, resulting in loss from the nucleus where it functions as a coactivator of transcription factors including p73.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-135203	Ser129	SGSPSDNsGAEEMEV	Homo sapiens
pmid	sentence
15818404	Akt/pkb ser129 is phosphorylated by ck2 in vitro and in vivo;(4) such a phosphorylation of activated akt/pkb correlates with a further increase in catalytic activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252595	Ser129	SGSPSDNsGAEEMEV	Homo sapiens	HEK-293 Cell
pmid	sentence
21735093	CK2 hyperactivates AKT by phosphorylation at Ser129

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252543	Ser134	ANLNRSTsVPENPKS	Homo sapiens	Acute Lymphoblastic Leukemia Cell
pmid	sentence
24291004	Akt1 impairs glucocorticoid-induced gene expression by direct phosphorylation of nr3c1 at position s134 and blocking glucocorticoid-induced nr3c1 translocation to the nucleus

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-252471	Ser1394	VRRPRPLsEPPRPT	Homo sapiens
pmid	sentence
14505491	Akt/pkb phosphorylates ron ser-1394, thus providing a docking site for 14-3-3based on these results, we propose a mechanism based on msp-ron-dependent phosphorylation and 14-3-3 association, whereby the function of alpha6beta4 switches from a mechanical adhesive device into a signaling component, and might be critically involved in human epidermal wound healing

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252482	Ser1417	INRERQKsLTLTPTR	Homo sapiens
pmid	sentence
16139227	Akt phosphorylates serine at position 1416 in girdin, and phosphorylated girdin accumulates at the leading edge of migrating cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-156122	Ser142	PQPREKVsSIDLEID	Homo sapiens
pmid	sentence
17572661	Akt binds and phosphorylates zyxin on serine 142, leading to its association with acinus zyxin is a substrate of caspases, but akt phosphorylation fails to protect its proteolytic degradation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-170530	Ser143	RTPRRSKsDGEAKPE	Homo sapiens
pmid	sentence
21151116	Akt1 kinase colocalizes and directly interacts with dnmt1 and phosphorylates ser143. Phosphorylated dnmt1 peaks during dna synthesis, before dnmt1 methylation. Depletion of akt1 or overexpression of dominant-negative akt1 increases methylated dnmt1, resulting in a decrease in dnmt1 abundance. In mammalian cells, phosphorylated dnmt1 is more stable than methylated dnmt1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252525	Ser145	IERIRMDsIGSTVSS	Homo sapiens
pmid	sentence
19526459	Here, we present evidence that akt inhibits mad1-mediated transcription repression by physical interaction with and phosphorylation of mad1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-198913	Ser1450	TVRSRHTsVVSSGPS	Homo sapiens	Leukemia Cell
pmid	sentence
23940660	Akt-induced phosphorylation of n-cor at serine 1450 contributes to its misfolded conformational dependent loss (mcdl) in acute myeloid leukemia of the m5 subtype.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-157790	Ser146	GRKRRQTsMTDFYHS	Homo sapiens
pmid	sentence
31575057	Pim-1, PKC, and Akt1 kinases phosphorylate Thr-145 and Ser-146 sites on p21 protein. Phosphorylation at Thr-145 promotes cytoplasmic translocation and stability of p21. Ser-146 phosphorylation mediated by Akt1 enhances p21 stabilization and promotes cell survival.

Identifier	Residue	Sequence	Organism
SIGNOR-149698	Thr145	QGRKRRQtSMTDFYH	Homo sapiens
pmid	sentence
16982699	Whereas akt1 phosphorylates p21, inducing its release from cdk2 and cytoplasmic localization as previously described for akt, akt2 binds p21 in the region spanning the t145 site of p21, thus competing with phosphorylation by akt1 and inducing its accumulation in the nucleus. These distinct roles of akt/pkb isoforms in modulating proliferation and p21 have important implications for the development of drugs aimed at inhibiting cancer cell proliferation.[...] We next investigated if phosphorylation of p21-t145 interfered with akt2 binding. As shown in fig. ?Fig.8e8e (right lane), phosphorylation of p21 on t145 effectively prevented akt2 interaction.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-252468	Ser159	LLRERKSsAPSHSSQ	Homo sapiens
pmid	sentence
11782427	Pkb constitutively associates with gab2, phosphorylates gab2 on a consensus phosphorylation site, ser159, in vitro and inhibits gab2 tyrosine phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277802	Ser165	LSRLRSPsVLEVREK	Homo sapiens	HuH-7 Cell
pmid	sentence
36797475	Rabin8 is phosphorylated and activated by Akt in cells grown on stiff ECM.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277816	Ser165	LSRLRSPsVLEVREK	Homo sapiens	HuH-7 Cell
pmid	sentence
36797475	Rabin8 is phosphorylated and activated by Akt in cells grown on stiff ECM.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-116270	Ser166	SSRRRAIsETEENSD	Homo sapiens
pmid	sentence
11504915	Mitogen-induced activation of phosphatidylinositol 3-kinase (pi3-kinase) and its downstream target, the akt/pkb serine-threonine kinase, results in phosphorylation of mdm2 on serine 166 and serine 186. Phosphorylation on these sites is necessary for translocation of mdm2 from the cytoplasm into the nucleus.Both akt expression and serum treatment induced phosphorylation of mdm2 at ser186.

Identifier	Residue	Sequence	Organism
SIGNOR-124949	Ser166	SSRRRAIsETEENSD	Homo sapiens
pmid	sentence
15169778	Stabilization of mdm2 via decreased ubiquitination is mediated by protein kinase b/akt-dependent phosphorylation.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265724	Ser173	VFLKRDDsNESDVVE	Homo sapiens	PC-3 Cell
pmid	sentence
31406245	In mitochondria, LonP1 is phosphorylated by Akt on Ser173 and Ser181, enhancing its protease activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265725	Ser181	NESDVVEsLDEIYHT	Homo sapiens	PC-3 Cell
pmid	sentence
31406245	In mitochondria, LonP1 is phosphorylated by Akt on Ser173 and Ser181, enhancing its protease activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-148983	Ser1834	MLRRRMAsMQRTGVV	Homo sapiens
pmid	sentence
16926151	We find that suberoylanilide hydroxamic acid stimulates akt activity, which is required to phosphorylate p300 at ser(1834). Akt-mediated phosphorylation of p300 dramatically increases its acetyltransferase activity

Identifier	Residue	Organism
SIGNOR-158624		Homo sapiens
pmid	sentence
17964260	Akt1 and 2 promote the association of myod with p300 and pcaf acetyltransferases, via direct phosphorylation of p300.

Publications:

2

Organism:

Homo Sapiens

Tissue:

Muscle

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252538	Ser184	VAGVLTAsLTIWKKM	Homo sapiens	Polymorphonuclear Neutrophil
pmid	sentence
14766748	Phosphorylation of Bax Ser184 by Akt regulates its activity and apoptosis in neutrophilsWe suggest that Bax is regulated by phosphorylation of Ser(184) in an Akt-dependent manner and that phosphorylation inhibits Bax effects on the mitochondria by maintaining the protein in the cytoplasm, heterodimerized with antiapoptotic Bcl-2 family members

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-116274	Ser186	RQRKRHKsDSISLSF	Homo sapiens
pmid	sentence
11504915	Mitogen-induced activation of phosphatidylinositol 3-kinase (pi3-kinase) and its downstream target, the akt/pkb serine-threonine kinase, results in phosphorylation of mdm2 on serine 166 and serine 186. Phosphorylation on these sites is necessary for translocation of mdm2 from the cytoplasm into the nucleus.Both akt expression and serum treatment induced phosphorylation of mdm2 at ser186.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-124953	Ser188	RKRHKSDsISLSFDE	Homo sapiens
pmid	sentence
15169778	Stabilization of mdm2 via decreased ubiquitination is mediated by protein kinase b/akt-dependent phosphorylationhere we show that pkb inhibits mdm2 self-ubiquitination via phosphorylation of mdm2 on ser(166) and ser(188)

Publications:

1

Organism:

Homo Sapiens

Tissue:

Kidney

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252506	Ser188	LYRSRMNsLEMTPAV	Homo sapiens	HEK-293 Cell
pmid	sentence
15581622	We have identified a putative consensus sequence for phosphorylation by akt/pkb of ho-1 at ser188. although the changes in activity are small, this study provides the first evidence for a role of the survival kinase akt in the regulation of ho-1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277548	Ser19	KMAVESPsDSAENGQ	Homo sapiens	MDA-MB-231 Cell
pmid	sentence
33574926	Akt interacts with and phosphorylates RSK2 at S19.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252497	Ser193	GLPERSVsLTGAPES	Homo sapiens
pmid	sentence
17177604	Beta-catenin transcript can be stabilized by either wnt or pi3k-akt signaling activation. Akt phosphorylates ksrp at a unique serine residue akt phosphorylates the mrna decay-promoting factor ksrp at a unique serine residue, induces its association with the multifunctional protein 14-3-3, and prevents ksrp interaction with the exoribonucleolytic complex exosome.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-252581	Ser196	KLRRRFSsLHFMVEV	in vitro
pmid	sentence
9812896	Akt phosphorylated recombinant casp9 in vitro on serine-196 and inhibited its protease activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252585	Ser196	KLRRRFSsLHFMVEV	Homo sapiens	Neuron
pmid	sentence
10529400	Akt phosphorylation site found in human caspase-9 is absent in mouse caspase-9BAD phosphorylation by Akt is an essential step for growth factor-mediated inhibition of caspase activation

Publications:

2

Organism:

In Vitro, Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-252472	Ser196	KLRRRFSsLHFMVEV	Homo sapiens
pmid	sentence
15004527	Akt phosphorylated recombinant casp9 in vitro on serine-196 and inhibited its protease activity

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-252484	Ser197	APRRRAAsMDSSSKL	Homo sapiens
pmid	sentence
16272144	Foxo4 transcription factor, also referred to afx, contains three putative phosphorylation motif sites for protein kinase b (pkb), thr32, ser197, and ser262, and it is proposed that phosphorylated foxo4 stays in the cytosol and is imported to the nucleus through dephosphorylation to induce target gene expression

Identifier	Residue	Sequence	Organism
SIGNOR-252485	Ser262	TFRPRSSsNASSVST	Homo sapiens
pmid	sentence
16272144	Foxo4 transcription factor, also referred to afx, contains three putative phosphorylation motif sites for protein kinase b (pkb), thr32, ser197, and ser262, and it is proposed that phosphorylated foxo4 stays in the cytosol and is imported to the nucleus through dephosphorylation to induce target gene expression

Identifier	Residue	Sequence	Organism
SIGNOR-252486	Thr32	QSRPRSCtWPLPRPE	Homo sapiens
pmid	sentence
16272144	Foxo4 transcription factor, also referred to afx, contains three putative phosphorylation motif sites for protein kinase b (pkb), thr32, ser197, and ser262, and it is proposed that phosphorylated foxo4 stays in the cytosol and is imported to the nucleus through dephosphorylation to induce target gene expression

Identifier	Residue	Organism
SIGNOR-175291		Homo sapiens
pmid	sentence
21798082	Akt inactivates protein degradation by phosphorylating and thus repressing the transcription factors of the foxo family, and stimulates protein synthesis via the mammalian target of rapamycin (mtor) and glycogen synthase kinase 3b (gsk3b).

Identifier	Residue	Organism
SIGNOR-252515		Homo sapiens
pmid	sentence
21620960	Akt phosphorylates members of the foxo factors (forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localisation. In particular, akt phosphorylates foxo1 on thr24, ser256 and ser319. Foxo 3alfa and foxo4 are phosphorylated on equivalent sites. In addition, phosphorylation of afx by protein kinase b inhibits its transcriptional activity.

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252853	Ser197	APRRRAAsMDSSSKL	Homo sapiens
pmid	sentence
16272144	Foxo4 transcription factor, also referred to afx, contains three putative phosphorylation motif sites for protein kinase b (pkb), thr32, ser197, and ser262, and it is proposed that phosphorylated foxo4 stays in the cytosol and is imported to the nucleus through dephosphorylation to induce target gene expression

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252856	Ser256	SPRRRAAsMDNNSKF	in vitro	CV-1 Cell
pmid	sentence
10377430	Here we show that the activation of phosphatidylinositol 3 (PI3) kinase by extracellular growth factors induces phosphorylation, nuclear export, and transcriptional inactivation of FKHR1, a member of the FKHR subclass of the forkhead family of transcription factors. Protein kinase B (PKB)/Akt, a key mediator of PI3 kinase signal transduction, phosphorylated recombinant FKHR1 in vitro at threonine-24 and serine-253. Mutants FKHR1(T24A), FKHR1(S253A), and FKHR1(T24A/S253A) were resistant to both PKB/Akt-mediated phosphorylation and PI3 kinase-stimulated nuclear export.

Identifier	Residue	Sequence	Organism
SIGNOR-252854	Ser262	TFRPRSSsNASSVST	Homo sapiens
pmid	sentence
16272144	Foxo4 transcription factor, also referred to afx, contains three putative phosphorylation motif sites for protein kinase b (pkb), thr32, ser197, and ser262, and it is proposed that phosphorylated foxo4 stays in the cytosol and is imported to the nucleus through dephosphorylation to induce target gene expression

Identifier	Residue	Sequence	Organism
SIGNOR-252860	Ser319	TFRPRTSsNASTISG	Homo sapiens
pmid	sentence
11237865	The transcription factor, forkhead in rhabdomyosarcoma (fkhr), is phosphorylated at three amino acid residues (thr-24, ser-256 and ser-319) by protein kinase b (pkb)alpha.Fkhr (forkhead in rhabdomyosarcoma), afx (all1 fused gene from chromosome x) and fkhrl1 (fkhr-like 1) are phosphorylated directly by pkb in cells, preventing them from stimulating gene transcription and leading to their exit from the nucleus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252857	Thr24	LPRPRSCtWPLPRPE	in vitro	CV-1 Cell
pmid	sentence
10377430	Here we show that the activation of phosphatidylinositol 3 (PI3) kinase by extracellular growth factors induces phosphorylation, nuclear export, and transcriptional inactivation of FKHR1, a member of the FKHR subclass of the forkhead family of transcription factors. Protein kinase B (PKB)/Akt, a key mediator of PI3 kinase signal transduction, phosphorylated recombinant FKHR1 in vitro at threonine-24 and serine-253. Mutants FKHR1(T24A), FKHR1(S253A), and FKHR1(T24A/S253A) were resistant to both PKB/Akt-mediated phosphorylation and PI3 kinase-stimulated nuclear export.

Identifier	Residue	Sequence	Organism
SIGNOR-252855	Thr32	QSRPRSCtWPLPRPE	Homo sapiens
pmid	sentence
16272144	Foxo4 transcription factor, also referred to afx, contains three putative phosphorylation motif sites for protein kinase b (pkb), thr32, ser197, and ser262, and it is proposed that phosphorylated foxo4 stays in the cytosol and is imported to the nucleus through dephosphorylation to induce target gene expression

Identifier	Residue	Organism
SIGNOR-252859		Homo sapiens
pmid	sentence
18394876	The phosphorylation of the two remaining akt-dependent sites inhibits foxo6 transcriptional activity

Identifier	Residue	Organism	Cell Line
SIGNOR-252852		Mus musculus	MEF Cell
pmid	sentence
18423396	Akt1/PKBalpha was found to be the major regulator of phosphorylation and nuclear export ofFoxO1, whose presence in the nucleus strongly attenuates adipocyte differentiation.

Identifier	Residue	Organism
SIGNOR-252843		Homo sapiens
pmid	sentence
21798082	Akt inactivates protein degradation by phosphorylating and thus repressing the transcription factors of the foxo family, and stimulates protein synthesis via the mammalian target of rapamycin (mtor) and glycogen synthase kinase 3b (gsk3b).

Identifier	Residue	Organism
SIGNOR-252847		Homo sapiens
pmid	sentence
21620960	Akt phosphorylates members of the foxo factors (forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localisation. In particular, akt phosphorylates foxo1 on thr24, ser256 and ser319. Foxo 3alfa and foxo4 are phosphorylated on equivalent sites. In addition, phosphorylation of afx by protein kinase b inhibits its transcriptional activity.

Publications:

10

Organism:

Homo Sapiens, In Vitro, Mus Musculus

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252568	Ser197	APRRRAAsMDSSSKL	Mus musculus	NIH-3T3-A14 Cell
pmid	sentence
10217147	Here we show that protein kinase B phosphorylates AFX, a human orthologue of daf -16 (refs 5, 6, 9), both in vitro and in vivo.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252569	Ser262	TFRPRSSsNASSVST	Mus musculus	NIH-3T3-A14 Cell
pmid	sentence
10217147	Here we show that protein kinase B phosphorylates AFX, a human orthologue of daf -16 (refs 5, 6, 9), both in vitro and in vivo.

Publications:

2

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252861	Ser197	APRRRAAsMDSSSKL	Mus musculus	NIH-3T3-A14 Cell
pmid	sentence
10217147	Here we show that protein kinase B phosphorylates AFX, a human orthologue of daf -16 (refs 5, 6, 9), both in vitro and in vivo.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252849	Ser253	APRRRAVsMDNSNKY	Homo sapiens	Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell
pmid	sentence
19188143	Akt-dependent phosphorylation of foxo3a (thr32, ser253, and ser315 for human foxo3) enhances foxo3a/14?3?3 Interaction and promotes foxo3a nuclear export to the cytoplasm, resulting in the repression of foxo3a transcriptional function

Identifier	Residue	Sequence	Organism
SIGNOR-252862	Ser262	TFRPRSSsNASSVST	Mus musculus
pmid	sentence
10217147	Here we show that protein kinase B phosphorylates AFX, a human orthologue of daf -16 (refs 5, 6, 9), both in vitro and in vivo.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252850	Ser315	DFRSRTNsNASTVSG	Homo sapiens	Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell
pmid	sentence
19188143	Akt-dependent phosphorylation of foxo3a (thr32, ser253, and ser315 for human foxo3) enhances foxo3a/14?3?3 Interaction and promotes foxo3a nuclear export to the cytoplasm, resulting in the repression of foxo3a transcriptional function

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252848	Thr32	QSRPRSCtWPLQRPE	Homo sapiens	Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell
pmid	sentence
19188143	Akt-dependent phosphorylation of foxo3a (thr32, ser253, and ser315 for human foxo3) enhances foxo3a/14-3-3 Interaction and promotes foxo3a nuclear export to the cytoplasm, resulting in the repression of foxo3a transcriptional function

Identifier	Residue	Organism	Cell Line
SIGNOR-252851		Mus musculus	MEF Cell
pmid	sentence
18423396	Akt1/PKBalpha was found to be the major regulator of phosphorylation and nuclear export ofFoxO1, whose presence in the nucleus strongly attenuates adipocyte differentiation.

Identifier	Residue	Organism
SIGNOR-252841		Homo sapiens
pmid	sentence
21798082	Akt inactivates protein degradation by phosphorylating and thus repressing the transcription factors of the foxo family, and stimulates protein synthesis via the mammalian target of rapamycin (mtor) and glycogen synthase kinase 3b (gsk3b).

Publications:

7

Organism:

Mus Musculus, Homo Sapiens

Tissue:

Skeletal Muscle

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-252519	Ser199	SQRGRSGsGNFGGGR	Homo sapiens
pmid	sentence
18562319	Our data also suggest that akt negatively regulates hnrnp a1-mediated ires activity via phosphorylation at ser199.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-141043	Ser21	CWRKRVKsEYMRLRQ	Homo sapiens
pmid	sentence
16224021	Enhancer of zeste homolog 2 (ezh2) is a methyltransferase that plays an important role in many biological processes through its ability to trimethylate lysine 27 in histone h3. Here, we show that akt phosphorylates ezh2 at serine 21 and suppresses its methyltransferase activity by impeding ezh2 binding to histone h3

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-252589	Ser21	SGRARTSsFAEPGGG	Homo sapiens
pmid	sentence
11035810	In response to insulin, gsk3a inhibited by phosphorylation at ser-21 by pkb/akt1;phosphorylation at this site causes a conformational change, preventing access of substrates to the active site.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252500	Ser212	RVRVRLLsGDTYEAV	Homo sapiens
pmid	sentence
17311912	Akt attenuation of the serine protease activity of htra2/omi through phosphorylation of serine 212

Publications:

1

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling, Glioblastoma Multiforme, Parkinson

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-154631	Ser215	SGRAREAsGAPTSSK	Homo sapiens	Neuron
pmid	sentence
17470458	The work presented here is the first demonstration that phosphorylation at s215 and s792 by akt regulates ligand binding, and the subcellular distribution of the receptor

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-108504	Ser215	SGRAREAsGAPTSSK	Chlorocebus aethiops	COS-1 Cell
pmid	sentence
11404460	Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor. Here, we demonstrate that akt phosphorylates the androgen receptor (ar) at ser-210 and ser-790

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-108508	Ser792	CVRMRHLsQEFGWLQ	Chlorocebus aethiops	COS-1 Cell
pmid	sentence
11404460	Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor. Here, we demonstrate that akt phosphorylates the androgen receptor (ar) at ser-210 and ser-790

Publications:

2

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273481	Ser220	GKDQRGQsIYSTSFP	Homo sapiens	Vascular Endothelial Cell Line
pmid	sentence
31341021	We observed that IGPR-1 is activated by shear stress and tensile force and that flow shear stress-mediated IGPR-1 activation modulates remodeling of endothelial cells. Mechanistically, shear stress stimulated activation of AKT Ser/Thr kinase 1 (AKT1), leading to phosphorylation of IGPR-1 at Ser-220.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276328	Ser227	QQRRRITsVQPPTGL	Homo sapiens	HeLa Cell
pmid	sentence
21620836	A reciprocal immunoprecipiation with anti-phospho-Akt substrate antibody followed by immunoblotting with anti-FLAG antibodies confirmed these findings (Fig. 1C). We concluded that Fbw7 is phosphorylated at S227 in vivo. Phosphorylation of Fbw7 is required for its biological activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-67313	Ser227	GARRRGGsASRSLPL	Homo sapiens
pmid	sentence
10224060	Akt kinase enhances human telomerase activity through phosphorylation of htert subunit as one of its substrate proteins.

Identifier	Residue	Sequence	Organism
SIGNOR-67317	Ser824	AVRIRGKsYVQCQGI	Homo sapiens
pmid	sentence
10224060	Akt kinase enhances human telomerase activity through phosphorylation of htert subunit as one of its substrate proteins.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-278373	Ser230	PKYSRQFsLEHVHGS	Homo sapiens
pmid	sentence
35080342	AKT1 and AKT2 phosphorylate HSF1 at S326 but only AKT1 activates HSF1.\|Mass spectrometry showed that AKT1 also phosphorylated HSF1 at T142, S230 and T527 in addition to S326, whereas the other kinases did not.

Identifier	Residue	Sequence	Organism
SIGNOR-277580	Ser230	PKYSRQFsLEHVHGS	in vitro
pmid	sentence
35080342	Mass spectrometry showed that AKT1 also phosphorylated HSF1 at T142, S230 and T527 in addition to S326, whereas the other kinases did not. Subsequent investigation revealed that phosphorylation at T142 is necessary for HSF1 trimerization and that S230, S326 and T527 are required for HSF1 gene transactivation and recruitment of TFIIB and CDK9.

Identifier	Residue	Sequence	Organism
SIGNOR-277581	Ser326	SSVDTLLsPTALIDS	in vitro
pmid	sentence
35080342	Mass spectrometry showed that AKT1 also phosphorylated HSF1 at T142, S230 and T527 in addition to S326, whereas the other kinases did not. Subsequent investigation revealed that phosphorylation at T142 is necessary for HSF1 trimerization and that S230, S326 and T527 are required for HSF1 gene transactivation and recruitment of TFIIB and CDK9.

Identifier	Residue	Sequence	Organism
SIGNOR-278374	Ser326	SSVDTLLsPTALIDS	Homo sapiens
pmid	sentence
35080342	AKT1 and AKT2 phosphorylate HSF1 at S326 but only AKT1 activates HSF1.\|Mass spectrometry showed that AKT1 also phosphorylated HSF1 at T142, S230 and T527 in addition to S326, whereas the other kinases did not.

Identifier	Residue	Sequence	Organism
SIGNOR-278372	Thr142	DSVTKLLtDVQLMKG	Homo sapiens
pmid	sentence
35080342	AKT1 and AKT2 phosphorylate HSF1 at S326 but only AKT1 activates HSF1.\|Mass spectrometry showed that AKT1 also phosphorylated HSF1 at T142, S230 and T527 in addition to S326, whereas the other kinases did not.

Identifier	Residue	Sequence	Organism
SIGNOR-277579	Thr142	DSVTKLLtDVQLMKG	in vitro
pmid	sentence
35080342	Mass spectrometry showed that AKT1 also phosphorylated HSF1 at T142, S230 and T527 in addition to S326, whereas the other kinases did not. Subsequent investigation revealed that phosphorylation at T142 is necessary for HSF1 trimerization and that S230, S326 and T527 are required for HSF1 gene transactivation and recruitment of TFIIB and CDK9.

Identifier	Residue	Sequence	Organism
SIGNOR-277578	Thr527	PPKAKDPtVS	in vitro
pmid	sentence
35080342	Mass spectrometry showed that AKT1 also phosphorylated HSF1 at T142, S230 and T527 in addition to S326, whereas the other kinases did not. Subsequent investigation revealed that phosphorylation at T142 is necessary for HSF1 trimerization and that S230, S326 and T527 are required for HSF1 gene transactivation and recruitment of TFIIB and CDK9.

Identifier	Residue	Sequence	Organism
SIGNOR-278371	Thr527	PPKAKDPtVS	Homo sapiens
pmid	sentence
35080342	AKT1 and AKT2 phosphorylate HSF1 at S326 but only AKT1 activates HSF1.\|Mass spectrometry showed that AKT1 also phosphorylated HSF1 at T142, S230 and T527 in addition to S326, whereas the other kinases did not.

Publications:

8

Organism:

Homo Sapiens, In Vitro

Identifier	Residue	Sequence
SIGNOR-275517	Ser230	LKRNRYLsFHFKSGS
pmid	sentence
15870194	Site-directed mutagenesis, mass spectrometry, and kinetic analyses identified S(230) in hBVR (225)RNRYLSF sequence as the Akt1 target.

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273540	Ser241	RMLSSSSsVSSLNSS	Homo sapiens	LNCaP Cell
pmid	sentence
15998322	By mutagenesis analysis and subsequent immunoprecipitation (IP), we established that Akt phosphorylates JFC1 at serine 241. Phosphorylation did not alter the ability of JFC1 to bind to Rab27a. Instead, phosphorylation by Akt dramatically decreased when JFC1 was bound to Rab27a. Finally, we show that as a consequence of in vivo phosphorylation, JFC1 dissociates from the membrane, promoting JFC1 redistribution to the cytosol.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251099	Ser2448	RSRTRTDsYSAGQSV	Homo sapiens
pmid	sentence
10910062	Although AKT phosphorylated mTOR at two COOH-terminal sites (Thr2446 and Ser2448) in vitro, Ser2448 was the major phosphorylation site in insulin-stimulated or -activated AKT-expressing human embryonic kidney cells. Transient transfection assays with mTOR mutants bearing Ala substitutions at Ser2448 and/or Thr2446 indicated that AKT-dependent mTOR phosphorylation was not essential for either PHAS-I phosphorylation or p70S6K activation in HEK cells.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-276055	Ser246	LSRERVFsEDRARFY	in vitro
pmid	sentence
16549426	Autophosphorylation of Akt on Thr-72 and Ser-246 appeared to require prior phosphorylation of Akt on Thr-308 and Ser-473. Compared with wild-type Akt, Akt/T72A/S246A mutant exhibited markedly reduced basal Akt kinase activity and response to cellular stimulation by insulin-like growth factor-1, and also conferred less cellular resistance to doxorubicin-induced apoptosis.

Identifier	Residue	Sequence	Organism
SIGNOR-276054	Thr72	TERPRPNtFIIRCLQ	in vitro
pmid	sentence
16549426	Autophosphorylation of Akt on Thr-72 and Ser-246 appeared to require prior phosphorylation of Akt on Thr-308 and Ser-473. Compared with wild-type Akt, Akt/T72A/S246A mutant exhibited markedly reduced basal Akt kinase activity and response to cellular stimulation by insulin-like growth factor-1, and also conferred less cellular resistance to doxorubicin-induced apoptosis.

Publications:

2

Organism:

In Vitro

Pathways:

Adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme, IGF and Myogenesis, P38 Signaling and Myogenesis, Parkinson

Identifier	Residue	Sequence	Organism
SIGNOR-252503	Ser250	RLRGRKRsMVG	Homo sapiens
pmid	sentence
17712528	Here we show that such an activation of prpk is mediated by another kinase, akt/pkb, which phosphorylates prpk at ser250.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-252844	Ser253	APRRRAVsMDNSNKY
pmid	sentence
19951971	AKT phosphorylates FOXO3a at three conserved sites (Thr32, Ser253 and Ser315), therefore creating binding sites for the 14-3-3 chaperone proteins and leading to the active export of FOXO3a to the cytoplasm where it is targeted for proteasomal degradation.

Identifier	Residue	Sequence
SIGNOR-252845	Ser315	DFRSRTNsNASTVSG
pmid	sentence
19951971	AKT phosphorylates FOXO3a at three conserved sites (Thr32, Ser253 and Ser315), therefore creating binding sites for the 14-3-3 chaperone proteins and leading to the active export of FOXO3a to the cytoplasm where it is targeted for proteasomal degradation.

Identifier	Residue	Sequence
SIGNOR-252846	Thr32	QSRPRSCtWPLQRPE
pmid	sentence
19951971	AKT phosphorylates FOXO3a at three conserved sites (Thr32, Ser253 and Ser315), therefore creating binding sites for the 14-3-3 chaperone proteins and leading to the active export of FOXO3a to the cytoplasm where it is targeted for proteasomal degradation.

Identifier	Residue	Organism
SIGNOR-252858		Homo sapiens
pmid	sentence
21440011	Phosphorylation of FoxOs by Akt inhibits transcriptional functions of FoxOs and contributes to cell survival, growth and proliferation.The PI3K/Akt signaling regulates cell proliferation and survival in part by phosphorylating FoxOs to promote their interaction with 14-3-3 protein that results in nuclear exclusion and eventual ubiquitin proteasome pathway (UPP)-dependent degradation of FoxOs

Publications:

4

Organism:

, Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-252522	Ser253	APRRRAVsMDNSNKY	Homo sapiens
pmid	sentence
19188143	Akt-dependent phosphorylation of foxo3a (thr32, ser253, and ser315 for human foxo3) enhances foxo3a/14?3?3 Interaction and promotes foxo3a nuclear export to the cytoplasm, resulting in the repression of foxo3a transcriptional function

Identifier	Residue	Sequence	Organism
SIGNOR-252523	Ser315	DFRSRTNsNASTVSG	Homo sapiens
pmid	sentence
19188143	Akt-dependent phosphorylation of foxo3a (thr32, ser253, and ser315 for human foxo3) enhances foxo3a/14?3?3 Interaction and promotes foxo3a nuclear export to the cytoplasm, resulting in the repression of foxo3a transcriptional function

Identifier	Residue	Sequence	Organism
SIGNOR-252524	Thr32	QSRPRSCtWPLQRPE	Homo sapiens
pmid	sentence
19188143	Akt-dependent phosphorylation of foxo3a (thr32, ser253, and ser315 for human foxo3) enhances foxo3a/14-3-3 Interaction and promotes foxo3a nuclear export to the cytoplasm, resulting in the repression of foxo3a transcriptional function

Identifier	Residue	Organism
SIGNOR-175288		Homo sapiens
pmid	sentence
21798082	Akt inactivates protein degradation by phosphorylating and thus repressing the transcription factors of the foxo family, and stimulates protein synthesis via the mammalian target of rapamycin (mtor) and glycogen synthase kinase 3b (gsk3b).

Publications:

4

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence
SIGNOR-249626	Ser253	APRRRAVsMDNSNKY
pmid	sentence
19951971	AKT phosphorylates FOXO3a at three conserved sites (Thr32, Ser253 and Ser315), therefore creating binding sites for the 14-3-3 chaperone proteins and leading to the active export of FOXO3a to the cytoplasm where it is targeted for proteasomal degradation.

Identifier	Residue	Sequence
SIGNOR-249627	Ser315	DFRSRTNsNASTVSG
pmid	sentence
19951971	AKT phosphorylates FOXO3a at three conserved sites (Thr32, Ser253 and Ser315), therefore creating binding sites for the 14-3-3 chaperone proteins and leading to the active export of FOXO3a to the cytoplasm where it is targeted for proteasomal degradation.

Identifier	Residue	Sequence
SIGNOR-249625	Thr32	QSRPRSCtWPLQRPE
pmid	sentence
19951971	AKT phosphorylates FOXO3a at three conserved sites (Thr32, Ser253 and Ser315), therefore creating binding sites for the 14-3-3 chaperone proteins and leading to the active export of FOXO3a to the cytoplasm where it is targeted for proteasomal degradation.

Publications:

3

Pathways:

Adipogenesis, IGF and Myogenesis

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236159	Ser256	SPRRRAAsMDNNSKF	in vitro	CV-1 Cell
pmid	sentence
10377430	Here we show that the activation of phosphatidylinositol 3 (PI3) kinase by extracellular growth factors induces phosphorylation, nuclear export, and transcriptional inactivation of FKHR1, a member of the FKHR subclass of the forkhead family of transcription factors. Protein kinase B (PKB)/Akt, a key mediator of PI3 kinase signal transduction, phosphorylated recombinant FKHR1 in vitro at threonine-24 and serine-253. Mutants FKHR1(T24A), FKHR1(S253A), and FKHR1(T24A/S253A) were resistant to both PKB/Akt-mediated phosphorylation and PI3 kinase-stimulated nuclear export.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236163	Thr24	LPRPRSCtWPLPRPE	in vitro	CV-1 Cell
pmid	sentence
10377430	Here we show that the activation of phosphatidylinositol 3 (PI3) kinase by extracellular growth factors induces phosphorylation, nuclear export, and transcriptional inactivation of FKHR1, a member of the FKHR subclass of the forkhead family of transcription factors. Protein kinase B (PKB)/Akt, a key mediator of PI3 kinase signal transduction, phosphorylated recombinant FKHR1 in vitro at threonine-24 and serine-253. Mutants FKHR1(T24A), FKHR1(S253A), and FKHR1(T24A/S253A) were resistant to both PKB/Akt-mediated phosphorylation and PI3 kinase-stimulated nuclear export.

Identifier	Residue	Organism	Cell Line
SIGNOR-236206		Mus musculus	MEF Cell
pmid	sentence
18423396	Akt1/PKBalpha was found to be the major regulator of phosphorylation and nuclear export ofFoxO1, whose presence in the nucleus strongly attenuates adipocyte differentiation.

Publications:

3

Organism:

In Vitro, Mus Musculus

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272922	Ser257	PSRPPRPsRPPPPTP	Homo sapiens	MDA-MB-231 Cell
pmid	sentence
30517763	AKT1-mediated phosphorylation of ITCH at Ser257 drives its nuclear translocation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252588	Ser259	SQRQRSTsTPNVHMV	Homo sapiens	Myoblast
pmid	sentence
10576741	Akt and protein kinase a (pka) phosphorylate s259 on raf-1 and inhibit its activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-147963	Ser259	SQRQRSTsTPNVHMV	Homo sapiens	Breast Cancer Cell, Prostate Gland Cancer Cell
pmid	sentence
16854453	Akt and protein kinase a (pka) phosphorylate s259 on raf-1 and inhibit its activity.

Identifier	Residue	Organism
SIGNOR-252531		Homo sapiens
pmid	sentence
22798428	Akt negatively regulates the raf and gsk-3 kinases and the cell cycle regulatory transcription factor fkhr.

Publications:

3

Organism:

Homo Sapiens

Tissue:

Muscle, Myotube

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-184922	Ser260	GSRVRVDsTAKVAEI	Homo sapiens
pmid	sentence
19332537	Furthermore, ha-tagged akt can phosphorylate gst-cct_ protein in vitro

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252476	Ser260	GTRGRLEsAQATFQA	Homo sapiens	Neuron
pmid	sentence
15809304	Akt phosphorylated arfaptin 2 at ser(260). we have also demonstrated that arfaptin 2 phosphorylation restores proteasome activity that is inhibited by the presence of polyq-huntingtin in cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-24994	Ser27	YYRQRAHsNPMADHT	Homo sapiens
pmid	sentence
3627513	The trna methylase mettl1 is phosphorylated and inactivated by pkb and rsk in vitro and in cells

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252548	Ser273	LLRDTFTsLGYEVQK	Homo sapiens
pmid	sentence
19339247	TNFalpha enhanced FLIP(L) serine phosphorylation, which was increased by activated Akt-1. Serine 273, a putative Akt-1 phosphorylation site in FLIP(L), was critical for the activation-induced reduction of FLIP(L). Thus, these observations document a novel mechanism where by TNFalpha facilitates the reduction of FLIP(L) protein, which is dependent on the phosphatidylinositol 3-kinase/Akt signaling.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-124365	Ser280	AKRPRVTsGGVSESP	Homo sapiens
pmid	sentence
15107605	The chk1 protein phosphorylated by pkb on serine 280 does not enter into protein complexes after replication arrest. Moreover, chk1 phosphorylated by pkb fails to undergo activating phosphorylation on serine 345 by atm/atr. Phosphorylation by atm/atr and association with other checkpoint proteins are essential steps in activation of chk1.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Adipogenesis, IGF and Myogenesis

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252535	Ser282	FFAKRKRsAPEKSSG	Homo sapiens	Breast Cancer Cell
pmid	sentence
23421998	Cdk inhibitor p57 (kip2) is downregulated by akt during her2-mediated tumorigenicityakt phosphorylates p57 on ser 282 or thr310. Akt activity results in destabilization of p57 by accelerating turnover rate of p57 and enhancing p57 ubiquitination

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252536	Thr310	GVGSVEQtPRKRLR	Homo sapiens	Breast Cancer Cell
pmid	sentence
23421998	Cdk inhibitor p57 (kip2) is downregulated by akt during her2-mediated tumorigenicityakt phosphorylates p57 on ser 282 or thr310. Akt activity results in destabilization of p57 by accelerating turnover rate of p57 and enhancing p57 ubiquitination

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-274064	Ser283	ILSLRSCsLGSLGAL	in vitro
pmid	sentence
27407113	We demonstrate that S6 kinases can phosphorylate the extended C-terminal domain of TRBP and interact with TRBP in situ in primary cells. TRBP serines 283/286 are essential for S6K-mediated TRBP phosphorylation, optimal expression of TRBP, and the S6K-TRBP interaction in human primary cells. In vitro kinase assays demonstrated that TRBP-D3 can be phosphorylated by S6K1, S6K2, but also AKT1 (Figure (Figure1C),1C),

Identifier	Residue	Sequence	Organism
SIGNOR-274067	Ser286	LRSCSLGsLGALGPA	in vitro
pmid	sentence
27407113	We demonstrate that S6 kinases can phosphorylate the extended C-terminal domain of TRBP and interact with TRBP in situ in primary cells. TRBP serines 283/286 are essential for S6K-mediated TRBP phosphorylation, optimal expression of TRBP, and the S6K-TRBP interaction in human primary cells.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-252529	Ser291	ELRRRKIsKGCEVPL	Homo sapiens
pmid	sentence
22334668	Akt phosphorylates phf20 at ser(291) in vitro and in vivo, which results in its translocation from the nucleus to the cytoplasm and attenuation of phf20 function.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252583	Ser295	VIRPRRRsSCVSLGE	Homo sapiens
pmid	sentence
10454575	Pde3b is a physiological substrate of akt and that akt-mediated phosphorylation of pde3b on serine-273 is important for insulin-induced activation of pde3b.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252573	Ser295	VIRPRRRsSCVSLGE	Mus musculus	NIH-3T3 Cell
pmid	sentence
10454575	PDE3B is a physiological substrate of Akt and that Akt-mediated phosphorylation of PDE3B on serine-273 is important for insulin-induced activation of PDE3B

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252554	Ser318	CKIFRRPsLPCISRE	Mus musculus	3T3-L1 Cell
pmid	sentence
10454575	PDE3B is a physiological substrate of Akt and that Akt-mediated phosphorylation of PDE3B on serine-273 is important for insulin-induced activation of PDE3B.

Publications:

2

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252586	Ser304	GAPPRRSsIRNAHSI	Homo sapiens	Neutrophil
pmid	sentence
10559253	Akt phosphorylates p47phox and mediates respiratory burst activity in human neutrophils. A direct interaction between p47(phox) and akt was shown. Active recombinant akt phosphorylated recombinant p47(phox) in vitro. Mutation analysis indicated that 2 aa residues, ser(304) and ser(328), were phosphorylated by akt. Inhibition of akt activity also inhibited fmlp-stimulated neutrophil chemotaxis.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252587	Ser328	QDAYRRNsVRFLQQR	Homo sapiens	Neutrophil
pmid	sentence
10559253	Akt phosphorylates p47phox and mediates respiratory burst activity in human neutrophils. A direct interaction between p47(phox) and akt was shown. Active recombinant akt phosphorylated recombinant p47(phox) in vitro. Mutation analysis indicated that 2 aa residues, ser(304) and ser(328), were phosphorylated by akt. Inhibition of akt activity also inhibited fmlp-stimulated neutrophil chemotaxis.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252501	Ser304	KNTKKRHsFTSLTMA	Homo sapiens
pmid	sentence
17535800	We report here that posh is a direct substrate for phosphorylation by akt in vivo and in vitro, and we identify a major site of akt phosphorylation as serine 304 of posh, which lies within the rac-binding domain. We further show that phosphorylation of posh results in a decreased ability to bind activated rac, as does phosphomimetic s304d and s304e mutation of posh.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252474	Ser307	PARNRSAsITNLSLD	Homo sapiens
pmid	sentence
15546921	Here we report that serine318 on the fyve domain-containing ptdins3p 5-kinase (pikfyve) is a novel substrate for pkb, and show that phosphorylation stimulates the ptdins3p 5-kinase activity of the enzyme.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle

Identifier	Residue	Sequence	Organism
SIGNOR-139782	Ser310	QTRNRKAsGKGKKKR	Homo sapiens
pmid	sentence
16107690	We found that akt directly phosphorylates the transcription factor gata-1 at serine 310 and that this site-specific phosphorylation is required for the transcriptional activation of the timp-1 promoter.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-252559	Ser316	ANRPRKSsVNGSSAT
pmid	sentence
22505453	The polycomb group silencing protein Bmi1 can be phosphorylated by AKT, which enhances its oncogenic potential in PCa. Overexpression of Bmi1 can act in combination with PTEN haploinsufficiency to induce invasive carcinogenic formation in the prostate

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-105459	Ser319	TFRPRTSsNASTISG	Homo sapiens
pmid	sentence
11237865	The transcription factor, forkhead in rhabdomyosarcoma (FKHR), is phosphorylated at three amino acid residues (Thr-24, Ser-256 and Ser-319) by protein kinase b (PKB)alpha. FKHR (forkhead in rhabdomyosarcoma), AFX (all1 fused gene from chromosome x) and FKHRL1 (FKHR-like 1) are phosphorylated directly by PKB in cells, preventing them from stimulating gene transcription and leading to their exit from the nucleus.

Identifier	Residue	Organism	Cell Line
SIGNOR-236209		Mus musculus	MEF Cell
pmid	sentence
18423396	Akt1/PKBalpha was found to be the major regulator of phosphorylation and nuclear export of FoxO1, whose presence in the nucleus strongly attenuates adipocyte differentiation.

Identifier	Residue	Organism
SIGNOR-175285		Homo sapiens
pmid	sentence
21798082	Akt inactivates protein degradation by phosphorylating and thus repressing the transcription factors of the FoxO family, and stimulates protein synthesis via the mammalian target of rapamycin (mTOR) and glycogen synthase kinase 3b (GSK3B).

Publications:

3

Organism:

Homo Sapiens, Mus Musculus

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277376	Ser33	AETAAADsEPDTDPE	Homo sapiens	HEK-293T Cell
pmid	sentence
29343641	Here we show that the low levels of FBXO31 are maintained through proteasomal degradation by anaphase-promoting complex/cyclosome (APC/C). We find that the APC/C coactivators CDH1 and CDC20 bind to a destruction-box (D-box) motif present in FBXO31 to promote its polyubiquitination and degradation in a cell-cycle-regulated manner, which requires phosphorylation of FBXO31 on serine-33 by the prosurvival kinase AKT.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-278465	Ser338	PKRERPTsPAPHRPP	Homo sapiens
pmid	sentence
25074979	AKT1 interacts with and phosphorylates SIRT6 on Ser 338.\|Because AKT1 suppresses SIRT6 protein abundance by decreasing its stability, we investigated whether MDM2 is involved in this process.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275834	Ser34	WILGRKYsIFTEKDE	Homo sapiens	Colonic Cancer Cell
pmid	sentence
29165041	In this study, we identified a novel phosphorylation site at Ser34 of ATG4B induced by AKT in HCC cells.\| In brief, our results demonstrate for the first time that the phosphorylation of ATG4B at Ser34 participates in the metabolic reprogramming of HCC cells via repressing mitochondrial function, which possibly results from the Ser34 phosphorylation-induced mitochondrial enrichment of ATG4B and the subsequent inhibition of F1Fo-ATP synthase activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-167336	Ser34	HKRRRSRsWSSSSDR	Homo sapiens	HeLa Cell
pmid	sentence
20682768	Akt directly binds to and phosphorylates clk2 on serine 34 and threonine 127, in vitro and in vivo.Our results suggest that akt activation controls cell survival to ionizing radiation by phosphorylating clk2, revealing an important regulatory mechanism required for promoting cell surviva

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-167340	Thr127	RRRRRSRtFSRSSSQ	Homo sapiens	HeLa Cell
pmid	sentence
20682768	Akt directly binds to and phosphorylates clk2 on serine 34 and threonine 127, in vitro and in vivo.Our results suggest that akt activation controls cell survival to ionizing radiation by phosphorylating clk2, revealing an important regulatory mechanism required for promoting cell surviva

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252469	Ser345	ELLCLRRsSLKAYGN	Homo sapiens
pmid	sentence
11809767	Akt mediates sequestration of the beta(2)-adrenergic receptor in response to insulin. Phosphorylation studies of the c-terminal cytoplasmic domain of the beta(2)-adrenergic receptor by akt in vitro identified ser(345) and ser(346) within a consensus motif for akt phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-252470	Ser346	LLCLRRSsLKAYGNG	Homo sapiens
pmid	sentence
11809767	Akt mediates sequestration of the beta(2)-adrenergic receptor in response to insulin. Phosphorylation studies of the c-terminal cytoplasmic domain of the beta(2)-adrenergic receptor by akt in vitro identified ser(345) and ser(346) within a consensus motif for akt phosphorylation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252466	Ser351	GRRGRLPsKPKQPPD	Homo sapiens
pmid	sentence
11274386	We show that akt interacts with nur77 and inactivates nur77 by phosphorylation at ser-350

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252491	Ser352	AATNRPNsIDPALRR	Homo sapiens	Breast Cancer Cell
pmid	sentence
16551632	Site-directed mutagenesis identified ser-351, ser-745, and ser-747 as akt phosphorylation sites on vcp. however, our study also suggests that other known biological activities of vcp, such as those related to intracellular trafficking, ubiquitin-mediated proteolysis, and activation of transcription (28), might be regulated by akt through the activation of vcp. I

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252492	Ser746	AMRFARRsVSDNDIR	Homo sapiens	Breast Cancer Cell
pmid	sentence
16551632	Site-directed mutagenesis identified ser-351, ser-745, and ser-747 as akt phosphorylation sites on vcp. however, our study also suggests that other known biological activities of vcp, such as those related to intracellular trafficking, ubiquitin-mediated proteolysis, and activation of transcription (28), might be regulated by akt through the activation of vcp. I

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252493	Ser748	RFARRSVsDNDIRKY	Homo sapiens	Breast Cancer Cell
pmid	sentence
16551632	Site-directed mutagenesis identified ser-351, ser-745, and ser-747 as akt phosphorylation sites on vcp. however, our study also suggests that other known biological activities of vcp, such as those related to intracellular trafficking, ubiquitin-mediated proteolysis, and activation of transcription (28), might be regulated by akt through the activation of vcp. I

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251471	Ser365	GQRDRSSsAPNVHIN	Homo sapiens
pmid	sentence
10869359	Akt phosphorylates both S364 and S428. Akt downregulates B-Raf activity in vivo

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251472	Ser429	PQRERKSsSSSEDRN	Homo sapiens	HEK-293 Cell
pmid	sentence
10869359	Akt phosphorylates both S364 and S428. Akt downregulates B-Raf activity in vivo

Publications:

2

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling, Glioblastoma Multiforme

Identifier	Residue	Sequence	Organism
SIGNOR-252517	Ser367	PDCRRTIsAPVVRPK	Homo sapiens
pmid	sentence
18356162	We demonstrate that the serine/threonine kinase akt mediates phosphorylation of mdmx at ser367. This phosphorylation leads to stabilization of mdmx and consequent stabilization of mdm2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277492	Ser371	YARRRRPsQPYMFPR	Homo sapiens	MCF-7 Cell
pmid	sentence
31740618	S379 of RARγ is indispensable for the CLDN6-triggered cellular events. The most important finding of the present study is that the CLDN6/SFK/PI3K/AKT signaling controls the RARγ and ERα activities (Fig. 6).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252508	Ser378	AYTPRSLsAPIFTTS	Homo sapiens
pmid	sentence
20059950	Phosphorylation of ttc3 at ser378 is required for efficient biological function together, these observations support that ttc3 is a phosphorylation target of akt both in an in vitro and in a cellular context

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252511	Ser39	TTSTRTYsLGSALRP	Homo sapiens
pmid	sentence
20856200	The binding of akt (tail region) to vim (head region) results in vim ser39 phosphorylation enhancing the ability of vim to induce motility and invasion while protecting vim from caspase-induced proteolysis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271820	Ser392	GGEPRAHsKAQEDAW	Homo sapiens	BxPC-3 Cell
pmid	sentence
33148467	HSPA1A was found to associate with ACOT4. Furthermore, we found that phosphorylation of ACOT4 at S392 by AKT decreased the binding of ACOT4 to HSPA1A, resulting in ACOT4 accumulation. \|AKT phosphorylates ACOT4 at S392 and promotes ACOT4 stability

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276868	Ser40	KGWEVVEsDLYAMNF	Homo sapiens	HEK-293 Cell
pmid	sentence
31358653	Akt phosphorylates NQO1 on S40 and T128 residues. Here we show that Akt phosphorylates NQO1 at T128 residues and triggers its polyubiquitination and proteasomal degradation, abrogating its antioxidative effects in PD. Akt binds NQO1 in a phosphorylation-dependent manner. Interestingly, Akt, but not PINK1, provokes NQO1 phosphorylation and polyubiquitination with Parkin as an E3 ligase.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276869	Thr128	FIGEFAYtYAAMYDK	Homo sapiens	HEK-293 Cell
pmid	sentence
31358653	Akt phosphorylates NQO1 on S40 and T128 residues. Here we show that Akt phosphorylates NQO1 at T128 residues and triggers its polyubiquitination and proteasomal degradation, abrogating its antioxidative effects in PD. Akt binds NQO1 in a phosphorylation-dependent manner. Interestingly, Akt, but not PINK1, provokes NQO1 phosphorylation and polyubiquitination with Parkin as an E3 ligase.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252571	Ser400	EDQPRCQsLDSALLE	Homo sapiens	HEK-293 Cell
pmid	sentence
12138205	Akt-dependent phosphorylation of Cot occurs exclusively on serines 400 and 413. Akt to phosphorylate Cot at two sites in the carboxy-terminal domain, at least one of which may promote binding of substrates or coactivators to Cot, or alternatively may relieve binding of a negative regulator.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252572	Ser413	LERKRLLsRKELELP	Homo sapiens	HEK-293 Cell
pmid	sentence
12138205	Akt-dependent phosphorylation of Cot occurs exclusively on serines 400 and 413. Akt to phosphorylate Cot at two sites in the carboxy-terminal domain, at least one of which may promote binding of substrates or coactivators to Cot, or alternatively may relieve binding of a negative regulator.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-135614	Ser401	QTRNRKMsNKSKKSK	Homo sapiens	Monocyte
pmid	sentence
15837948	We show that insulin induces gata2 phosphorylation on serine 401 in a pi-3k/akt-dependent manner. Insulin-dependent phosphorylation of serine 401 impairs gata2 translocation to the nucleus and its dna binding activity

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-277358	Ser41	KRPLRAPsPEPAAPR	in vitro
pmid	sentence
28689659	Here we show that Akt, Erk2, and IKK1/2 phosphorylate Bcl3. Phosphorylation of Ser33 by Akt induces switching of K48 ubiquitination to K63 ubiquitination and thus promotes nuclear localization and stabilization of Bcl3. Phosphorylation by Erk2 and IKK1/2 of Ser114 and Ser446 converts Bcl3 into a transcriptional coregulator by facilitating its recruitment to DNA.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252590	Ser419	GGRSRSGsIVELIAG	Homo sapiens	Neuron
pmid	sentence
12062094	We demonstrate that huntingtin is a substrate of akt and that phosphorylation of huntingtin by akt is crucial to mediate the neuroprotective effects of igf-1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-164884	Ser42	GGRKRRSsRRSAGGG	Homo sapiens
pmid	sentence
20400976	Moreover, phosphorylation of twist-1 at ser42 was shown in vivo in various human cancer tissues, suggesting that this post-translational modification ensures functional activation of twist-1 after promotion of survival during carcinogenesis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252520	Ser422	RERSRTGsESSQTGT	Homo sapiens
pmid	sentence
18836482	Using an in vitro kinase assay, we found that pkb can directly phosphorylate eif4b on serine 422 (ser422). This was prevented by pretreatment of cells with the phosphatidylinositol 3-kinase (pi3k) inhibitor ly294002 or pharmacological inhibition of pkb. Phosphorylation regultes the activation of eukaryotic translation initiation factor 4b.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-265056	Ser432	THQGRSSsSGHYVSW	Homo sapiens
pmid	sentence
26523394	Phosphorylation and activation of ubiquitin-specific protease-14 by Akt regulates the ubiquitin-proteasome system\|These results suggested S432 as a major and S143 as a minor phosphorylation site of Akt.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273482	Ser445	NHRLRNDsVIVDTFH	Homo sapiens
pmid	sentence
22706160	AKT-mediated phosphorylation relocates nuclear USP4 to the cytoplasm and membrane and is required for maintaining its protein stability.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277213	Ser451	QEKSPGTsPLLSRKM	Homo sapiens	HEK-293 Cell
pmid	sentence
26932461	Akt dependent phosphorylation of LARP6. We provide the first description that LARP6 is phosphorylated at multiple sites and that phosphorylation of S451 is critical to activate the protein in type I collagen biosynthesis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-245255	Ser455	PAPSRTAsFSESRAD	Rattus norvegicus	Adipocyte
pmid	sentence
12107176	Taken together, these results demonstrate that serine 454 of ATP-citrate lyase is a novel and major in vivo substrate for protein kinase B.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-252488	Ser457	RGRKRFVsEGDGGRL	Homo sapiens
pmid	sentence
16357133	Our results show that akt specifically phosphorylates ser(67) and ser(457) residues of pdcd4 in vitro and in vivo. We further show that phosphorylation of pdcd4 by akt causes nuclear translocation of pdcd4.

Identifier	Residue	Sequence	Organism
SIGNOR-252496	Ser67	KRRLRKNsSRDSGRG	Homo sapiens
pmid	sentence
17053147	Both akt and p70(s6k) phosphorylate pdcd4, allowing for binding of the e3-ubiquitin ligase beta-trcp and consequently ubiquitylation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252505	Ser67	KRRLRKNsSRDSGRG	Homo sapiens	HEK-293 Cell
pmid	sentence
18296647	Both akt and p70(s6k) phosphorylate pdcd4, allowing for binding of the e3-ubiquitin ligase beta-trcp and consequently ubiquitylation.

Publications:

3

Organism:

Homo Sapiens

Tissue:

Skin

Identifier	Residue	Sequence	Organism
SIGNOR-252477	Ser461	NPLMRRNsVTPLASP	Homo sapiens
pmid	sentence
15896703	We also found that AMP activated protein kinase and protein kinases A, B, and C catalyzed the phosphorylation of Ser-460 of HBP1, and that in addition both isoforms are phosphorylated at a second, as yet undetermined site by protein kinase C. However, none of the phosphorylations had any effect on the intrinsic kinetic characteristics of either enzymatic activity, and neither did point mutation (mimicking phosphorylation), deletion, and alternative-splice modification of the HBP1 carboxy-terminal region. Instead, these phosphorylations and mutations decreased the sensitivity of the 6PF2K to a potent allosteric inhibitor, phosphoenolpyruvate, which appears to be the major regulatory mechanism.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252574	Ser466	PVRMRRNsFTPLSSS	Homo sapiens	HeLa Cell
pmid	sentence
12853467	14-3-3s bind directly to cardiac PFK-2 phosphorylated by PKB. PFK-2 was phosphorylated on both Ser466 and Ser483 by PKB. the precise mechanism of fru-2,6-P2 regulation by 14-3-3s is still puzzling.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252575	Ser483	IRRPRNYsVGSRPLK	Homo sapiens	HeLa Cell
pmid	sentence
12853467	14-3-3s bind directly to cardiac PFK-2 phosphorylated by PKB. PFK-2 was phosphorylated on both Ser466 and Ser483 by PKB. the precise mechanism of fru-2,6-P2 regulation by 14-3-3s is still puzzling.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252555	Ser466	PVRMRRNsFTPLSSS	Homo sapiens	HeLa Cell
pmid	sentence
12853467	These findings suggest that PKB-dependent binding of 14-3-3s to phospho-Ser483 of cardiac PFK-2 mediates the stimulation of glycolysis by growth factor.

Identifier	Residue	Sequence	Organism
SIGNOR-252584	Ser466	PVRMRRNsFTPLSSS	Homo sapiens
pmid	sentence
10521487	Heart 6-phosphofructo-2-kinase activation by insulin results from ser-466 and ser-483 phosphorylation and requires 3-phosphoinositide-dependent kinase-1, but not protein kinase b.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252464	Ser483	IRRPRNYsVGSRPLK	Homo sapiens	HeLa Cell
pmid	sentence
12853467	These findings suggest that pkb-dependent binding of 14-3-3s to phospho-ser483 of cardiac pfk-2 mediates the stimulation of glycolysis by growth factor.

Identifier	Residue	Sequence	Organism
SIGNOR-252528	Ser483	IRRPRNYsVGSRPLK	Homo sapiens
pmid	sentence
23457334	Akt-dependent activation of the heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (pfkfb2) isoenzyme by amino acids.

Publications:

4

Organism:

Homo Sapiens

Tissue:

Heart

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252603	Ser473	RPHFPQFsYSASGTA	Homo sapiens	SK-BR-3 Cell
pmid	sentence
14633703	Here, we identify PP1 as a serine/threonine phosphatase that associates with and dephosphorylates AKT in breast cancer cells\|The heat shock protein 90 inhibitor geldanamycin and the ErbB inhibitor ZD1839 promote rapid PP1 phosphatase-dependent inactivation of AKT in ErbB2 overexpressing breast cancer cells

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252607	Ser473	RPHFPQFsYSASGTA	Homo sapiens
pmid	sentence
21159657	Consistent with previous reports (2830), we found that expression of sv40st, suppression of either pp2a c or b resulted in elevated levels of akt phosphorylation (ser473)

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252596	Ser473	RPHFPQFsYSASGTA	in vitro
pmid	sentence
11313365	ILK Phosphorylates PKB/Akt on Serine 473 To become fully activated, PKB/Akt requires phosphorylation at two sites, threonine 308 and serine 473, in a phosphatidylinositol (PI) 3-kinase-dependent manner.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-174044	Ser473	RPHFPQFsYSASGTA	Homo sapiens	Neuron
pmid	sentence
21658387	A knockdown experiment using intact cells also demonstrated LRRK2-mediated phosphorylation of Akt1 (Ser473), suggesting that Akt1 is a convincing candidate for the physiological substrate of LRRK2.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252598	Ser473	RPHFPQFsYSASGTA	Homo sapiens	Neuron
pmid	sentence
24916379	Expression of wild-type LRRK2 promoted neuronal survival against apoptosis through activation of the downstream effector, Akt by phosphorylation of Ser473. Phosphorylated Akt in turn inhibited FOXO 1 signaling

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-248628	Ser473	RPHFPQFsYSASGTA	Homo sapiens
pmid	sentence
18160256	Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252606	Ser473	RPHFPQFsYSASGTA	Mus musculus	NIH-3T3 Cell
pmid	sentence
15367694	Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes

Identifier	Residue	Sequence	Organism
SIGNOR-248626	Thr308	KDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
18160256	Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252614	Thr308	KDGATMKtFCGTPEY	Mus musculus	NIH-3T3 Cell
pmid	sentence
15367694	Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes

Publications:

4

Organism:

Homo Sapiens, Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-252604	Ser473	RPHFPQFsYSASGTA	Homo sapiens
pmid	sentence
14633703	Here, we identify PP1 as a serine/threonine phosphatase that associates with and dephosphorylates AKT in breast cancer cells\|The heat shock protein 90 inhibitor geldanamycin and the ErbB inhibitor ZD1839 promote rapid PP1 phosphatase-dependent inactivation of AKT in ErbB2 overexpressing breast cancer cells

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252605	Ser473	RPHFPQFsYSASGTA	Homo sapiens	SK-BR-3 Cell
pmid	sentence
14633703	Here, we identify PP1 as a serine/threonine phosphatase that associates with and dephosphorylates AKT in breast cancer cells\|The heat shock protein 90 inhibitor geldanamycin and the ErbB inhibitor ZD1839 promote rapid PP1 phosphatase-dependent inactivation of AKT in ErbB2 overexpressing breast cancer cells

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248327	Ser473	RPHFPQFsYSASGTA	Homo sapiens	Chronic Myeloid Leukemia Cell
pmid	sentence
19261608	The Abl kinase inhibitors and depletion of Bcr-Abl induced the expression of PHLPP1 and PHLPP2, which dephosphorylated Ser-473 on Akt1, -2, and -3, resulting in inhibited proliferation of CML cells.\|Thus, Bcr-Abl represses the expression of PHLPP1 and PHLPP2 and continuously activates Akt1, -2, and -3 via phosphorylation on Ser-473, resulting in the proliferation of CML cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252600	Ser473	RPHFPQFsYSASGTA	Homo sapiens	HT-29 Cell, A-549 Cell
pmid	sentence
15718470	The rictor-mtor complex directly phosphorylated akt/pkb on ser473 in vitro and facilitated thr308 phosphorylation by pdk1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-217012	Ser473	RPHFPQFsYSASGTA	Homo sapiens	Blood Platelet
pmid	sentence
21592956	Protein kinase B (PKB, Akt) is a Ser/Thr kinase involved in the regulation of cell survival, proliferation, and metabolism and is activated by dual phosphorylation on Thr(308) in the activation loop and Ser(473) in the hydrophobic motif. It plays a contributory role to platelet function, although little is known about its regulation. In this study, we investigated the role of the mammalian target of rapamycin complex (mTORC)-2 in Akt regulation using the recently identified small molecule ATP competitive mTOR inhibitors PP242 and Torin1.

Identifier	Residue	Sequence	Organism
SIGNOR-217004	Ser473	RPHFPQFsYSASGTA	Homo sapiens
pmid	sentence
21157483	Mammalian TOR complex 1 (mTORC1) and mTORC2 exert their actions by regulating other important kinases, such as S6 kinase (S6K) and Akt.Recent findings have revealed novel important roles for mTORC2 in the phosphorylation of AGC kinase family members. mTORC2 phosphorylates and activates Akt, SGK, and PKC, which regulate cell survival, cell cycle progression and anabolism

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252441	Ser477	PQFSYSAsGTA	Homo sapiens	MCF-7 Cell
pmid	sentence
24670654	Phosphorylation of S477 and T479 at the Akt extreme carboxy terminus by cyclin-dependent kinase 2 (Cdk2)/cyclin A or mTORC2, under distinct physiological conditions, promotes Akt activation through facilitating, or functionally compensating for, S473 phosphorylation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252438	Thr450	TAQMITItPPDQDDS	Mus musculus	MEF Cell
pmid	sentence
18566586	MTORC2 phosphorylates newly synthesized Akt at the TM (Thr450) site to facilitate carboxyl-terminal folding and to stabilize Akt

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252444	Thr479	FSYSASGtA	Homo sapiens	MCF-7 Cell
pmid	sentence
24670654	Phosphorylation of S477 and T479 at the Akt extreme carboxy terminus by cyclin-dependent kinase 2 (Cdk2)/cyclin A or mTORC2, under distinct physiological conditions, promotes Akt activation through facilitating, or functionally compensating for, S473 phosphorylation

Publications:

6

Organism:

Homo Sapiens, Mus Musculus

Pathways:

FLT3-ITD signaling, Glioblastoma Multiforme, Parkinson

Identifier	Residue	Sequence	Organism
SIGNOR-137246	Ser473	RPHFPQFsYSASGTA	Homo sapiens
pmid	sentence
15896785	Knock-down of lar by the l3 sirna probe markedly inhibited the insulin-stimulated increase in the phosphorylation of protein kinase b (pkb, also called akt) on serine 473 by >90%

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252599	Ser473	RPHFPQFsYSASGTA	Homo sapiens	HT-29 Cell, A-549 Cell
pmid	sentence
15718470	The rictor-mtor complex directly phosphorylated akt/pkb on ser473 in vitro and facilitated thr308 phosphorylation by pdk1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-217869	Ser473	RPHFPQFsYSASGTA	Homo sapiens	Blood Platelet
pmid	sentence
21592956	Protein kinase B (PKB, Akt) is a Ser/Thr kinase involved in the regulation of cell survival, proliferation, and metabolism and is activated by dual phosphorylation on Thr(308) in the activation loop and Ser(473) in the hydrophobic motif. It plays a contributory role to platelet function, although little is known about its regulation. In this study, we investigated the role of the mammalian target of rapamycin complex (mTORC)-2 in Akt regulation using the recently identified small molecule ATP competitive mTOR inhibitors PP242 and Torin1.

Identifier	Residue	Sequence	Organism
SIGNOR-170604	Ser473	RPHFPQFsYSASGTA	Homo sapiens
pmid	sentence
21157483	Mammalian TOR complex 1 (mTORC1) and mTORC2 exert their actions by regulating other important kinases, such as S6 kinase (S6K) and Akt.Recent findings have revealed novel important roles for mTORC2 in the phosphorylation of AGC kinase family members. mTORC2 phosphorylates and activates Akt, SGK, and PKC, which regulate cell survival, cell cycle progression and anabolism

Publications:

3

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-252608	Ser473	RPHFPQFsYSASGTA	Homo sapiens
pmid	sentence
21329883	Upon mitogen stimulation, triggering of the innate immune response, re-exposure to glucose, or oncogene activation, tbk1 is recruited to the exocyst, where it activates akt. Akt is a direct tbk1 substrate that connects tbk1 to prosurvival signaling.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264658	Ser473	RPHFPQFsYSASGTA	Homo sapiens	SK-BR-3 Cell
pmid	sentence
14633703	Here, we identify PP1 as a serine/threonine phosphatase that associates with and dephosphorylates AKT in breast cancer cells\|The heat shock protein 90 inhibitor geldanamycin and the ErbB inhibitor ZD1839 promote rapid PP1 phosphatase-dependent inactivation of AKT in ErbB2 overexpressing breast cancer cells

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248455	Ser473	RPHFPQFsYSASGTA	Mus musculus
pmid	sentence
17353188	Reduction in the levels of both LMW-PTP isoforms in vitro and in vivo increased tyrosine phosphorylation of IR and AktSer473 and increased IRS-1- and IRS-2-associated PI3-K activities in both liver and fat.\|Activated PI3-K stimulates Akt (or protein kinase B) that in turn phosphorylates and inactivates glycogen synthase kinase-3

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252431	Ser473	RPHFPQFsYSASGTA	Homo sapiens	HUVEC Cell
pmid	sentence
18439899	DNA-PK phosphorylates HM Ser473 of PKB. However, we also noted similar patterns in T loop Thr308 phosphorylation after _-IR []his function is apparently restricted to the PKBalpha isoform

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252597	Ser473	RPHFPQFsYSASGTA	Homo sapiens
pmid	sentence
9736715	Ilk can phosphorylate pkb-akt on serine-473, whereas kinase-deficient ilk severely inhibits endogenous phosphorylation of pkb-akt on serine-473, demonstrating that ilk is involved in agonist stimulated, pi(3)k-dependent, pkb-akt activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-249630	Ser473	RPHFPQFsYSASGTA
pmid	sentence
19951971	PIP3 recruits PDK1 and AKT to the plasma membrane, where PDK1 phosphorylates AKT on Thr308 in the activation loop of the kinase domain. The phosphorylation of AKT on Ser473 by PDK2 acts as a gain control for AKT and regulates its degree of activation. The sirolimus-insensitive mTORC2 complex exhibits PDK2 activity

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252602	Ser473	RPHFPQFsYSASGTA	Homo sapiens	Glioblastoma Cell
pmid	sentence
15808505	Here, we identify a protein phosphatase, ph domain leucine-rich repeat protein phosphatase (phlpp), that specifically dephosphorylates the hydrophobic motif of akt (ser473 in akt1), triggering apoptosis and suppressing tumor growth.[...] These data are consistent with phlpp terminating akt signaling by directly dephosphorylating and inactivating akt.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-67367	Ser473	RPHFPQFsYSASGTA	Homo sapiens
pmid	sentence
10226025	We have partially purified a kinase from brain extract that phosphorylates Ser473 of PKBalpha in a PtdIns(3,4,5)P3-dependent manner and that is immunoprecipitated with PDK1 antibodies.

Identifier	Residue	Sequence	Organism
SIGNOR-252611	Thr308	KDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
12808134	Akt1 and akt2 are phosphorylated and activated by the protein kinase pdk1 at thr-308 or thr-309, respectively, in the activation t-loop, and further activation occurs through phosphorylation at ser-473 or ser-474, respectively. In this paper, we demonstrate that this is indeed the case, and report the purification and initial characterization of a 3 phosphoinositide-dependent protein kinase, pdk1, which activates pkb by phosphorylating it at thr308. Akt is directly phosphorylated and activated by pdk1. Akt/pkb activation requires the phosphorylation of thr308 in the activation loop by the phosphoinositide-dependent kinase 1 (pdk1).

Identifier	Residue	Sequence	Organism
SIGNOR-175675	Thr308	KDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
21798082	Pip3 acts in turn as a docking site for two kinases, phosphoinositidedependent kinase 1 (pdk1) and akt, and the subsequent phosphorylation of akt at serine 308 by pdk1, leading to akt activation.

Identifier	Residue	Sequence	Organism
SIGNOR-91354	Thr308	KDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
12167717	Together, these results suggest a mechanism in which 3' phosphoinositide lipid-dependent translocation of pkb to the plasma membrane promotes serine 473 phosphorylation, which is, in turn, necessary for pdk1-mediated phosphorylation of threonine 308 and, consequentially, full pkb activation.

Identifier	Residue	Sequence	Organism
SIGNOR-67363	Thr308	KDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
10226025	Protein kinase b (pkb) is activated by phosphorylation of thr308 and of ser473. Thr308 is phosphorylated by the 3-phosphoinositide-dependent protein kinase-1 (pdk1) but the identity of the kinase that phosphorylates ser473 (provisionally termed pdk2) is unknown.

Publications:

5

Organism:

Homo Sapiens

Tissue:

Brain

Pathways:

Adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme, IGF and Myogenesis

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248728	Ser473	RPHFPQFsYSASGTA	Homo sapiens	Chronic Myeloid Leukemia Cell
pmid	sentence
19261608	The Abl kinase inhibitors and depletion of Bcr-Abl induced the expression of PHLPP1 and PHLPP2, which dephosphorylated Ser-473 on Akt1, -2, and -3, resulting in inhibited proliferation of CML cells.\|Thus, Bcr-Abl represses the expression of PHLPP1 and PHLPP2 and continuously activates Akt1, -2, and -3 via phosphorylation on Ser-473, resulting in the proliferation of CML cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252601	Ser473	RPHFPQFsYSASGTA	Homo sapiens	Glioblastoma Cell
pmid	sentence
15808505	Here, we identify a protein_ phosphatase, ph domain leucine-rich repeat protein_ phosphatase_ (phlpp), that specifically_ dephosphorylates_ the hydrophobic motif of_ akt_ (ser473 in akt1), triggering_ apoptosis_ and suppressing_ tumor_ growth.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252440	Ser477	PQFSYSAsGTA	Homo sapiens	MCF-7 Cell
pmid	sentence
24670654	Phosphorylation of S477 and T479 at the Akt extreme carboxy terminus by cyclin-dependent kinase 2 (Cdk2)/cyclin A or mTORC2, under distinct physiological conditions, promotes Akt activation through facilitating, or functionally compensating for, S473 phosphorylation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252443	Thr479	FSYSASGtA	Homo sapiens	MCF-7 Cell
pmid	sentence
24670654	Phosphorylation of S477 and T479 at the Akt extreme carboxy terminus by cyclin-dependent kinase 2 (Cdk2)/cyclin A or mTORC2, under distinct physiological conditions, promotes Akt activation through facilitating, or functionally compensating for, S473 phosphorylation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276667	Ser48	QLSLRTVsLGAGAKD	Homo sapiens	T-24 Cell
pmid	sentence
25071014	We find that AKT phosphorylation of NPM-Ser48 prevents oligomerization that results in nucleoplasmic localization of ARF, constitutive MDM2 inhibition and stabilization of p53.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276461	Ser496	ATPQRSGsVSNYRSC	in vitro
pmid	sentence
27784766	Purified PKC and Akt both phosphorylated AMPKα1 Ser487 in vitro with similar efficiency. PKC activation was associated with reduced AMPK activity, as inhibition of PKC increased AMPK activity and phorbol esters inhibited AMPK, an effect lost in cells expressing mutant AMPKα1 Ser487Ala. Consistent with a pathophysiological role for this modification, AMPKα1 Ser487 phosphorylation was inversely correlated with insulin sensitivity in human muscle.

Identifier	Residue	Organism
SIGNOR-252739		in vitro
pmid	sentence
16340011	It is proposed that the effect of insulin to antagonize AMP-activated protein kinase activation involves a hierarchical mechanism whereby Ser 485/Ser 491 phosphorylation by protein kinase B reduces subsequent phosphorylation of Thr 172 by LKB1 and the resulting activation of AMP-activated protein kinase.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252542	Ser50	RNRYRDVsPFDHSRI	Mus musculus	NIH-3T3 Cell
pmid	sentence
11579209	Phosphorylation of ptp1b at ser(50) by akt impairs its ability to dephosphorylate the insulin receptor.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276466	Ser51	FERGRRGsKKGSIDV	Homo sapiens	NAMALWA Cell
pmid	sentence
23754751	The activated serine/threonine kinase Akt/protein kinase B (PKB) phosphorylated Btk on two sites prior to 14-3-3ζ binding. The interaction sites were mapped to phosphoserine pS51 in the pleckstrin homology domain and phosphothreonine pT495 in the kinase domain.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276465	Thr495	EMRHRFQtQQLLEMC	Homo sapiens	NAMALWA Cell
pmid	sentence
23754751	The activated serine/threonine kinase Akt/protein kinase B (PKB) phosphorylated Btk on two sites prior to 14-3-3ζ binding. The interaction sites were mapped to phosphoserine pS51 in the pleckstrin homology domain and phosphothreonine pT495 in the kinase domain.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277281	Ser516	KTSSRRSsMSMEETE	Homo sapiens	HEK-293T Cell
pmid	sentence
27702651	We found that AKT phosphorylates MITF at S510. Phosphorylated MITF S510 enhances its affinity to TP53 and promotes CDKN1A expression. Phosphorylation of MITF by AKT induces its degradation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252478	Ser52	TRRTRTFsATVRASQ	Homo sapiens
pmid	sentence
15910284	These and other results demonstrate that crhsp24 is phosphorylated at ser52 by pkbalpha in response to igf-1, at ser52 by pkbalpha and rsk in response to egf

Publications:

1

Organism:

Homo Sapiens

Tissue:

Kidney

Identifier	Residue	Sequence	Organism
SIGNOR-252499	Ser552	QDTQRRTsMGGTQQQ	Homo sapiens
pmid	sentence
17287208	Phosphorylation of beta-catenin by akt promotes beta-catenin transcriptional activity\|we have demonstrated that akt phosphorylates beta-catenin at ser552 in vitro and in vivo.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-252483	Ser554	SIRPRPGsLRSKPEP	Homo sapiens
pmid	sentence
16256741	Akt phosphorylates s554 in acap1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276254	Ser558	MQPPRSRsSIMSITA	in vitro
pmid	sentence
24548923	Here we show that Akt-mediated NF-κB activation is mediated at least in part through direct phosphorylation of the adaptor protein Carma1, which we previously demonstrated could interact with Akt in a TCR ligation-dependent manner. The putative Akt phosphorylation sites in Carma1 are distinct from known PKC consensus sites. Mutation of S551, S637 and S645 in Carma1 to non-phosphorylatable residues decreased phosphorylation of GST-Carma1-linker construct by Akt in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-276255	Ser644	NLMFRKFsLERPFRP	in vitro
pmid	sentence
24548923	Here we show that Akt-mediated NF-κB activation is mediated at least in part through direct phosphorylation of the adaptor protein Carma1, which we previously demonstrated could interact with Akt in a TCR ligation-dependent manner. The putative Akt phosphorylation sites in Carma1 are distinct from known PKC consensus sites. Mutation of S551, S637 and S645 in Carma1 to non-phosphorylatable residues decreased phosphorylation of GST-Carma1-linker construct by Akt in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-276621	Ser644	NLMFRKFsLERPFRP	in vitro
pmid	sentence
24548923	Akt phosphorylates S637 and S645 in the linker region of Carma1

Identifier	Residue	Sequence	Organism
SIGNOR-276620	Ser652	LERPFRPsVTSVGHV	in vitro
pmid	sentence
24548923	Akt phosphorylates S637 and S645 in the linker region of Carma1

Identifier	Residue	Sequence	Organism
SIGNOR-276256	Ser652	LERPFRPsVTSVGHV	in vitro
pmid	sentence
24548923	Here we show that Akt-mediated NF-κB activation is mediated at least in part through direct phosphorylation of the adaptor protein Carma1, which we previously demonstrated could interact with Akt in a TCR ligation-dependent manner. The putative Akt phosphorylation sites in Carma1 are distinct from known PKC consensus sites. Mutation of S551, S637 and S645 in Carma1 to non-phosphorylatable residues decreased phosphorylation of GST-Carma1-linker construct by Akt in vitro.

Publications:

5

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-252502	Ser571	RMRSRSRsFSRHRSC	Homo sapiens
pmid	sentence
17554339	Here we describe a mechanism by which insulin, through the intermediary protein kinase akt2/protein kinase b (pkb)-beta, elicits the phosphorylation and inhibition of the transcriptional coactivator peroxisome proliferator-activated receptor-coactivator 1alpha (pgc-1alpha), a global regulator of hepatic metabolism during fasting / phosphorylation of pgc-1alpha At ser570 Is required for akt to inhibit recruitment of pgc-1alpha To chromatin.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Liver

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-116587	Ser58	VVGARRSsWRVVSSI	Homo sapiens	HEK-293 Cell
pmid	sentence
11956222	Ese data indicate that pkb/akt phosphorylates ser-58 on 14-3-3zeta both in vitro and in intact cells. The functional relevance of this phosphorylation remains to be determined.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252557	Ser598	SARSRSNsAERLLEA	Mus musculus
pmid	sentence
16141217	This study identifies APS as a novel physiological substrate for PKB and the first serine phosphorylation site on APS

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-252577	Ser598	SARSRSNsAERLLEA	Mus musculus
pmid	sentence
16141217	Serine 588 of APS is a newly identified target for protein kinase B in intact cells and in vitro. The precise function of this PKB-mediated phosphorylation event is not entirely clear but may be responsible for regulating cellular localization and will be the subject of future investigation.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-252532	Ser60	DHWIRMRsQEGRPVQ	Homo sapiens
pmid	sentence
23095642	Mechanistic studies show that akt causes csn6 phosphorylation at ser 60, which, in turn, reduces ubiquitin-mediated protein degradation of csn6.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252591	Ser600	PARQRIRsCVSAENF	Homo sapiens
pmid	sentence
12409306	Ser(600) in ark5 was found to be phosphorylated by active akt resulting in the activation of kinase activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252530	Ser602	ASPARRAsAILPGVL	Homo sapiens
pmid	sentence
22510990	We demonstrate here that ultraviolet irradiation induces phosphorylation of niban at s602 by akt, which increases the association of niban with nucleophosmin and disassociation of nucleophosmin from the mdm2 complex.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251622	Ser615	SYKIRFNsISCSDPL	Homo sapiens	Vascular Endothelium
pmid	sentence
24379783	The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252512	Ser647	RGRGRGGsIRGRGRG	Homo sapiens
pmid	sentence
20870937	Upon T cell activation, NF90 translocates from the nucleus into the cytoplasm, where it binds to the AU-rich element-containing 3' untranslated regions of IL-2 mRNA and stabilizes it.\|Our previous work showed that CD28 costimulation of T cells activated AKT to phosphorylate NF90 at Ser647 and caused NF90 to undergo nuclear export and stabilize IL-2 mRNA.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252592	Ser674	PGRERGEsPTTPPTP	Homo sapiens	Neuron
pmid	sentence
12458207	Negative regulation of mixed lineage kinase 3 by protein kinase b/akt leads to cell survivalthe expression of activated akt1 inhibits mlk3-mediated cell death in a manner dependent on serine 674 phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-163472	Ser694	QTSKRHDsDTFPELK	Homo sapiens
pmid	sentence
20085797	We identify a novel akt phosphorylation site in brca1 at s694 which is responsive to activation of these signaling pathways. These data suggest akt phosphorylation of brca1 increases total protein expression by preventing proteasomal degradation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-154312	Thr509	LKRKRRPtSGLHPED	Homo sapiens	Breast Cancer Cell
pmid	sentence
17428466	Phosphatidylinositol 3-kinase/akt signaling enhances nuclear localization and transcriptional activity of brca1. mutation of threonine 509 in brca1, the site of akt phosphorylation, to an alanine, attenuates the ability of heregulin to induce brca1 nuclear accumulation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276437	Ser695	EERMRMEsRRQATVS	in vitro
pmid	sentence
23264741	Here we show that soluble growth factors enhance integrin signaling through Akt phosphorylation of FAK at Ser695 and Thr700.

Identifier	Residue	Sequence	Organism
SIGNOR-276436	Thr700	MESRRQAtVSWDSGG	in vitro
pmid	sentence
23264741	Here we show that soluble growth factors enhance integrin signaling through Akt phosphorylation of FAK at Ser695 and Thr700.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252576	Ser71	YDRLRPLsYPQTDVF	Homo sapiens	Melanoma Cell
pmid	sentence
10617634	Akt protein kinase inhibits Rac1-GTP binding through phosphorylation at serine 71 of Rac1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-278274	Ser72	PPRKRLKsKGSDKDF	Homo sapiens
pmid	sentence
19270695	We further show that Akt1 phosphorylates Skp2 at Ser72, which is required to disrupt the interaction between Cdh1 and Skp2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252550	Ser766	VTRTRSLsACNKRVG	Rattus norvegicus
pmid	sentence
16338927	We have demonstrated that Ser-322 is phosphorylated upon insulin stimulation of intact cells and that this site is directly phosphorylated in vitro by PKB and ribosomal S6 kinase, members of the AGC (protein kinases A, G, and C) family of insulin-stimulated protein kinases

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252561	Ser775	ATRKRRWsAPESRKL	Homo sapiens	HeLa Cell
pmid	sentence
12757707	Interaction of Ataxin-1 and 14-3-3 Requires Akt Phosphorylation at S776. 14-3-3 protein, a multifunctional regulatory molecule, mediates the neurotoxicity of ataxin-1 by binding to and stabilizing ataxin-1, thereby slowing its normal degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273483	Ser78	SARPRVKsSYSMENA	Homo sapiens	HEK-293 Cell
pmid	sentence
29748601	Our findings also identify an essential role for activation of Trabid by AKT-mediated phosphorylation at Ser78/Thr117 in negatively regulating Twist1 signaling, which further provides insights into the mechanisms by which Trabid regulates Twist1 ubiquitination.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273484	Thr117	QRRTRSPtESPQSSG	Homo sapiens	HEK-293 Cell
pmid	sentence
29748601	Our findings also identify an essential role for activation of Trabid by AKT-mediated phosphorylation at Ser78/Thr117 in negatively regulating Twist1 signaling, which further provides insights into the mechanisms by which Trabid regulates Twist1 ubiquitination.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236494	Ser80	IERLRTHsIESSGKL	Homo sapiens	HEK-293 Cell
pmid	sentence
11707464	Akt phosphorylated sek1 on serine 78.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-252526	Ser82	RALSRQLsSGVSEIR	Homo sapiens
pmid	sentence
19593530	First, the akt1, akt2, and akt3 isoforms can bind directly to hsp27 and can be found in a complex with p38 mapk, mk2, and hsp27 [98_100]. Second, rane and colleagues showed that akt could phosphorylate hsp27 at ser-82, but not ser-15 or ser-78, in vitro, while co-expression of an active akt mutant and hsp27 in hek cells resulted in hsp27 phosphorylation at the same residue.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252465	Ser83	ATRGRGSsVGGGSRR	Homo sapiens	HEK-293 Cell
pmid	sentence
11154276	Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1 akt decreased ask1 kinase activity stimulated by both oxidative stress and overexpression in 293 cells by phosphorylating a consensus akt site at serine 83 of ask1.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-119488	Ser87	VGRHRKVsPNCRFIN	Homo sapiens
pmid	sentence
14645242	Akt, including akt1 and akt2, interacts with and phosphorylates x-linked inhibitor of apoptosis protein (xiap) at residue serine-87 in vitro and in vivo. Phosphorylation of xiap by akt protects xiap from ubiquitination and degradation in response to cisplatin.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Ovary Cancer Cell

Pathways:

Adipogenesis, FLT3-ITD signaling, IGF and Myogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-252487	Ser87	FIFMRRSsLLSRSSS	Homo sapiens
pmid	sentence
16282323	Recombinant Akt could directly phosphorylate a GST-Bim(EL) fusion protein and identified the Akt phosphorylation site in the Bim(EL) domain as Ser(87). Further, we demonstrated that cytokine stimulation promotes Bim(EL) binding to 14-3-3 proteins. Finally, we show that mutation of Ser(87) dramatically increases the apoptotic potency of Bim(EL).

Publications:

1

Organism:

Homo Sapiens

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:

Identifier	Residue	Sequence	Organism
SIGNOR-130376	Ser92	RFRDRSFsEGGERLL	Homo sapiens
pmid	sentence
15538381	Here we report that protein kinase b (pkb/akt) stabilizes are transcripts by phosphorylating brf1 at serine 92 (s92). Recombinant brf1 promoted in vitro decay of are-containing mrna (are-mrna), yet phosphorylation by pkb impaired this activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235511	Ser939	SFRARSTsLNERPKS	Mus musculus	NIH-3T3 Cell
pmid	sentence
12150915	We demonstrate that, upon activation of PI3K, tuberin is phosphorylated on consensus recognition sites for PI3K-dependent S/T kinases. Moreover, Akt/PKB can phosphorylate tuberin in vitro and in vivo. We also show that S939 and T1462 of tuberin are PI3K-regulated phosphorylation sites and that T1462 is constitutively phosphorylated in PTEN(-/-) tumor-derived cell lines.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235515	Thr1462	GLRPRGYtISDSAPS	Mus musculus	NIH-3T3 Cell
pmid	sentence
12150915	We demonstrate that, upon activation of PI3K, tuberin is phosphorylated on consensus recognition sites for PI3K-dependent S/T kinases. Moreover, Akt/PKB can phosphorylate tuberin in vitro and in vivo. We also show that S939 and T1462 of tuberin are PI3K-regulated phosphorylation sites and that T1462 is constitutively phosphorylated in PTEN(-/-) tumor-derived cell lines.

Publications:

2

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-265891	Ser96	LARKRRNsRDGDPLP	Mus musculus
pmid	sentence
25378391	Akt modulated the pathway by phosphorylating mevalonate diphosphate decarboxylase (MDD) at Ser96. These data suggest that Akt regulates Rac1 activity by directly phosphorylating MDD at Ser96, which augments Rac1 geranylgeranylation.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252489	Ser96	FVCQDKSsGYHYGVS	Homo sapiens	Lung Cancer Cell
pmid	sentence
16417524	We report that akt, which is constitutively activated in nsclc cells, phosphorylates raralpha and inhibits its transactivation. / mutation of ser96 to alanine abrogated the suppressive effect of akt.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-254780	Ser971	STRLRQQsSSSKGDS	Homo sapiens
pmid	sentence
27858941	DAB2IP can be phosphorylated by RIP1 on Ser 604 within the PER domain, and by AKT1 on Ser 847 within the proline-rich domain. Although RIP1-mediated phosphorylation is stimulatory,40 a recent study reported that AKT-mediated phosphorylation inhibits DAB2IP functions

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-183543	Ser985	THLSRVRsLDLDDWP	Homo sapiens	Prostate Gland Cancer Cell
pmid	sentence
19176382	In addition, we have found that activated akt can bind and phosphorylate ggap2 at serine 629, which enhances gtp binding by ggap2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252551	Thr100	LRARDIItAWHPPAP	Homo sapiens	HEK-293 Cell
pmid	sentence
11976320	CaMKKc and Akt overexpression increases IRAK1 phosphorylation at Thr100, and point mutation of this site abrogates the inhibitory effect of Akt on IRAK1-mediated NF-kappaB activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276193	Thr1033	RLGERLRtMSCSDKI	in vitro
pmid	sentence
31095429	AKT-dependent phosphorylation of the adenosine deaminases ADAR-1 and -2 inhibits deaminase activity. Coimmunoprecipitation studies and in vitro kinase assays revealed that AKT-1, -2, and -3 interact with both ADAR1p110 and ADAR2 and phosphorylate these RNA editases. Using site-directed mutagenesis of suspected AKT phosphorylation sites, AKT was found to primarily phosphorylate ADAR1p110 and ADAR2 on T738 and T553, respectively

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277445	Thr116	KYRPRRKtKTLMKKD	Homo sapiens	Esophageal Squamous Cell Carcinoma Cell Line
pmid	sentence
30894683	Phosphorylation of SOX2 at threonine 116 by AKT inhibits the interaction of UBR5 with SOX2 and thus stabilizes SOX2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-163533	Thr117	IIRLRNKtLIEDEIA	Homo sapiens
pmid	sentence
20086174	We determined that mst2 phosphorylation by akt limits mst2 activity in two ways: first, by blocking its binding to rassf1a and by promoting its association into the raf-1 inhibitory complex, and second, by preventing homodimerization of mst2, which is needed for its activation. we identified t117 and t384 as akt phosphorylation sites in mst2.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252509	Thr117	IIRLRNKtLIEDEIA	Homo sapiens	Breast Cancer Cell
pmid	sentence
20231902	Akt phosphorylates mst2 at thr117 in vitro and in vivo, which leads to mst2 cleavage and kinase activity as well as nuclear translocation.

Identifier	Residue	Sequence	Organism
SIGNOR-163537	Thr384	GTMKRNAtSPQVQRP	Homo sapiens
pmid	sentence
20086174	We determined that mst2 phosphorylation by akt limits mst2 activity in two ways: first, by blocking its binding to rassf1a and by promoting its association into the raf-1 inhibitory complex, and second, by preventing homodimerization of mst2, which is needed for its activation. we identified t117 and t384 as akt phosphorylation sites in mst2.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252507	Thr120	IIRLRNKtLTEDEIA	Homo sapiens
pmid	sentence
19940129	Akt interacts with mst1 and phosphorylates a highly conserved residue threonine 120 of mst1, which leads to inhibition of its kinase activity and nuclear translocation as well as the autophosphorylation of thr(183).

Identifier	Residue	Sequence	Organism
SIGNOR-252537	Thr387	TMKRRDEtMQPAKPS	Homo sapiens
pmid	sentence
23431053	Full activation of mst1 requires an activation cleavage that is prevented by the phosphorylation of thr-387 by akt.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275582	Thr125	GFGSKVTtHPLAKDK
pmid	sentence
32858971	Using a proteomic approach, we identified on DJ-1 a novel threonine phosphorylation (T125) that was found, by the in-silico tool scansite 4, as part of a putative Akt consensus. \|Deglycase activity of DJ-1 on histones proteins, investigated by coupling 2D tau gel with LC-MS/MS and 2D-TAU (Triton-Acid-Urea)-Western blot, was found correlated with its phosphorylation status that, in turn, depends from Akt activation.

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252558	Thr135	DWLMRSFtCPSCMEP	Homo sapiens	WM-239 Cell
pmid	sentence
16123141	Upon inhibition of the AKT pathway or mutation of T135, the phosphorylation at one of these sites is virtually eliminated, suggesting that AKT may phosphorylate RNF11 at T135. Moreover, RNF11 is phosphorylated by AKT in vitro and is recognized by phospho-AKT substrate antibodies. RNF11 shows enhanced binding to 14-3-3 in WM239 cells compared with that seen in the parental WM35 cells which have low AKT activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277597	Thr151	FCNGRGNtSGSHIVN	Homo sapiens	HEK-293T Cell
pmid	sentence
35675814	AKT-Mediated UPF1 Phosphorylation at T151 Promotes UPF1 Helicase Activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265078	Thr152	AARARLLtEIHGGAG	Homo sapiens	HEK-293 Cell
pmid	sentence
27593939	Mechanistically, Akt1 physically interacted with and phosphorylated UBE2S at Thr 152, enhancing its stability by inhibiting proteasomal degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-179109	Thr157	GIRKRPAtDDSSTQN	Homo sapiens
pmid	sentence
18570873	Mtor may promote g1 progression in part through sgk1 activation and deregulate the cell cycle in cancers through both akt- and sgk-mediated p27 t157 phosphorylation and cytoplasmic p27 mislocalization.

Identifier	Residue	Sequence	Organism
SIGNOR-88294	Thr198	PGLRRRQt	Homo sapiens
pmid	sentence
12042314	Because Thr198-phosphorylated p27Kip1 was localized only in the cytoplasm, Akt might promote 14-3-3 binding to p27Kip1 by phosphorylation at Thr198, allowing its cytoplasmic localization and degradation.

Identifier	Residue	Organism
SIGNOR-252534		Homo sapiens
pmid	sentence
23400686	Furthermore, akt promotes cell cycle progression through downregulation of the cyclin dependent kinase inhibitor p27kip1.

Identifier	Residue	Organism
SIGNOR-121944		Homo sapiens
pmid	sentence
14967450	Furthermore, akt promotes cell cycle progression through downregulation of the cyclin dependent kinase inhibitor p27kip1.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252533	Thr163	SRRPRRRtFPGVASR	Homo sapiens
pmid	sentence
23166294	The prosurvival kinase akt phosphorylates cdca7 at threonine 163, promoting binding to 14-3-3, dissociation from myc, and sequestration to the cytoplasm. we have mapped the domains of interaction and have discovered that akt phosphorylates cdca7 near this contact region, leading to loss of its association with myc, binding to 14-3-3 proteins, and exclusion from the nucleus.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252578	Thr17	SAIRRAStIEMPQQA	Mus musculus	Cardiac Muscle Cell Line
pmid	sentence
19696029	Akt interacts with and phosphorylates PLN at Thr(17), the Ca(2+)-calmodulin-dependent kinase IIdelta site, whereas silencing Akt signaling, through the knock-out of phosphatidylinositol-dependent kinase-1, resulted in reduced phosphorylation of PLN at Thr(17).

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276881	Thr181	LIRDRLKtEPFEENS	Homo sapiens	HeLa Cell
pmid	sentence
25661488	Akt1 phosphorylates XLF at T181 Here, we report that Akt phosphorylates XLF at Thr181 to trigger its dissociation from the DNA ligase IV/XRCC4 complex, and promotes its interaction with 14-3-3β leading to XLF cytoplasmic retention, where cytosolic XLF is subsequently degraded by SCF(β-TRCP) in a CKI-dependent manner.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252518	Thr219	GGGTRRGtRGGARGR	Homo sapiens
pmid	sentence
18562279	Nuclear akt directly binds aly and phosphorylates it on the t219 residue. gfp-aly t219d displayed comparable activity to gfp control and wild-type aly, indicating that aly phosphorylation by akt is sufficient to enhance mrna export.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-187006	Thr23	EMRERLGtGGFGNVC	Homo sapiens
pmid	sentence
19609947	Although there are likely to be multiple levels of crosstalk between the pi3k-akt and nf-kb pathways, one mechanism has been attributed to direct phosphorylation of the amino acid residue t23 on ikb kinase alfa (ikkalfa) by akt, thereby leading to activation of this kinase upstream of nf-kb akt mediates ikkalpha phosphorylation at threonine 23 akt transiently associates in vivo with ikk and induces ikk activation. Akt mediates ikkalfa phosphorylation at threonine 23.Akt phosphorylates ikkalpha on t23, and this phosphorylation event is a prerequisite for the phosphorylation of p65 at s534 by ikkalpha and beta

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252545	Thr235	QARKRKRtSIENRVR	Homo sapiens	NCCIT Cell
pmid	sentence
23041284	Here we show that in ECCs, Akt phosphorylated the master pluripotency factor Oct4 at threonine 235, and that the levels of phosphorylated Oct4 in ECCs correlated with resistance to apoptosis and tumorigenic potential. Phosphorylation of Oct4 increased its stability and facilitated its nuclear localization and its interaction with Sox2, which promoted the transcription of the core stemness genes POU5F1 and NANOG.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252467	Thr236	RTRSRRLtFRKNISK	Homo sapiens
pmid	sentence
11583630	Activated akt binds to edg-1 and phosphorylates the third intracellular loop at the t(236) residue. Transactivation of edg-1 by akt is not required for g(i)-dependent signaling but is indispensable for rac activation, cortical actin assembly, and chemotaxis

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252544	Thr246	LPRPRLNtSDFQKLK	Homo sapiens	HEK-293 Cell
pmid	sentence
12524439	Treatment of these cells with 4-hydroxytamoxifen stimulated the phosphorylation of wt PRAS40 but not the mutant PRAS40 in which Thr-246 was mutated. These results demonstrate that activation of Akt alone is sufficient to induce phosphorylation of PRAS40

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277515	Thr299	QSRKRLAtSSASSQS	Homo sapiens	HEK-293T Cell
pmid	sentence
32123010	Here, we report that AKT phosphorylates MASTL at residue T299, which plays a critical role in its activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252615	Thr308	KDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
16495456	Activation of pp2a is the intermediate step between the abeta-ceramide cascade and the subsequent inactivation of akt.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-249629	Thr308	KDGATMKtFCGTPEY
pmid	sentence
19951971	PIP3 recruits PDK1 and AKT to the plasma membrane, where PDK1 phosphorylates AKT on Thr308 in the activation loop of the kinase domain.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252612	Thr308	KDGATMKtFCGTPEY	Homo sapiens	HeLa Cell
pmid	sentence
15718470	Akt/PKB activation requires the phosphorylation of Thr308 in the activation loop by the phosphoinositide-dependent kinase 1 (PDK1) and Ser473 within the carboxyl-terminal hydrophobic motif by an unknown kinase.

Publications:

2

Organism:

, Homo Sapiens

Pathways:

Adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme, IGF and Myogenesis

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275450	Thr308	KDGATMKtFCGTPEY	Homo sapiens	HCT-116 Cell
pmid	sentence
30688659	Mechanistically, MAPK4 directly bound and activated AKT by phosphorylation of the activation loop at threonine 308.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252613	Thr308	KDGATMKtFCGTPEY	Mus musculus	NIH-3T3 Cell
pmid	sentence
18042541	Regulation of phosphorylation of Thr-308 of Akt, cell proliferation, and survival by the B55alpha regulatory subunit targeting of the protein phosphatase 2A holoenzyme to Akt.\|Phosphorylation of Akt at regulatory residues Thr-308 and Ser-473 leads to its full activation. The protein phosphatase 2A (PP2A) has long been known to negatively regulate Akt activity. The PP2A holoenzyme consists of the structural subunit (A), catalytic subunit (C), and a variable regulatory subunit (B).

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence
SIGNOR-252609	Thr308	KDGATMKtFCGTPEY
pmid	sentence
10833263	Protein kinase B (PKB) was recently reported to be activated on the phosphorylation of Thr(308) by Ca(2+)/calmodulin-dependent protein kinase kinase alpha (CaM-kinase kinase alpha), suggesting that PKB was regulated through not only the phosphoinositide 3-kinase pathway but also the Ca(2+)/calmodulin protein kinase pathway.

Publications:

1

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-276756	Thr309	APLRRCRtLSGSPRP	in vitro
pmid	sentence
25361894	Here, we report that Cables1 levels are controlled by a phosphorylation and 14-3-3-dependent mechanism. Mutagenic analyses identified two residues, T44 and T150, that are specifically critical for 14-3-3 binding and that serve as substrates for phosphorylation by the cell survival kinase Akt, which by binding directly to Cables1 recruits 14-3-3 to the complex.Ectopic expression of activated Akt (AKT1) prevented Cables1-induced apoptosis.

Identifier	Residue	Sequence	Organism
SIGNOR-276757	Thr415	AFGARRNtIDSTSSF	in vitro
pmid	sentence
25361894	Here, we report that Cables1 levels are controlled by a phosphorylation and 14-3-3-dependent mechanism. Mutagenic analyses identified two residues, T44 and T150, that are specifically critical for 14-3-3 binding and that serve as substrates for phosphorylation by the cell survival kinase Akt, which by binding directly to Cables1 recruits 14-3-3 to the complex.Ectopic expression of activated Akt (AKT1) prevented Cables1-induced apoptosis.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252434	Thr312	TMKTFCGtPEYLAPE	Mus musculus	Th17 Cell
pmid	sentence
23142783	GSK3_ negatively regulates AKT activation by phosphorylating AKT at T312 in the substrate binding site, which inhibited IL-1-induced AKT activation and function.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-252516	Thr324	GGRSREGtMELRTTP	Homo sapiens
pmid	sentence
22044535	Blt2 phosphorylation at thr355 by akt is necessary for blt2-mediated chemotaxis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277272	Thr346	APRPRVEtSRAVPLA	in vitro
pmid	sentence
27505672	Using a phosphoproteomics screen, we now show that active Akt accumulates in the mitochondria during hypoxia and phosphorylates pyruvate dehydrogenase kinase 1 (PDK1) on Thr346 to inactivate the pyruvate dehydrogenase complex.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265101	Thr382	GCATRNRtVPFCSTF	Homo sapiens	HeLa Cell
pmid	sentence
24981175	Akt phosphorylates TKT on Thr382, markedly enhancing enzyme activity and increasing carbon flow through the nonoxidative PPP, thereby increasing purine synthesis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-178058	Thr39	LKKIRLDtETEGVPS	Homo sapiens
pmid	sentence
18354084	Akt phosphorylates cdk2 at threonine 39 residue both in vitro and in vivo. Although cdk2 threonine 39 phosphorylation mediated by akt enhances cyclin-a binding, it is dispensable for its basal binding and the kinase activity.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-252616	Thr450	TAQMITItPPDQDDS	Homo sapiens
pmid	sentence
11839802	Integrin alpha 2 beta 1 promotes activation of protein phosphatase 2a and dephosphorylation of akt and glycogen synthase kinase 3 beta

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-163965	Thr450	TAQMITItPPDQDDS	Homo sapiens
pmid	sentence
20186153	Akt activation is achieved through a series of phosphorylation steps, the first being akt phosphorylation at thr-450 by jnk kinases. Pp-1 acts as a major phosphatase to dephosphorylate akt at thr-450 and thus modulate its functions.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-163961	Thr450	TAQMITItPPDQDDS	Homo sapiens
pmid	sentence
20186153	Several stps have been reported to negatively regulate akt pathway. It has been shown that pp1 dephosphorylates akt and regulates cell survival.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252426	Thr450	TAQMITItPPDQDDS	Rattus norvegicus	Cardiomyocyte Cell Line
pmid	sentence
16306447	We report that JNKs are necessary for the reactivation of Akt after ischemic injury. We identified Thr450 of Akt as a residue that is phosphorylated by JNKs, and the phosphorylation status of Thr450 regulates reactivation of Akt after hypoxia, apparently by priming Akt for subsequent phosphorylation by 3-phosphoinositide-dependent protein kinase.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-252527	Thr458	QPRKRKLtVDTPGAP	Homo sapiens
pmid	sentence
19875456	The phosphorylation of ski at threonine 458 is induced by akt pathway activators including insulin, insulin-like growth factor-1, and hepatocyte growth factor. The phosphorylation of ski causes its destabilization and reduces ski-mediated inhibition of expression of another negative regulator of tgf-beta, smad7

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265496	Thr469	STRHRVLtSAFSRAT	Homo sapiens	HeLa Cell
pmid	sentence
24769208	In previous work, we demonstrated that TEIF (transcriptional element-interacting factor) distributes in the centrosomes and regulates centrosome status under both physiologic and pathologic conditions.\|A consensus motif for Akt phosphorylation (RHRVLT) proved to be involved in centrosomal TEIF localization, and the 469-threonine of this motif may be phosphorylated by Akt both in vitro and in vivo. Elimination of this phosphorylated site on TEIF caused reduced centrosome distribution and centrosome splitting or amplification.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-259984	Thr473	QHRARQKtLEHLQLS	Homo sapiens	Nasopharyngeal Carcinoma Cell
pmid	sentence
31435020	K63-linked ubiquitination enhances the interaction between Akt and HK2 and eventually increases HK2 phosphorylation on Thr473 and mitochondrial localization

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-186760	Thr492	PSHDRSRtVSASSTG	Homo sapiens	Neuron
pmid	sentence
19592491	Here we show that srpk2, a protein kinase specific for the serine/arginine (sr) family of splicing factors, triggers cell cycle progression in neurons and induces apoptosis through regulation of nuclear cyclin d1. Akt phosphorylates srpk2 on thr-492 and promotes its nuclear translocation leading to cyclin d1 up-regulation, cell cycle reentry, and neuronal apoptosis.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-276194	Thr553	LQGERLLtMSCSDKI	in vitro
pmid	sentence
31095429	AKT-dependent phosphorylation of the adenosine deaminases ADAR-1 and -2 inhibits deaminase activity. Coimmunoprecipitation studies and in vitro kinase assays revealed that AKT-1, -2, and -3 interact with both ADAR1p110 and ADAR2 and phosphorylate these RNA editases. Using site-directed mutagenesis of suspected AKT phosphorylation sites, AKT was found to primarily phosphorylate ADAR1p110 and ADAR2 on T738 and T553, respectively

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-252481	Thr60	EYRRRRHtMDKDSRG	Homo sapiens
pmid	sentence
16081417	Phosphorylation of wnk1 on thr-58 contributes to sgk1 activation. these data suggest that activation of sgk1 by wnk1 requires the catalytic activity of akt.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275722	Thr607	SHRPREVtVSLRATG
pmid	sentence
25753393	P84 forms a negative regulatory complex with p110gamma to control PI3Kgamma signalling during cell migration\|However, phosphorylation at this site was confirmed using an in vitro kinase assay in which Akt kinase was shown to readily phosphorylate Thr607 using a p84 peptide (Figure 1e), where Thr607 in conjunction with surrounding residues forms an Akt kinase consensus sequence\|In contrast, although p84-T607A exhibited basal p110γ dimerisation, this interaction could not be further induced with stimulation

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-252494	Thr642	QFRRRAHtFSHPPSS	Homo sapiens
pmid	sentence
16880201	14-3-3 proteins interact with as160 in an insulin- and akt-dependent manner via an akt phosphorylation site, thr-642.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-259815	Thr70	GRRIRELtAVVQKRF	Rattus norvegicus	PC12-AC Cell
pmid	sentence
20605787	Here, we show that human RPS3 is a physiological target of Akt kinase and a novel mediator of neuronal apoptosis. NGF stimulation resulted in phosphorylation of threonine 70 of RPS3 by Akt, and this phosphorylation was required for Akt binding to RPS3.our experiment demonstrated that Akt up-regulates the endonuclease activity of RPS3 via phosphorylation and led us to believe that Akt phosphorylation of RPS3 after DNA damage is an antiapoptotic signal or a molecular switch that extends the life of a cell after DNA damage.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252552	Thr779	LYKEATStFTNITYR	Homo sapiens	Blood Platelet
pmid	sentence
10896934	A survey of several protein kinases revealed that Thr-753 was avidly phosphorylated by PDK1 and Akt/PKB in vitro. These observations suggest that activation of PDK1 and/or Akt/PKB in platelets may modulate the binding activity and/or specificity of beta(3) for signaling molecules.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276932	Thr86	GIRRRSNtAQRLERL	Mus musculus	MEF Cell
pmid	sentence
26235620	Akt phosphorylates SIN1 at T86, enhancing mTORC2 kinase activity, which leads to phosphorylation of Akt S473 by mTORC2, thereby catalyzing full activation of Akt.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273542	Thr9	TSFEDADtEETVTCL	Homo sapiens	HEK-293 Cell
pmid	sentence
27965388	For the activation of signal 2, Akt is involved in TIFA Thr9 phosphorylation, which is essential for TIFA-TIFA homophilic oligomerization. Thr9 phosphorylation-dependent TIFA oligomerization facilitates the higher-order assembly of NLRP3 inflammasome, as indicated by the interaction between TIFA and caspase-1 in the activated ECs.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252479	Thr90	EARHRVPtTELCRPP	Homo sapiens	T-lymphocyte, Leukemia Cell
pmid	sentence
15930267	Akt phosphorylates tal1 oncoprotein and inhibits its repressor activity. / our results show that akt specifically phosphorylates thr90 of the tal1 protein within its transactivation domain in vitro and in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252446	Tyr176	EKATGRYyAMKILKK	Mus musculus
pmid	sentence
20333297	Ack1 (also known as ACK or TNK2), which directly phosphorylates AKT at an evolutionarily conserved tyrosine 176 in the kinase domain. Tyr176-phosphorylated AKT localizes to the plasma membrane and promotes Thr308/Ser473-phosphorylation leading to AKT activation.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-252617	Tyr315	TFCGTPEyLAPEVLE	Homo sapiens
pmid	sentence
15994200	These observations suggest that RET/PTC is able to phosphorylate the Y315 residue of PKB, an event that results in maximal activation of PKB for RET/PTC-induced thyroid tumorigenesis.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252618	Tyr315	TFCGTPEyLAPEVLE	Homo sapiens	Breast Cancer Cell
pmid	sentence
20606012	Here we demonstrate that AKT is a direct substrate of PTK6 and that AKT tyrosine residues 315 and 326 are phosphorylated by PTK6.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252622	Tyr326	EVLEDNDyGRAVDWW	Homo sapiens	Breast Cancer Cell
pmid	sentence
20606012	Here we demonstrate that AKT is a direct substrate of PTK6 and that AKT tyrosine residues 315 and 326 are phosphorylated by PTK6.

Publications:

3

Organism:

Homo Sapiens

Tissue:

Prostate Gland

Identifier	Residue	Sequence	Organism
SIGNOR-252620	Tyr315	TFCGTPEyLAPEVLE	Chlorocebus aethiops
pmid	sentence
11445557	Regulation of Akt/PKB Activation by Tyrosine PhosphorylationAs shown in Fig. 2 d, while mutation of Tyr340 has little effect on either tyrosine phosphorylation or kinase activity of Akt induced by Src527F, substitution of Tyr315 or Tyr326 with a phenylalanine, respectively, dramatically reduces both the tyrosine phosphorylation and kinase activity of Akt. The combination of these two mutations abolishes Src-induced tyrosine phosphorylation of Akt as well as its kinase activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252621	Tyr315	TFCGTPEyLAPEVLE	Homo sapiens	HEK-293 Cell
pmid	sentence
12600984	We also showed that phosphorylation of Tyr-315 in Akt induced by Src or EGF is dependent on the integrity of this proline-rich motif. Furthermore, the Akt mutant lacking this proline motif fails to block the transcription activity of Forkhead in 293 cells and poorly stimulates the proliferation of Madin-Darby canine kidney cells. Taken together, our data suggest that the interaction between the SH3 domain of Src family kinases and the proline-rich motif in the C-terminal regulatory region of Akt is required for tyrosine phosphorylation of Akt and its subsequent activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252623	Tyr326	EVLEDNDyGRAVDWW	Chlorocebus aethiops	COS Cell
pmid	sentence
11445557	Regulation of Akt/PKB Activation by Tyrosine PhosphorylationAs shown in Fig. 2 d, while mutation of Tyr340 has little effect on either tyrosine phosphorylation or kinase activity of Akt induced by Src527F, substitution of Tyr315 or Tyr326 with a phenylalanine, respectively, dramatically reduces both the tyrosine phosphorylation and kinase activity of Akt. The combination of these two mutations abolishes Src-induced tyrosine phosphorylation of Akt as well as its kinase activity.

Publications:

3

Organism:

Chlorocebus Aethiops, Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252619	Tyr315	TFCGTPEyLAPEVLE	Homo sapiens	NIH-3T3 Cell
pmid	sentence
15994200	The PKB Y315 residue, which is known to be phosphorylated by Src tyrosine kinase, was also a major site of phosphorylation by RET/PTC. RET/PTC-mediated tyrosine phosphorylation results in the activation of PKB kinase activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277237	Tyr47	KTGQAPGySYTAANK	in vitro
pmid	sentence
32781572	Finally, we propose that pro-survival kinase Akt (protein kinase B) is a likely mediator of the S47 phosphorylation of Cytc in the brain.

Publications:

1

Organism:

In Vitro

Pathways:

Identifier	Residue	Organism
SIGNOR-106593		Homo sapiens
pmid	sentence
11287630	Tumor necrosis factor (tnf) inhibited insulin-promoted tyrosine phosphorylation of irs-1 and activated the akt/protein kinase b serine-threonine kinase, a downstream target for phosphatidylinositol 3-kinase

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-258064		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Identifier	Residue	Organism
SIGNOR-259688		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Organism	Cell Line
SIGNOR-270267		Homo sapiens	Nasopharyngeal Carcinoma Cell
pmid	sentence
31435020	K63-linked ubiquitination enhances the interaction between Akt and HK2 and eventually increases HK2 phosphorylation on Thr473 and mitochondrial localization

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252539		Homo sapiens
pmid	sentence
20138985	Pras40 is an insulin-regulated inhibitor of the mtorc1 protein kinase. Insulin stimulates akt/pkb-mediated phosphorylation of pras40, which prevents its inhibition of mtorc1 in cells and in vitro. Phosphorylation of pras40 on thr246 by pkb/akt facilitates efficient phosphorylation of ser183 by mtorc1.

Identifier	Residue	Organism
SIGNOR-252540		Homo sapiens
pmid	sentence
17130464	Phosphorylation of pras40-thr246 by pkb/akt, and pras40-ser183 and pras40-ser221 by mtorc1 results in dissociation from mtorc1, and its binding to 14-3-3 proteins.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Glioblastoma Multiforme

Identifier	Residue	Organism	Cell Line
SIGNOR-81713		Homo sapiens	T-lymphocyte, Leukemia Cell
pmid	sentence
10983986	In vivo, tcl1 forms trimers, which associate with akt. Tcl1 facilitates the oligomerization and activation of akt. Our data show that tcl1 is a novel akt kinase coactivator, which promotes akt-induced cell survival and proliferation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-278304		Homo sapiens
pmid	sentence
20361981	Co-expression of Pc2 and Akt1 results in both phosphorylation and ubiquitylation of CtBP1, thereby targeting CtBP1 for degradation.\|CtBP1 phosphorylation by Akt1 appears to both decrease dimerization and induce ubiquitylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252710		Homo sapiens
pmid	sentence
12167717	PKB induction requires phosphorylation of two critical residues, threonine 308 in the activation loop and serine 473 near the carboxyl terminus. Membrane localization of PKB was found to be a primary determinant of serine 473 phosphorylation. PI3K activity was equally important for promoting phosphorylation of serine 473,

Identifier	Residue	Organism
SIGNOR-252711		Homo sapiens
pmid	sentence
16293724	We show that PGE2 stimulates colon cancer cell growth through its heterotrimeric guanine nucleotide-binding protein;G protein)-coupled receptor, EP2, by a signaling route that involves the activation of phosphoinositide 3-kinase and the protein kinase Akt

Identifier	Residue	Organism
SIGNOR-252704		Homo sapiens
pmid	sentence
19573809	However, here we show through phosphoprotein profiling and functional genomic studies that many PIK3CA mutant cancer cell lines and human breast tumors exhibit only minimal AKT activation and a diminished reliance on AKT for anchorage-independent growth

Identifier	Residue	Organism	Cell Line
SIGNOR-252708		Homo sapiens	Neuron
pmid	sentence
9346240	Growth factors can promote cell survival by activating the phosphatidylinositide-3'-OH kinase and its downstream target, the serine-threonine kinase Akt

Publications:

4

Organism:

Homo Sapiens

Tissue:

Breast Cancer Cell, Colonic Cancer Cell

Pathways:

IGF and Myogenesis, P38 Signaling and Myogenesis

Identifier	Residue	Organism	Cell Line
SIGNOR-79338		Homo sapiens	Myoblast
pmid	sentence
10896679	Two candidates that may function as mediators of pi3-k in the phosphorylation of mef2 proteins are pkb and big map kinase 1.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle

Pathways:

Identifier	Residue	Organism	Cell Line
SIGNOR-262227		Homo sapiens	T-lymphocyte
pmid	sentence
25336630	stimulations were performed in the presence or absence of Akt inhibitor VIII, which selectively inhibits Akt1/Akt2 activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262010
pmid	sentence
25309440	Different agents were used to inhibit either the PI3K/Akt or MEK/ERK pathways. The PI3K inhibitor, LY294002, and the Akt inhibitor, Akt inhibitor VIII, were used to inhibit the PI3K/Akt pathway.

Publications:

2

Organism:

Homo Sapiens,

Identifier	Residue	Organism
SIGNOR-252640		Homo sapiens
pmid	sentence
12612081	We found that insulin-induced ir tyrosine phosphorylation and pkb/akt sig- naling were enhanced in tcptp- cells and suppressed upon tcptp reconstitution, providing persuasive evidence that tcptp can regulate ir activation and signaling.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252579		Homo sapiens
pmid	sentence
8940145	The constitutively active akt also increased the synthesis of the ubiquitously expressed glucose transporter 1. The increased glucose influx in the 3t3-l1 adipocytes directed lipid but not glycogen synthesis

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-277106		Homo sapiens
pmid	sentence
24070612	Further, we show that INPP4B but not PTEN is able to reduce tyrosine phosphorylation of Akt1 and both the lipid and PTP activity of INPP4B likely contribute to the reduction of Akt1 phosphorylation.\|Further, we show that INPP4B but not PTEN is able to reduce tyrosine phosphorylation of Akt1 and both the lipid and protein tyrosine phosphatase activity of INPP4B likely contribute to the reduction of Akt1 phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252634		Homo sapiens
pmid	sentence
19573809	However, here we show through phosphoprotein profiling and functional genomic studies that many PIK3CA mutant cancer cell lines and human breast tumors exhibit only minimal AKT activation and a diminished reliance on AKT for anchorage-independent growth

Identifier	Residue	Organism
SIGNOR-235914		Homo sapiens
pmid	sentence
16293724	We show that PGE2 stimulates colon cancer cell growth through its heterotrimeric guanine nucleotide-binding protein;G protein)-coupled receptor, EP2, by a signaling route that involves the activation of phosphoinositide 3-kinase and the protein kinase Akt

Identifier	Residue	Organism	Cell Line
SIGNOR-236428		Homo sapiens	Neuron
pmid	sentence
9346240	Growth factors can promote cell survival by activating the phosphatidylinositide-3'-OH kinase and its downstream target, the serine-threonine kinase Akt

Identifier	Residue	Organism
SIGNOR-236353		Homo sapiens
pmid	sentence
12167717	PKB induction requires phosphorylation of two critical residues, threonine 308 in the activation loop and serine 473 near the carboxyl terminus. Membrane localization of PKB was found to be a primary determinant of serine 473 phosphorylation. PI3K activity was equally important for promoting phosphorylation of serine 473,

Publications:

4

Organism:

Homo Sapiens

Tissue:

Breast Cancer Cell, Colonic Cancer Cell

Pathways:

Glioblastoma Multiforme, IGF and Myogenesis

Identifier	Residue	Organism	Cell Line
SIGNOR-255658		Homo sapiens	Kasumi-1 Cell
pmid	sentence
26084673	We have determined that Id1 physically interacts with AKT1, through its C-terminal region, and promotes AKT1 phosphorylation;

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-252625		Homo sapiens	Lung Cancer Cell
pmid	sentence
16407838	Fhit inhibited activity of akt, a key effector in the phosphatidylinositol 3-oh kinase (pi3k) pathway;loss of endogenous fhit expression caused increased akt activity in vitro and in vivo, and overexpression of constitutively active akt inhibited fhit-induced apoptosis

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-256447		in vitro
pmid	sentence
10579725	P53 can inhibit the survival function of integrins by inducing the caspase-dependent cleavage and inactivation of the serine/threonine kinase akt/pkb;the involvement of caspase 3 in akt/pkb regulation was indicated by the ability of z-devd-fmk, a caspase 3 inhibitor, to block the alpha6beta4-associated reduction in akt/pkb levels in vivo, and by the ability of recombinant caspase 3 to promote the cleavage of akt/pkb in vitro

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism	Cell Line
SIGNOR-252490		Homo sapiens	Neuron
pmid	sentence
16537363	Indicating that akt positively regulates shh signaling by controlling pka-mediated gli inactivation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252514		Homo sapiens
pmid	sentence
21619873	Akt, a member of the ser-ine/threonine-specific protein kinase, was found to phosphorylate osx and dlx5

Identifier	Residue	Organism
SIGNOR-195549		Homo sapiens
pmid	sentence
21777568	We found that Akt phosphorylates Osterix and that Akt activation increases protein stability, osteogenic activity and transcriptional activity of Osterix. We also found that BMP-2 increases the protein level of Osterix in an Akt activity-dependent manner.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-209647		Homo sapiens
pmid	sentence
21440011	Phosphorylation of FoxOs by Akt inhibits transcriptional functions of FoxOs and contributes to cell survival, growth and proliferation.The PI3K/Akt signaling regulates cell proliferation and survival in part by phosphorylating FoxOs to promote their interaction with 14-3-3 protein that results in nuclear exclusion and eventual ubiquitin proteasome pathway (UPP)-dependent degradation of FoxOs

Publications:

1

Organism:

Homo Sapiens

Pathways:

Adipogenesis, IGF and Myogenesis

Identifier	Residue	Organism
SIGNOR-265320		Homo sapiens
pmid	sentence
12588998	Additionally, active akt1 kinase strongly phosphorylates histone h3 at serine 10 in vitro

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-252435		Mus musculus	MEF Cell
pmid	sentence
19074868	The BRCA1-BRCT domains bind to phosphorylated AKT (pAKT) and lead to its ubiquitination toward protein degradation

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-255107		Homo sapiens
pmid	sentence
15829723	Once phosphorylated, Akt can act on a broad spectrum of substrates that can influence cell survival and proliferation and protein synthesis (65). Phosphorylation of mTOR by Akt leads to mTOR activation (40, 52) and the subsequent activation of p70S6K

Publications:

1

Organism:

Homo Sapiens

Tissue:

Skeletal Muscle

Pathways:

FLT3-ITD signaling, Glioblastoma Multiforme, Parkinson

Identifier	Residue	Organism
SIGNOR-141817		Homo sapiens
pmid	sentence
16293724	Pge2 also stimulated akt activity in a pi3k-dependent manner.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252580		Homo sapiens
pmid	sentence
9415393	Akt is not only capable of stimulating the translocation of glut4 to the cell surface. Endogenous akt is likely to play a significant physiological role in insulin-stimulated glucose uptake in insulin targets such as muscle and adipose tissue

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-80706		Homo sapiens	B-lymphocyte
pmid	sentence
10942391	Taken together, the data presented here demonstrate that ship inhibits akt primarily through regulation of akt membrane localization.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252636		Homo sapiens
pmid	sentence
8650155	These results confirm that the activity changes observed are achieved by a reversible phosphorylation mechanism, and also argue that pp2a may negatively regulate rac-pk activity in vivo. Dephosphorylation of the activated rac-pk in itro by pp2ac resulted in an 87% reduction of kinase activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252639		Homo sapiens
pmid	sentence
15632081	Whereas insulin-induced phosphatidylinositol 3-kinase/akt signaling was prolonged in both tcptp-/- and ptp1b-/- immortalized mouse embryo fibroblasts (mefs), mitogen-activated protein kinase erk1/2 signaling was elevated only in ptp1b- mefs

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-252635		Homo sapiens	NCCIT Cell
pmid	sentence
23041284	Furthermore, in ECCs, unphosphorylated Oct4 bound to the AKT1 promoter and repressed its transcription.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-255844		Homo sapiens
pmid	sentence
15829723	Once phosphorylated, Akt can act on a broad spectrum of substrates that can influence cell survival and proliferation and protein synthesis (65). Phosphorylation of mTOR by Akt leads to mTOR activation (40, 52) and the subsequent activation of p70S6K

Publications:

1

Organism:

Homo Sapiens

Tissue:

Skeletal Muscle

Pathways:

Glioblastoma Multiforme

Identifier	Residue	Organism
SIGNOR-111003		Homo sapiens
pmid	sentence
11598301	Here, we describe a protein partner for pkbalpha termed ctmp, or carboxyl-terminal modulator protein, that binds specifically to the carboxyl-terminal regulatory domain of pkbalpha at the plasma membrane. Binding of ctmp reduces the activity of pkbalpha by inhibiting phosphorylation on serine 473 and threonine 308.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-195546		Homo sapiens
pmid	sentence
22298955	Akt, a member of the ser-ine/threonine-specific protein kinase, was found to phosphorylate osx and dlx5. akt interacts with and phosphorylates dlx5. In addition, we provide evidences that akt kinase activity is important for akt to enhance the protein stability and transcriptional activity of dlx5.

Identifier	Residue	Organism
SIGNOR-252513		Homo sapiens
pmid	sentence
21619873	Akt, a member of the ser-ine/threonine-specific protein kinase, was found to phosphorylate osx and dlx5. akt interacts with and phosphorylates dlx5. In addition, we provide evidences that akt kinase activity is important for akt to enhance the protein stability and transcriptional activity of dlx5.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252541		Mus musculus
pmid	sentence
15173318	Akt binds prohibitin 2 and relieves its repression of myod and muscle differentiation

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-254372		Homo sapiens
pmid	sentence
24743741	Activation of PDGFRα stimulates proliferation of PDGFRα(+) cells through PI3K-Akt and MEK2-MAPK signaling pathways, and aberrant accumulation of PDGFRα(+) cells was conspicuous in muscles of patients with both genetic and non-genetic muscle diseases.

Publications:

1

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling, Glioblastoma Multiforme

Identifier	Residue	Organism	Cell Line
SIGNOR-261262		Chlorocebus aethiops	COS Cell
pmid	sentence
10930578	Further, we have demonstrated an in vivo association of IMPDH and PKB/Akt by co‐immunoprecipitation from COS cells expressing a constitutively active form of PKB/Akt. Finally, we were able to show that this constitutively active PKB/Akt could phosphorylate IMPDH in vitro. Thus, the interplay between PKB/Akt and IMPDH reported here could suggest that PKB/Akt activation leads to IMPDH type II activation which in turn prepares the cell for entry into S phase.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Organism
SIGNOR-252642		Homo sapiens
pmid	sentence
23119004	Binding of igf to igf-ir activates pi3k to generate pip3 which in turn recruits and activates proteins that contain a pleckstrin homology ph) domain, including akt and pdk1.

Identifier	Residue	Organism
SIGNOR-252641		Homo sapiens
pmid	sentence
23633519	Akt is a serine-threonine protein kinase that plays important roles in cell growth, proliferation and apoptosis. It is activated after binding to phosphatidylinositol phosphates pips) with phosphate groups at positions 3,4 and 3,4,5 on the inositol ring.

Identifier	Residue	Organism
SIGNOR-236349		Homo sapiens
pmid	sentence
21798082	Pip3 acts in turn as a docking site for two kinases, phosphoinositidedependent kinase 1 pdk1) and akt, and the subsequent phosphorylation of akt at serine 308 by pdk1, leading to akt activation.

Publications:

3

Organism:

Homo Sapiens

Pathways:

Adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme

Identifier	Residue	Organism	Cell Line
SIGNOR-235340		Mus musculus	3T3-L1 Cell
pmid	sentence
19593385	In examining the requirements for different Akt-mediated phosphorylation sites on TSC2, we find that only TSC2 mutants lacking all five previously identified Akt sites fully block insulin-stimulated mTORC1 signaling in reconstituted Tsc2 null cells, and this mutant also inhibits adipogenesis

Identifier	Residue	Organism	Cell Line
SIGNOR-235628		Mus musculus	NIH-3T3 Cell
pmid	sentence
12150915	We have shown thataktregulates the tsc1-tsc2 complex by directly phosphorylating tsc2. Tsc2 is inactivated by akt-dependent phosphorylation, which destabilizes tsc2 and disrupts its interaction with tsc1. Tsc2 is inactivated by akt-dependent phosphorylation, which destabilizes tsc2 and disrupts its interaction with tsc1akt has been shown to directly phosphorylate two sites on tsc2 (s939 and t1462 on the full-length human protein), which are conserved and phosphorylated in drosophila tsc2, and is likely to phosphorylate two or three additional sites (s981 and s1130/s1132).

Publications:

2

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-235373		Mus musculus
pmid	sentence
11715022	We show that IGF-1 unexpectedly acts via Akt to antagonize calcineurin signalling during myotube hypertrophy.

Publications:

1

Organism:

Mus Musculus

Pathways:

IGF and Myogenesis, P38 Signaling and Myogenesis

Identifier	Residue	Organism
SIGNOR-254376		Homo sapiens
pmid	sentence
24743741	To further investigate the signaling pathway through which PDGFRα promotes the proliferation of PDGFRα+ cells, we used inhibitors of PI3K-Akt and Ras-MAPK pathways, which are known to be downstream signaling pathways of PDGFRα

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-252436		Mus musculus	NIH-3T3 Cell
pmid	sentence
20059950	TTC3 is an Akt-specific E3 ligase that binds to phosphorylated Akt and facilitates its ubiquitination and degradation within the nucleus

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-175294		Homo sapiens
pmid	sentence
21798082	Akt inactivates protein degradation by phosphorylating and thus repressing the transcription factors of the foxo family, and stimulates protein synthesis via the mammalian target of rapamycin (mtor) and glycogen synthase kinase 3b (gsk3b).

Identifier	Residue	Organism
SIGNOR-252582		Homo sapiens
pmid	sentence
18394876	The phosphorylation of the two remaining akt-dependent sites inhibits foxo6 transcriptional activity

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-81680		Homo sapiens	T-lymphocyte, Leukemia Cell
pmid	sentence
10983986	Full-length tcl1 and its isoforms bind to akt / in in vitro kinase assays using gsk-3_ as a substrate, we found that the presence of any of the tcl1 family proteins (tcl1, mtcp1, or tcl1b) as gst fusion proteins significantly enhanced akt-induced gsk-3_ phosphorylation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252630		Homo sapiens
pmid	sentence
22090271	Perifosine is an alkylphospholipid that targets the pleckstrin homology domain of akt and blocks its membrane translocation, hence preventing akt phosphorylation and activation

Identifier	Residue	Organism	Cell Line
SIGNOR-252629		Homo sapiens	Prostate Gland Cancer Cell
pmid	sentence
14617782	Perifosine is an alkylphospholipid that targets the pleckstrin homology domain of akt and blocks its membrane translocation, hence preventing akt phosphorylation and activation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-252644		Homo sapiens	HEK-293 Cell
pmid	sentence
12791994	TRB3 expression is induced in liver under fasting conditions, and TRB3 disrupts insulin signaling by binding directly to Akt and blocking activation of the kinase.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Liver

Identifier	Residue	Organism
SIGNOR-255106		Homo sapiens
pmid	sentence
15829723	IGF-I binding to its receptor activates the kinase activity of the receptor, which then recruits the insulin response substrate-1, causing activation of phosphatidyl-inositol-3 kinase (PI3K) to phosphorylate Akt.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Skeletal Muscle

Pathways:

Identifier	Residue	Organism
SIGNOR-266605		Homo sapiens
pmid	sentence
18718903	Akt1 Overexpression in Skeletal Muscle Increases Capillary Vessel Formation and Up-regulates Fstl1 Expression

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-178269		Homo sapiens
pmid	sentence
18423396	Moreover, expression of p27(kip1), an inhibitor of the cell cycle, was down regulated in an akt1/pkbalpha-specific manner during adipocytedifferentiation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-157291		Homo sapiens	Myoblast, Satellite Cell
pmid	sentence
17688959	Most importantly, we report that shh induces mapk/erk and phosphoinositide 3-kinase (pi3k)-dependent akt phosphorylation and that activation of both signaling pathways is essential for shh's signaling in muscle cells. However, the effect of shh on akt phosphorylation is more robust than that on mapk/erk, and data suggest that shh influences these pathways in a manner similar to igf-i.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle

Identifier	Residue	Organism
SIGNOR-252432		Homo sapiens
pmid	sentence
18249092	Furthermore, overall PKB activity, primarily consisting of cytosolic enzyme, was dependent upon levels of PI(3,4)P2, while only membrane-associated PKB activity was dependent upon PI(3,4,5)P3 levels. We conclude that PI(3,4,5)P3 and PI(3,4)P2 have distinct roles in determining PKB phosphorylation and activity. Thus, when investigating PI3K-PKB pathways, the importance of both lipids must be considered

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252631		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252462		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-278856		Homo sapiens	SUP-T1 Cell
pmid	sentence
26100275	These data suggest that miR-374b may negatively regulate the expression of Wnt16 and AKT1 by directly targeting the 3'-UTR of their mRNA.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252632		Homo sapiens
pmid	sentence
10698680	One of the best characterized targets of pi3k lipid products is the protein kinase akt or protein kinase b (pkb). In quiescent cells, pkb resides in the cytosol in a low-activity conformation. Upon cellular stimulation, pkb is activated through recruitment to cellular membranes by pi3k lipid products and phosphorylation by 3h-phosphoinositide-dependent kinase-1 (pdk1).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258118		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-217670		Homo sapiens
pmid	sentence
17964260	Akt1 and 2 promote the association of myod with p300 and pcaf acetyltransferases, via direct phosphorylation of p300.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle

Pathways:

Identifier	Residue	Organism
SIGNOR-277222		Homo sapiens
pmid	sentence
38402584	Jagged1 is upregulated by Akt upon activation by R-Ras. All three Akt isoforms influence Jagged1 expression in ECs, but Akt3 is the most prominent Akt isoform in this role, despite its low expression level compared with Akt1. Jagged1 then activates Notch to upregulate Hey1, Hes1, p21, p53, and Unc5b in adjacent cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-252461		Homo sapiens	Skin Cancer Cell
pmid	sentence
21841310	Treatment with the pi3k inhibitor ly294002 or the akt inhibitor mk2206 diminished s473 phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252594		Homo sapiens
pmid	sentence
12637568	Recently, we identified a 160-kda protein in adipocytes, designated as160, that is phosphorylated by the insulin-activated kinase akt

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle

Identifier	Residue	Organism
SIGNOR-254371		Homo sapiens
pmid	sentence
18483217	PDGF signaling has been implicated in several fibrotic conditions and is assumed to play a role in driving proliferation of cells with a myofibroblast phenotype.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252495		Homo sapiens
pmid	sentence
16892082	The glucose dependence of the antiapoptotic effects of growth factors and akt plus a strong correlation between akt-regulated mitochondrial hexokinase association and apoptotic susceptibility suggest a major role for hexokinases in these effects.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252626		Homo sapiens
pmid	sentence
16266983	We show that the presence of Flt3-ITD constitutively activates Akt (PKB), a key serine-threonine kinase within the phosphatidylinositol 3-kinase pathway.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism	Cell Line
SIGNOR-81671		Homo sapiens	T-lymphocyte, Leukemia Cell
pmid	sentence
10983986	Full-length tcl1 and its isoforms bind to akt / in in vitro kinase assays using gsk-3_ as a substrate, we found that the presence of any of the tcl1 family proteins (tcl1, mtcp1, or tcl1b) as gst fusion proteins significantly enhanced akt-induced gsk-3_ phosphorylation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252643		Homo sapiens
pmid	sentence
16452206	We now show that mtor inhibition induces insulin receptor substrate-1 expression and abrogates feedback the pathway, resulting in akt activation both in cancer cell lines and in patient tumors treated with the rapamycin derivative, rad001.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-123606		Homo sapiens
pmid	sentence
15048128	Pkb inhibits smad3 by preventing its phosphorylation, binding to smad4 and nuclear translocation. [...] Regulation of smad3 by pkb occurs through a kinase-activity-independent mechanism, resulting in a decrease in smad3-mediated transcription and protection of cells against tgf-beta-induced apoptosis.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-252637		Mus musculus
pmid	sentence
18042541	Regulation of phosphorylation of Thr-308 of Akt, cell proliferation, and survival by the B55alpha regulatory subunit targeting of the protein phosphatase 2A holoenzyme to Akt.\|Phosphorylation of Akt at regulatory residues Thr-308 and Ser-473 leads to its full activation. The protein phosphatase 2A (PP2A) has long been known to negatively regulate Akt activity. The PP2A holoenzyme consists of the structural \|Here we report the identification of the specific B regulatory subunit that targets the PP2A holoenzyme to Akt. We found endogenous association of PP2A AB55C holoenzymes with Akt by co-immunoprecipitation analyses in pro-lymphoid FL5.12 cells.subunit (A), catalytic subunit (C), and a variable regulatory subunit (B).

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-254351		Homo sapiens
pmid	sentence
21106848	It has been reported that IL-5 family members and selected chemotactic factors can activate the PI3K-Akt pathway in human blood eosinophils

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252624		in vitro
pmid	sentence
10579725	P53 can inhibit the survival function of integrins by inducing the caspase-dependent cleavage and inactivation of the serine/threonine kinase akt/pkb;the involvement of caspase 3 in akt/pkb regulation was indicated by the ability of z-devd-fmk, a caspase 3 inhibitor, to block the alpha6beta4-associated reduction in akt/pkb levels in vivo, and by the ability of recombinant caspase 3 to promote the cleavage of akt/pkb in vitro

Publications:

1

Organism:

In Vitro

Pathways:

Identifier	Residue	Organism
SIGNOR-252633		Homo sapiens
pmid	sentence
10698680	Pkb is activated through recruitment to cellular membranes by pi3k lipid products and phosphorylation by 3h-phosphoinositide-dependent kinase-1 (pdk1)

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-161434		Homo sapiens
pmid	sentence
18534819	The decreased atm expression suggests that atm is involved in the development of insulin resistance through down-regulation of akt activity.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle

Pathways:

Identifier	Residue	Organism
SIGNOR-252628		Homo sapiens
pmid	sentence
15505410	Akt to the plasma membrane where it is phosphorylated and activated by phosphoinositide-dependent kinase (pdk) 1 and pdk2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-271852		Homo sapiens	HEK-293 Cell
pmid	sentence
21333377	Here, we demonstrate that overexpression of RFP2 in cells induced apoptosis through proteasomal degradation of MDM2 and AKT. We observed that RFP2 formed a complex with MDM2, a negative regulator of the p53 tumor suppressor, and AKT, a regulator of apoptosis inhibition at the cellular level. Additionally, we found that the interaction of RFP2 with MDM2 and AKT resulted in ubiquitination and proteasomal degradation of MDM2 and AKT in vivo and in vitro.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-217460		Homo sapiens	Thymoma Cell
pmid	sentence
19609947	Although there are likely to be multiple levels of crosstalk between the pi3k-akt and nf-kb pathways, one mechanism has been attributed to direct phosphorylation of the amino acid residue t23 on ikb kinase alfa (ikkalfa) by akt, thereby leading to activation of this kinase upstream of nf-kb akt mediates ikkalpha phosphorylation at threonine 23 akt transiently associates in vivo with ikk and induces ikk activation. Akt mediates ikkalfa phosphorylation at threonine 23.Akt phosphorylates ikkalpha on t23, and this phosphorylation event is a prerequisite for the phosphorylation of p65 at s534 by ikkalpha and beta

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism	Cell Line
SIGNOR-252638		Homo sapiens	Leukemia Cell
pmid	sentence
20596030	Exposure of eol-1r cells to imatinib failed to dephosphorylate akt, erk and stat5, although pdgfralpha was effectively inactivated. The forced expression of pten negatively regulated these signal pathways and sensitized eol-1r cells to imatinib.

Identifier	Residue	Organism	Cell Line
SIGNOR-189105		Homo sapiens	DU-145 Cell
pmid	sentence
19903340	PTEN-mediated suppression of the PI3K/AKT pathway is well established, accumulating evidence suggests that nuclear PTEN also plays a critical role in tumor suppression

Publications:

2

Organism:

Homo Sapiens

Pathways:

Glioblastoma Multiforme

Identifier	Residue	Organism
SIGNOR-252463		Homo sapiens
pmid	sentence
18801898	Akt/mTOR signaling is a key target that accounts for myostatin function during muscle atrophy, uncovering a novel role for myostatin in protein metabolism and more specifically in the regulation of translation in skeletal muscle.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-245402		Homo sapiens
pmid	sentence
23300340	Akt normally resides in the cytosol under serum-starved conditions, but translocates to the plasma membrane where it is subsequently phosphorylated and activated in response to growth factor treatment. Phosphorylation of Akt at Thr308 by phosphoinositide-dependent kinase-1 (PDK1) and at Ser473 by mammalian target of rapamycin (mTOR) complex 2 (mTORC2) is required for full Akt activation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252627		Mus musculus
pmid	sentence
12530968	The forkhead transcription factor foxo1 is regulated by insulin via akt-dependent phosphorylation and nuclear exclusion.

Publications:

1

Organism:

Mus Musculus

Pathways: