Relation Results

Acute Myeloid Leukemia, miRNA in AML, FLT3-ITD signaling, Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, Luminal Breast Cancer, Malignant Melanoma, Triple mutant AML, NPM1_new, Prostate Cancer, Pancreatic ductal adenocarcinoma (PDA)

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-174691	Ser129	SGSPSDNsGAEEMEV	Homo sapiens	HEK-293 Cell
pmid	sentence
21735093	CK2 hyperactivates AKT by phosphorylation at Ser129

Identifier	Residue	Organism	Cell Line
SIGNOR-244400		Homo sapiens	JURKAT Cell
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.

Publications:

2

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236216	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

Identifier	Residue	Sequence	Organism
SIGNOR-118053	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-140216	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-244389	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-244232	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-186130	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-244318	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-113669	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-262613	Ser16	ARRARSKsLVMGEQS	Homo sapiens	HEK-293 Cell
pmid	sentence
21969604	Akt phosphorylates RhoGAP22 at the 14-3-3 binding site and is required for insulin-stimulated 14-3-3 binding. we have demonstrated that Akt is the kinase responsible for phosphorylation of Ser16 in order to mediate 14-3-3 binding to RhoGAP22.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262631	Ser161	SFRRRHNsWSSSSRH	Cricetulus griseus	CHO Cell
pmid	sentence
20051463	Together these data show that recombinant EDC3 co-immunoprecipitates with endogenous 14-3-3 isoforms in response to insulin in vivo and is phosphorylated at the putative 14-3-3 binding and AKT phosphorylation site Ser-161. Collectively, these data suggest that Ser-161 in EDC3 is phosphorylated in response to insulin principally by AKT and that this subsequently triggers 14-3-3 binding. Constitutive 14-3-3 binding to EDC3 alters p-body morphology and function

Publications:

1

Organism:

Cricetulus Griseus

Identifier	Residue	Sequence	Organism
SIGNOR-244296	Ser166	SSRRRAIsETEENSD	Homo sapiens
pmid	sentence
15169778	Stabilization of mdm2 via decreased ubiquitination is mediated by protein kinase b/akt-dependent phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-244292	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.

Identifier	Residue	Sequence	Organism
SIGNOR-244300	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:

3

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-244236	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-244239		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

Pathways:

Acute Myeloid Leukemia, FLT3 in AML, COVID-19 Causal Network

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-209651	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:

Acute Myeloid Leukemia, COVID-19 Causal Network, FLT3-ITD signaling, Inhibition of Apoptosis, Malignant Melanoma, SARS-COV APOPTOSIS

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-161283	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

Pathways:

Hepatocellular Tumor

Identifier	Residue	Sequence	Organism
SIGNOR-151216	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-71480	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

Identifier	Residue	Sequence	Organism
SIGNOR-251473	Ser196	KLRRRFSsLHFMVEV	in vitro
pmid	sentence
9812896	Akt phosphorylated recombinant Casp9 in vitro on serine-196 and inhibited its protease activity.

Publications:

2

Organism:

Homo Sapiens, In Vitro

Pathways:

COVID-19 Causal Network, Inhibition of Apoptosis, SARS-COV APOPTOSIS

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251477	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
SIGNOR-251478	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.

Publications:

2

Organism:

Mus Musculus

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, FLT3-ITD in AML, FLT3-ITD signaling, NPM1_new, PI3K/AKT Signaling, Thyroid Hormone Metabolism

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252838	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-252826	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-252839	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-252827	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-252825	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-252836		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

Publications:

6

Organism:

Mus Musculus, Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-252828	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-252831	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-252829	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-252835	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-252832	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-252830	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-252824		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.

Identifier	Residue	Organism
SIGNOR-252834		Homo sapiens
pmid	sentence
18394876	The phosphorylation of the two remaining akt-dependent sites inhibits foxo6 transcriptional activity

Identifier	Residue	Organism	Cell Line
SIGNOR-252837		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-252820		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:

10

Organism:

Homo Sapiens, In Vitro, Mus Musculus

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, FLT3-ITD in AML, FLT3-ITD signaling, NPM1_new, PI3K/AKT Signaling, Thyroid Hormone Metabolism

Identifier	Residue	Sequence	Organism
SIGNOR-141416	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-141420	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-141424	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-174021		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:

4

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, ASXL1 in AML, Prostate Cancer

Identifier	Residue	Sequence	Organism
SIGNOR-179059	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-244259	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-83217	Ser21	SGRARTSsFAEPGGG	Homo sapiens
pmid	sentence
11035810	In response to insulin, gsk3a inhibited by phosphorylation at ser-21 by pkb/akt1;phosphorylation at this site causes a conformational change, preventing access of substrates to the active site.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-153323	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-244140	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

Pathways:

Prostate Cancer

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262616	Ser2233	LGRERLGsFGSITRQ	Mus musculus	C2C12 Cell
pmid	sentence
32444788	We identified the extended basophilic phosphosite motif RxRxxp[S/T]xxp[S/T] in various proteins including filamin-C (FLNc). Importantly, this extended motif, located in a unique insert in Ig-like domain 20 of FLNc, is doubly phosphorylated. The protein kinases responsible for this dual-site phosphorylation are Akt and PKCα. Proximity proteomics and interaction analysis identified filamin A-interacting protein 1 (FILIP1) as direct FLNc binding partner. FILIP1 binding induces filamin degradation, thereby negatively regulating its function. Here, dual-site phosphorylation of FLNc not only reduces FILIP1 binding, providing a mechanism to shield FLNc from FILIP1-mediated degradation, but also enables fast dynamics of FLNc necessary for its function as signaling adaptor in cross-striated muscle cells. In vitro kinase assays combined with LC-MS confirmed hFLNc-S2233 as a substrate of Akt, whereas PKCα preferentially targeted S2236.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276755	Ser224	EKSYRHRsAFIVHKR	Homo sapiens	NCI-H1299 Cell
pmid	sentence
31399647	We studied AKT-mediated phosphorylation sites, viz. Thr-150, Ser-224, Thr-234, and Thr-262. ZNF322A phosphorylation at Thr-262 by AKT promoted ZNF322A protein stability thus increased ADD1 promoter activity. Interestingly, phosphorylation at Thr-150, Ser-224, and Thr-234 enhanced transcription activity without affecting protein stability of ZNF322A.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276754	Thr150	LVHQRSHtGEKPYLC	Homo sapiens	NCI-H1299 Cell
pmid	sentence
31399647	We studied AKT-mediated phosphorylation sites, viz. Thr-150, Ser-224, Thr-234, and Thr-262. ZNF322A phosphorylation at Thr-262 by AKT promoted ZNF322A protein stability thus increased ADD1 promoter activity. Interestingly, phosphorylation at Thr-150, Ser-224, and Thr-234 enhanced transcription activity without affecting protein stability of ZNF322A.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276752	Thr234	IVHKRVHtGEKPYKC	Homo sapiens	NCI-H1299 Cell
pmid	sentence
31399647	We studied AKT-mediated phosphorylation sites, viz. Thr-150, Ser-224, Thr-234, and Thr-262. ZNF322A phosphorylation at Thr-262 by AKT promoted ZNF322A protein stability thus increased ADD1 promoter activity. Interestingly, phosphorylation at Thr-150, Ser-224, and Thr-234 enhanced transcription activity without affecting protein stability of ZNF322A.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276753	Thr262	IVHQRVHtGEKPYKC	Homo sapiens	NCI-H1299 Cell
pmid	sentence
31399647	We studied AKT-mediated phosphorylation sites, viz. Thr-150, Ser-224, Thr-234, and Thr-262. ZNF322A phosphorylation at Thr-262 by AKT promoted ZNF322A protein stability thus increased ADD1 promoter activity. Interestingly, phosphorylation at Thr-150, Ser-224, and Thr-234 enhanced transcription activity without affecting protein stability of ZNF322A.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-244361	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-244357	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

Pathways:

Hepatocellular Tumor, Pancreatic ductal adenocarcinoma (PDA)

Identifier	Residue	Sequence	Organism
SIGNOR-244311	Ser2448	RSRTRTDsYSAGQSV	Homo sapiens
pmid	sentence
10910062	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. These results demonstrate that mTOR is a direct target of the PI3K-AKT signaling pathway in mitogen-stimulated cells, and that the identified AKT phosphorylation sites are nested within a repressor domain that negatively regulates the catalytic activity of mTOR.¬†

Identifier	Residue	Sequence	Organism
SIGNOR-251482	Thr2446	NKRSRTRtDSYSAGQ	Homo sapiens
pmid	sentence
10910062	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. These results demonstrate that mTOR is a direct target of the PI3K-AKT signaling pathway in mitogen-stimulated cells, and that the identified AKT phosphorylation sites are nested within a repressor domain that negatively regulates the catalytic activity of mTOR.¬†

Publications:

2

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, miRNA in AML, FLT3-ITD in AML, FLT3-ITD signaling, Glioblastoma Multiforme, Leptin Signaling, MTOR Signaling, Pancreatic ductal adenocarcinoma (PDA)

Identifier	Residue	Sequence	Organism
SIGNOR-157467	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	Organism
SIGNOR-252821	Ser253	APRRRAVsMDNSNKY	Homo sapiens
pmid	sentence
19951971	AKT phosphorylates FOXO3a at three conserved sites (Thr32, Ser253 and Ser315), therefore creating binding sites for the 14-3-3 chaperone proteins and leading to the active export of FOXO3a to the cytoplasm where it is targeted for proteasomal degradation.

Identifier	Residue	Sequence	Organism
SIGNOR-252822	Ser315	DFRSRTNsNASTVSG	Homo sapiens
pmid	sentence
19951971	AKT phosphorylates FOXO3a at three conserved sites (Thr32, Ser253 and Ser315), therefore creating binding sites for the 14-3-3 chaperone proteins and leading to the active export of FOXO3a to the cytoplasm where it is targeted for proteasomal degradation.

Identifier	Residue	Sequence	Organism
SIGNOR-252823	Thr32	QSRPRSCtWPLQRPE	Homo sapiens
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-252833		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:

Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, FLT3-ITD in AML, FLT3-ITD signaling, NPM1_new, PI3K/AKT Signaling, Thyroid Hormone Metabolism

Identifier	Residue	Sequence
SIGNOR-249646	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-249647	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-249645	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:

FLT3 in AML, AMPK Signaling, Insulin Signaling, Inhibition of Apoptosis, Integrin Signaling, Thyroid cancer

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-183612	Ser253	APRRRAVsMDNSNKY	Homo sapiens	Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell
pmid	sentence
19188143	Akt-dependent phosphorylation of foxo3a (thr32, ser253, and ser315 for human foxo3) enhances foxo3a/14?3?3 Interaction and promotes foxo3a nuclear export to the cytoplasm, resulting in the repression of foxo3a transcriptional function

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-183616	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-183620	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
SIGNOR-261526		Mus musculus
pmid	sentence
14981546	Phosphorylation of Foxo proteins through FLT3-ITD signaling promotes their translocation from the nucleus into the cytoplasm, which requires the presence of conserved Akt phosphorylation sites in Forkhead transcription factors and PI3K activity.

Publications:

4

Organism:

Homo Sapiens, Mus Musculus

Pathways:

FLT3 in AML, AMPK Signaling, Insulin Signaling, Inhibition of Apoptosis, Integrin Signaling, Thyroid cancer

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252346	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. These results indicate that phosphorylation by PKB/Akt negatively regulates FKHR1 by promoting export from the nucleus.

Identifier	Residue	Sequence	Organism
SIGNOR-252349	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-252347	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-252350		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-252352		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-252348		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

Identifier	Residue	Organism	Cell Line
SIGNOR-277740		Homo sapiens	PANC-1 Cell
pmid	sentence
30519351	The results showed that TNC induced the cytoplasmic translocation of pFOXO1 via regulation of AKT activation. As shown in Fig. 3C, stimulation of PANC-1 cells with exogenous TNC markedly increased the phosphorylation of AKT and FOXO1. Our study showed that pFOXO1 translocates from the nucleus to the cell cytoplasm after exogenous TNC treatment, which indicates that its transcriptional activity was inhibited.

Publications:

7

Organism:

In Vitro, Homo Sapiens, Mus Musculus

Pathways:

FAP: Insulin-mediated adipogenesis, Insulin Signaling, Inhibition of Apoptosis, Leptin Signaling, Rhabdomyosarcoma, WNT/FLT3

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-244337	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	Sequence	Organism	Cell Line
SIGNOR-72669	Ser259	SQRQRSTsTPNVHMV	Homo sapiens	Myoblast
pmid	sentence
10576741	The stage-specific inhibitory action of Akt correlated with its stage-specific ability to form a complex with Raf, suggesting the existence of differentially expressed mediators of an inhibitory Akt-Raf complex.

Identifier	Residue	Organism
SIGNOR-244333		Homo sapiens
pmid	sentence
14967450	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:

COVID-19 Causal Network, Insulin Signaling, Integrin Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-244172	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-135105	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-244307	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-245304	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	Cell Line
SIGNOR-262615	Ser28	GQVPRTWsEKDLREL	Mus musculus	C2C12 Cell
pmid	sentence
18570922	CUG repeat binding protein, CUGBP1, is a key regulator of translation of proteins that are involved in muscle development and differentiation. In normal myoblasts, Akt kinase phosphorylates CUGBP1 at Ser28 and increases interactions of CUGBP1 with cyclin D1 mRNA.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-244206	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:

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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-201042	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-201046	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-196112	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	Cell Line
SIGNOR-251483	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-248027	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
SIGNOR-70205	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-72133	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-72137	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-155229	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-130920	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-244267	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	Organism	Cell Line
SIGNOR-249581	Ser316	ANRPRKSsVNGSSAT	Homo sapiens	Prostate Cancer Cell Line
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

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275836	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-244214	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-244218	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-114466	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-114470	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	Cell Line
SIGNOR-105927	Ser351	GRRGRLPsKPKQPPD	Homo sapiens	T-lymphocyte
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-145284	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-145288	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-145292	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-244152	Ser364	FGQRDRSsSAPNVHI	Homo sapiens
pmid	sentence
10869359	We show that phosphorylation of b-raf by akt occurs at multiple residues within its amino terminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity b-raf contains three akt consensus sites, table i. One site, ser364 is conserved with c-raf;however, two sites, ser428 and thr439, are unique to b-raf

Identifier	Residue	Sequence	Organism
SIGNOR-244160	Ser428	GPQRERKsSSSSEDR	Homo sapiens
pmid	sentence
10869359	We show that phosphorylation of b-raf by akt occurs at multiple residues within its amino terminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity b-raf contains three akt consensus sites, table i. One site, ser364 is conserved with c-raf;however, two sites, ser428 and thr439, are unique to b-raf

Identifier	Residue	Sequence	Organism
SIGNOR-244156	Thr440	EDRNRMKtLGRRDSS	Homo sapiens
pmid	sentence
10869359	We show that phosphorylation of b-raf by akt occurs at multiple residues within its amino terminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity b-raf contains three akt consensus sites, table i. One site, ser364 is conserved with c-raf;however, two sites, ser428 and thr439, are unique to b-raf

Publications:

3

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, AML_TRIPLETS, EGFR Signaling, ErbB receptors in cancer, FLT3-ITD signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Inhibition of Apoptosis, Luminal Breast Cancer, Malignant Melanoma, NPM1_new, Non-small-cell lung cancer (NSCLC), Pancreatic ductal adenocarcinoma (PDA), PI3K/AKT Signaling, Rhabdomyosarcoma, RTKs in cancer, Thyroid cancer, T cell activation, VEGF Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-178063	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
SIGNOR-162984	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-167971	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-271821	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-251480	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-251481	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-244271	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:

FAP: Insulin-mediated adipogenesis, Thyroid Hormone Metabolism

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-89696	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-244373	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

Pathways:

Acute Myeloid Leukemia, miRNA in AML

Identifier	Residue	Sequence	Organism
SIGNOR-181536	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	Cell Line
SIGNOR-265055	Ser432	THQGRSSsSGHYVSW	Homo sapiens	HEK-293 Cell
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-273825	Ser433	PMNTRRSsVGVGVVE	in vitro
pmid	sentence
26435498	Consistent with the fact that S433 is a component of Akt and PKA phosphorylation motifs, in vitro kinase assay demonstrated that Akt and PKA can phosphorylate KLHL3 at S433, that was previously reported to be phosphorylated by PKC.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262629	Ser45	ERMKRRSsASVSDSS	Homo sapiens	HeLa Cell
pmid	sentence
19162005	Akt phosphorylated GST-RGC-32 in vitro, and CDC2 was also able to phosphorylate RGC-32. Akt failed to phosphorylate RGC-32 S45A-S47A mutant. These data indicate that Ser 45 and Ser 47 may be the RGC-32 phosphorylation sites for Akt kinase.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262628	Ser47	MKRRSSAsVSDSSGF	Homo sapiens	HeLa Cell
pmid	sentence
19162005	Akt phosphorylated GST-RGC-32 in vitro, and CDC2 was also able to phosphorylate RGC-32. Akt failed to phosphorylate RGC-32 S45A-S47A mutant. These data indicate that Ser 45 and Ser 47 may be the RGC-32 phosphorylation sites for Akt kinase.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273539	Ser451	QEKSPGTsPLLSRKM	Homo sapiens	HEK-293 Cell
pmid	sentence
26932461	This strongly suggested that Akt dependent phosphorylation of LARP6 targets S451.S451A mutant of LARP6 acts as dominant negative protein in collagen synthesis. these results support the hypothesis that phosphorylation of S451 by Akt is a necessary step to activate productive synthesis type I collagen and suggests that secretion and modifications of type I collagen are impaired if LARP6 is not phosphorylated on S451.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-245259	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-143098	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-150140	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-160982	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-137241	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

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248031	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-71419	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
SIGNOR-192260	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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-103462	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.

Publications:

4

Organism:

Homo Sapiens

Tissue:

Heart

Pathways:

AMPK Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251484	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-251485	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

Pathways:

AMPK Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262619	Ser472	SRLRRRAsQLKITIP	Homo sapiens	HEK-293 Cell
pmid	sentence
12818177	Here we report that Akt phosphorylates, both in vitro and in vivo, the type A gamma-aminobutyric acid receptor (GABA(A)R), the principal receptor mediating fast inhibitory synaptic transmission in the mammalian brain. Akt-mediated phosphorylation increases the number of GABA(A)Rs on the plasma membrane surface, thereby increasing the receptor-mediated synaptic transmission in neurons. These results identify the GABA(A)R as a novel substrate of Akt, thereby linking Akt to the regulation of synaptic strength.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248502	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

Pathways:

COVID-19 Causal Network

Identifier	Residue	Sequence	Organism
SIGNOR-60115	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

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-256269	Ser473	RPHFPQFsYSASGTA	Rattus norvegicus
pmid	sentence
11782444	Here it is shown that WISP-1 can activate the antiapoptotic Akt/PKB signaling pathway.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-250261	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

Pathways:

FLT3-ITD signaling, mTOR in cancer, MTOR Signaling, PI3K/AKT Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-217008	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-252451	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-252448	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-252454	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

Identifier	Residue	Organism
SIGNOR-251982		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	Organism	Cell Line
SIGNOR-251983		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.

Publications:

6

Organism:

Homo Sapiens, Mus Musculus

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-205115	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

Identifier	Residue	Organism	Cell Line
SIGNOR-244410		Homo sapiens	Neuron
pmid	sentence
21658387	Lrrk2 directly phosphorylates akt1 as a possible physiological substrate. These data establish that lrrk2 can protect neurons from apoptotic insult through a survival pathway in which lrrk2 signals to activate akt. Lrrk2-mediated phosphorylation of akt1 (ser473)

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-135046	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-172132	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

Pathways:

COVID-19 Causal Network, EBV infection, Inflammosome Activation, SARS-CoV INFLAMMATORY RESPONSE

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-134185	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	Organism	Cell Line
SIGNOR-244417		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.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, miRNA in AML, FLT3-ITD in AML, FLT3-ITD signaling, Glioblastoma Multiforme, Leptin Signaling, MTOR Signaling, Pancreatic ductal adenocarcinoma (PDA)

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252447	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

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-135005	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
SIGNOR-248627	Ser473	RPHFPQFsYSASGTA	Mus musculus
pmid	sentence
15367694	Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248629	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

Identifier	Residue	Organism
SIGNOR-248655		Homo sapiens
pmid	sentence
18160256	Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A.

Publications:

3

Organism:

Mus Musculus, Homo Sapiens

Pathways:

COVID-19 Causal Network, PI3K/AKT Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248559	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-248575	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
SIGNOR-170699	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	Cell Line
SIGNOR-252450	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-252453	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
SIGNOR-262623	Ser486	GLETRRLsLPSSKAK	in vitro
pmid	sentence
17256767	These data define a new protein complex in mammalian cells where 14‐3‐3 associates with FAKTS through phosphorylated S479. Our research identifies a widely expressed eukaryotic protein FAKTS, as a new Akt/PKB substrate localized in the nucleus. Akt/PKB promotes FAKTS association with 14‐3‐3, placing FAKTS under the control of 14‐3‐3 proteins. FAKTS may play an important role in transmitting Akt/PKB‐mediated signals in the complex network of intracellular signal transduction.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235411	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

Pathways:

Acute Myeloid Leukemia, FLT3 in AML, FLT3-ITD in AML, FLT3-ITD signaling, Hepatocellular Tumor, Pancreatic ductal adenocarcinoma (PDA), Rhabdomyosarcoma, Thyroid cancer, WNT/FLT3

Identifier	Residue	Sequence	Organism
SIGNOR-137430	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-244222	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-141343	Ser554	SIRPRPGsLRSKPEP	Homo sapiens
pmid	sentence
16256741	Akt phosphorylates s554 in acap1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276150	Ser57	HGTGHPEsAGEHALE	Homo sapiens	HEK-293 Cell
pmid	sentence
18280241	Akt phosphorylates RanBP3 at Serine 58 residue in vitro and in vivo. RanBP3 phosphorylation increases its affinity towards Ran

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-155532	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

Pathways:

AMPK Signaling, MTOR Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266361	Ser577	TKRKRENsLQEDRGS	Homo sapiens	U2-OS Cell
pmid	sentence
28954236	AKT phosphorylation of cyclin F enhances its stability and promotes assembly into productive E3 ligase complexes.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266360	Thr31	RRRPRNLtILSLPED	Homo sapiens	U2-OS Cell
pmid	sentence
28954236	AKT phosphorylation of cyclin F enhances its stability and promotes assembly into productive E3 ligase complexes.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-244381	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	Cell Line
SIGNOR-245268	Ser588	RMRGRLGsVDSFERS	Mus musculus	3T3-L1 Cell
pmid	sentence
11994271	To determine directly whether AS160 was a substrate for Akt, we examined the phosphorylation of recombinant AS160, as well as mutant forms with Ser-588, Thr-642, or both converted to Ala, by recombinant Akt 1.

Identifier	Residue	Sequence	Organism
SIGNOR-148342	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:

2

Organism:

Mus Musculus, Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262627	Ser59	SSSVRLGsFRSPRAG	Homo sapiens	HEK-293 Cell
pmid	sentence
17569669	Here we demonstrate that peripherin, which is a peripheral nervous system neuron-specific intermediate filament protein, is a novel Akt substrate, and that Ser66 of peripherin is the phosphorylation site. Peripherin phosphorylation is apparently induced in motor neurons after nerve injury, suggesting that the Akt-mediated peripherin phosphorylation may play a role in motor nerve regeneration.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251487	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-248042	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-199254	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-95247	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-197053	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-251628	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

Pathways:

VEGF Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-168169	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-96062	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	Cell Line
SIGNOR-244164	Ser694	QTSKRHDsDTFPELK	Homo sapiens	Breast Cancer Cell
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-244168	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

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248036	Ser71	YDRLRPLsYPQTDVF	Homo sapiens	SK-MEL-2 Cell
pmid	sentence
10617634	The results suggest that Akt kinase of the phosphoinositide 3-kinase signal transduction pathway phosphorylates serine 71 of Rac1 as one of its authentic substrates and modulates the Rac1 signal transduction pathway through phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3-ITD in AML, WNT/FLT3

Identifier	Residue	Sequence	Organism
SIGNOR-244353	Ser719	AEKEAATsELQSIQR	Homo sapiens
pmid	sentence
25595898	We have identified TBX3 as a key substrate of AKT3 in melanomagenesis. we have identified the AKT3 target site at serine residue 720 in the TBX3 protein and show that this site is phosphorylated in vivo. the phosphorylation at S720 promotes TBX3 protein stability, nuclear localization, transcriptional repression of E-cadherin, and its role in cell migration and invasion.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247997	Ser766	VTRTRSLsACNKRVG	Rattus norvegicus	Adipocyte
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-251468	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-244136	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:

1

Organism:

Chlorocebus Aethiops

Pathways:

Prostate Cancer

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-244285	Ser80	IERLRTHsIESSGKL	Homo sapiens	HEK-293 Cell
pmid	sentence
11707464	Akt phosphorylated sek1 on serine 78.

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, EGFR Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275980	Ser80	IERLRTHsIESSGKL	Homo sapiens	HEK-293T Cell
pmid	sentence
11707464	Akt (Protein Kinase B) Negatively Regulates SEK1 by Means of Protein Phosphorylation. In vitro and in vivo (32)P labeling indicated that Akt phosphorylated SEK1 on serine 78. The SEK1 mutant SEK1(S78A) was resistant to Akt-induced inhibition.

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, EGFR Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-186772	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-104646	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

Identifier	Residue	Sequence	Organism
SIGNOR-141581	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

Pathways:

COVID-19 Causal Network, Inhibition of Apoptosis, SARS-COV APOPTOSIS

Identifier	Residue	Sequence	Organism
SIGNOR-244377	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:

Inhibition of Apoptosis

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

Identifier	Residue	Sequence	Organism
SIGNOR-245428	Ser9	SGRPRTTsFAESCKP	Homo sapiens
pmid	sentence
23552696	Active AKT, a common mediator of cell survival signals induced by radiation through multiple intracellular signaling pathways,11, 12 suppresses apoptosis. AKT positively regulates cyclin D1 expression through inactivation of glycogen synthase kinase 3_ (GSK3_). The AKT-mediated phosphorylation of glycogen synthase kinase 3_ on serine9 decreases its kinase activity for Thr286 of cyclin D1, which inhibits the nuclear export and the cytoplasmic proteasomal degradation of cyclin D1

Publications:

2

Organism:

Homo Sapiens

Pathways:

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

Identifier	Residue	Sequence	Organism
SIGNOR-244385	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-244369	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-244365	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	Cell Line
SIGNOR-143721	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

Pathways:

Acute Myeloid Leukemia, ASXL1 in AML

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-244132	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-248008	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-266357	Thr1033	RLGERLRtMSCSDKI	in vitro
pmid	sentence
31095429	AKT-dependent phosphorylation of the adenosine deaminases ADAR-1 and -2 inhibits deaminase activity. Using site-directed mutagenesis of suspected AKT phosphorylation sites, AKT was found to primarily phosphorylate ADAR1p110 and ADAR2 on T738 and T553, respectively, and overexpression of the phosphomimic mutants ADAR1p110 (T738D) and ADAR2 (T553D) resulted in a 50-100% reduction in editase activity.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-164298	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-244345	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
SIGNOR-244349	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-161829	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-201121	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	Organism	Cell Line
SIGNOR-248085	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
SIGNOR-244180	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.

Identifier	Residue	Sequence	Organism
SIGNOR-244184	Thr145	QGRKRRQtSMTDFYH	Homo sapiens
pmid	sentence
16982699	Whereas akt1 phosphorylates p21, inducing its release from cdk2 and cytoplasmic localization as previously described for akt.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3-ITD in AML, FLT3-ITD signaling, Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, Rhabdomyosarcoma

Identifier	Residue	Sequence	Organism
SIGNOR-254974	Thr156	KTYRRSYtHAKPPYS	Homo sapiens
pmid	sentence
14500912	Foxa-2 physically interacts with Akt, a key mediator of the phosphatidylinositol 3-kinase pathway and is phosphorylated at a single conserved site (T156) that is absent in Foxa-1 and Foxa-3 proteins. This Akt phosphorylation site in Foxa-2 is highly conserved from mammals to insects. Mutant Foxa-2T156A is resistant to Akt-mediated phosphorylation, nuclear exclusion, and transcriptional inactivation of Foxa-2-regulated gene expression.

Publications:

1

Organism:

Homo Sapiens

Pathways:

FAP: Insulin-mediated adipogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-244202	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-244194	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.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, Integrin Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-199776	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-252035	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
SIGNOR-179054	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-244210	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-242092	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-110845	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-236929	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

Pathways:

MTOR Signaling

Identifier	Residue	Sequence
SIGNOR-250714	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

Identifier	Residue	Sequence	Organism
SIGNOR-144808	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	Organism
SIGNOR-243203	Thr308	KDGATMKtFCGTPEY	Homo sapiens
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.

Identifier	Residue	Sequence	Organism
SIGNOR-134477	Thr308	KDGATMKtFCGTPEY	Mus musculus
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-244480	Thr308	KDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
9512493	The activation of PKBbeta and PKBamma by PDK11 was accompanied by the phosphorylation of the residues equivalent to Thr308 in PKBalpha, namely Thr309 (PKBbeta) and Thr305 (PKBgamma)

Identifier	Residue	Sequence	Organism
SIGNOR-244421	Thr308	KDGATMKtFCGTPEY	Rattus norvegicus
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.

Identifier	Residue	Organism
SIGNOR-244469		Homo sapiens
pmid	sentence
15743829	3-phosphoinositide-dependent kinase 1 (PDK1) phosphorylates the activation loop of a number of protein serine/threonine kinases of the AGC kinase superfamily, including protein kinase B (PKB; also called Akt),

Publications:

5

Organism:

Homo Sapiens, Mus Musculus, Rattus Norvegicus

Tissue:

Muscle, Skeletal Muscle, Myotube, Brain

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, miRNA in AML, AMPK Signaling, B-cell activation, EGFR Signaling, ErbB receptors in cancer, FAP: Insulin-mediated adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, Luminal Breast Cancer, mTOR in cancer, Malignant Melanoma, MTOR Signaling, Non-small-cell lung cancer (NSCLC), Prostate Cancer, PI3K/AKT Signaling, Rhabdomyosarcoma, RTKs in cancer, Thyroid cancer, T cell activation, VEGF Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252455	Thr312	TMKTFCGtPEYLAPE	Mus musculus	Th17 Cell
pmid	sentence
23142783	GSK3_ negatively regulates AKT activation by phosphorylating AKT at T312 in the substrate binding site, which inhibited IL-1-induced AKT activation and function.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-177019	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	Cell Line
SIGNOR-265102	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-244176	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

Identifier	Residue	Sequence	Organism
SIGNOR-114767	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

Pathways:

COVID-19 Causal Network, PI3K/AKT Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-188969	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-267576	Thr473	QHRARQKtLEHLQLS	Homo sapiens	Cardiomyocyte Cell Line
pmid	sentence
25323588	Hexokinase II is phosphorylated by Akt leading to increased mitochondrial binding and mitochondrial protection.We found that Akt, activated by receptor agonists, translocates to mitochondria and phosphorylates HK-II at Thr473, a critical step in Akt-mediated mitoHK-II increase and protection in cardiomyocytes

Identifier	Residue	Organism	Cell Line
SIGNOR-259985		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:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-244341	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-266358	Thr553	LQGERLLtMSCSDKI	in vitro
pmid	sentence
31095429	AKT-dependent phosphorylation of the adenosine deaminases ADAR-1 and -2 inhibits deaminase activity. Using site-directed mutagenesis of suspected AKT phosphorylation sites, AKT was found to primarily phosphorylate ADAR1p110 and ADAR2 on T738 and T553, respectively, and overexpression of the phosphomimic mutants ADAR1p110 (T738D) and ADAR2 (T553D) resulted in a 50-100% reduction in editase activity.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-244263	Thr567	QGRDKYKtLRQIRQG	Homo sapiens
pmid	sentence
15531580	Purified akt directly phosphorylates recombinant ezrin at threonine 567 in vitro in an atp-dependent manner. ezrin activation after initiation of na+-glucose cotransport requires akt2 expression

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-139391	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-275723	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	Cell Line
SIGNOR-259816	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
SIGNOR-251479	Thr779	LYKEATStFTNITYR	in vitro
pmid	sentence
10896934	Threonine phosphorylation of the beta 3 integrin cytoplasmic tail, at a site recognized by PDK1 and Akt/PKB in vitro, regulates Shc binding.\|We recently observed that phosphorylation of a threonine (Thr-753), six amino acids proximal to tyrosine 759 in beta(3) of the platelet specific integrin alpha(IIb)beta(3), inhibits outside-in signaling through this receptor.\| A survey of several protein kinases revealed that Thr-753 was avidly phosphorylated by PDK1 and Akt/PKB in vitro.

Publications:

1

Organism:

In Vitro

Pathways:

EGFR Signaling, Integrin Signaling, Rhabdomyosarcoma

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-137942	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-252457	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

Tissue:

Prostate Adenocarcinoma Cell

Identifier	Residue	Sequence	Organism
SIGNOR-166514	Tyr315	TFCGTPEyLAPEVLE	Homo sapiens
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

Identifier	Residue	Organism
SIGNOR-244443		Homo sapiens
pmid	sentence
12242309	Overexpressed rai resulted in the potentiation of the ret-dependent activation of phosphatidylinositol 3-kinase (pi3k) and akt. The ret/ptc receptor tyrosine kinase that responds to glial cell-line-derived neurotrophic factor also phosphorylated akt tyrosine residue 315 promoting activation of akt

Publications:

2

Organism:

Homo Sapiens

Pathways:

Thyroid cancer

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246373	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-246368	Tyr315	TFCGTPEyLAPEVLE	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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246377	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:

Homo Sapiens, Chlorocebus Aethiops

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-138437	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-166506	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-166510	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	Organism
SIGNOR-261215		Mus musculus
pmid	sentence
24663380	Ano6 deficiency significantly reduces ERK/AKT phosphorylation. In addition, Ano6-KD also affected levels of phosphorylated and total AKT levels.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism	Cell Line
SIGNOR-244187		Homo sapiens	Myoblast
pmid	sentence
16982699	More importantly, the consequences of phosphorylation of either Thr145 or Ser146 are distinct. When p21 is phosphorylated on Thr145, it localizes to the nucleus and results in the disruption of the association between proliferating cell nuclear antigen and p21. Furthermore, phosphorylation of Thr145 promotes stabilization of p21

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3-ITD in AML, FLT3-ITD signaling, Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, Rhabdomyosarcoma

Identifier	Residue	Organism	Cell Line
SIGNOR-244406		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-98811		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-244314		Homo sapiens
pmid	sentence
12782654	It was shown recently that akt activates mtor through direct phosphorylation of tsc2 the serine/threonine kinase akt is an upstream positive regulator of the mammalian target of rapamycin (mtor). However, the mechanism by which akt activates mtor is not fully understood. The known pathway by which akt activates mtor is via direct phosphorylation and tuberous sclerosis complex 2 (tsc2), which is a negative regulator of mtor.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, miRNA in AML, FLT3-ITD in AML, FLT3-ITD signaling, Glioblastoma Multiforme, Leptin Signaling, MTOR Signaling, Pancreatic ductal adenocarcinoma (PDA)

Identifier	Residue	Organism
SIGNOR-132959		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

Pathways:

FLT3-ITD signaling, Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition

Identifier	Residue	Organism
SIGNOR-251552		Homo sapiens
pmid	sentence
16697957	NKX3.1 negatively regulates AKT activity in an AR-dependent manner

Publications:

1

Organism:

Homo Sapiens

Pathways:

Prostate Cancer

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-255493
pmid	sentence
26721223	Excessive accumulation of Aβ protein in the AD brain may lead to a decrease in the levels of phosphatidylinositol-3 kinase (PI3K) and the serine/threonine protein kinase B (Akt) activity.

Publications:

1

Identifier	Residue	Organism
SIGNOR-244455		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	Cell Line
SIGNOR-243526		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 \|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-256212		Mus musculus
pmid	sentence
21723501	MTORC1 activation is not sufficient to stimulate hepatic SREBP1c in the absence of Akt signaling, revealing the existence of an additional downstream pathway also required for this induction. We provide evidence that this mTORC1-independent pathway involves Akt-mediated suppression of Insig2a, a liver-specific transcript encoding the SREBP1c inhibitor INSIG2.

Publications:

1

Organism:

Mus Musculus

Tissue:

Liver

Identifier	Residue	Organism
SIGNOR-244392		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-244465		Homo sapiens
pmid	sentence
12181443	We show [] that the kinase activity and s473 phosphorylation of akt induced by lpa and s1p requires both mitogen-activated protein (map) kinase kinase (mek) and p38 map kinase. [] among different stimuli tested, platelet-derived growth factor stimulates s473 phosphorylation of akt in a mek- and p38-dependent manner. However, epidermal growth factor, thrombin, and endothelin-1?stimulated Akt s473 phosphorylation require p38 but not mek.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, ASXL1 in AML, BCR-ABL in AML, FLT3 in AML, KIT in AML, B-cell activation, COVID-19 Causal Network, EBV infection, ErbB receptors in cancer, FAP: Insulin-mediated adipogenesis, FLT3-ITD in AML, FLT3-ITD signaling, Hepatocellular Tumor, Inflammosome Activation, Integrin Signaling, Leptin Signaling, mTOR in cancer, Non-small-cell lung cancer (NSCLC), Pancreatic ductal adenocarcinoma (PDA), PI3K/AKT Signaling, RTKs in cancer, SARS-CoV INFLAMMATORY RESPONSE, T cell activation, Thyroid Hormone Metabolism, VEGF Signaling, WNT/FLT3

Identifier	Residue	Organism	Cell Line
SIGNOR-243530		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	Organism
SIGNOR-254950		Homo sapiens
pmid	sentence
15526160	C-Kit promotes survival via PI3-kinase-dependent activation of Akt and phosphorylation of Bad, a pro-apoptotic molecule, at S136 in vivo.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism	Cell Line
SIGNOR-244449		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	Cell Line
SIGNOR-248331		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	Organism
SIGNOR-173976		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.

Identifier	Residue	Organism
SIGNOR-244228		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.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-75370		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	Cell Line
SIGNOR-254952		Homo sapiens	Mast Cell
pmid	sentence
15526160	c-Kit promotes survival via PI3-kinase-dependent activation of Akt and phosphorylation of Bad, a pro-apoptotic molecule, at S136 in vivo.

Identifier	Residue	Organism
SIGNOR-251550		Homo sapiens
pmid	sentence
16288293	Akt promotes both cell growth and cell survival by inactivating its downstream substrates including GSK3, BAD, FOXO and TSC2.

Publications:

2

Organism:

Homo Sapiens

Pathways:

ErbB receptors in cancer, Glioblastoma Multiforme, Hepatocellular Tumor, Inhibition of Apoptosis, Luminal Breast Cancer, Malignant Melanoma, Non-small-cell lung cancer (NSCLC), Prostate Cancer, Pancreatic ductal adenocarcinoma (PDA), PI3K/AKT Signaling, Rhabdomyosarcoma, RTKs in cancer, Thyroid cancer

Identifier	Residue	Organism
SIGNOR-257606		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.

Identifier	Residue	Organism
SIGNOR-254353		Mus musculus
pmid	sentence
16982699	Protein kinase B (PKB/Akt) is an important modulator of insulin signaling, cell proliferation, and survival. Using small interfering RNA duplexes in nontransformed mammalian cells, we show that only Akt1 is essential for cell proliferation

Publications:

2

Organism:

Homo Sapiens, Mus Musculus

Pathways:

Acute Myeloid Leukemia, ASXL1 in AML, BCR-ABL in AML, FLT3 in AML, KIT in AML, miRNA in AML, AML_TRIPLETS, AMPK Signaling, B-cell activation, COVID-19 Causal Network, EGFR Signaling, EBV infection, ErbB receptors in cancer, FLT3-ITD in AML, FLT3-ITD signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, Integrin Signaling, Luminal Breast Cancer, Leptin Signaling, mTOR in cancer, Malignant Melanoma, Triple mutant AML, NPM1_new, Non-small-cell lung cancer (NSCLC), Prostate Cancer, Pancreatic ductal adenocarcinoma (PDA), PI3K/AKT Signaling, Rhabdomyosarcoma, RTKs in cancer, Thyroid cancer, VEGF Signaling, WNT/FLT3

Identifier	Residue	Organism
SIGNOR-129965		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
SIGNOR-123239		Homo sapiens
pmid	sentence
15004527	Akt may serve to stimulate certain proteins (e.g., Ikk) involved in the prevention of apoptosis such as nf-kb as well as repress other proteins normally involved in the induction of apoptosis such as the forkhead transcription factors (fkhr, now know as foxo3), creb, glycogen synthetase-3 kinase-beta (gsk-3beta), fas, caspase-9 and cell cycle inhibitors such as p27

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, SARS-COV APOPTOSIS

Identifier	Residue	Organism	Cell Line
SIGNOR-260200		Homo sapiens	HEK-293FT Cell
pmid	sentence
25271362	Consistent with our previous result, we detected a reduced phosphorylated PKB/Akt level and diminished PKB/Akt activity in mammalian cells expressing M-protein.

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, SARS-COV APOPTOSIS, SARS-CoV INFLAMMATORY RESPONSE

Identifier	Residue	Organism
SIGNOR-200875		Homo sapiens
pmid	sentence
23400686	Furthermore, akt promotes cell cycle progression through downregulation of the cyclin dependent kinase inhibitor p27kip1.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, Integrin Signaling

Identifier	Residue	Organism
SIGNOR-244396		Homo sapiens
pmid	sentence
21798082	Positive feedback involves mtorc2, which phosphorylates akt at serine 473, a phosphorylation required for maximum activation of akt in addition to phosphorylation at threonine 308 by pdk1.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, miRNA in AML, AMPK Signaling, B-cell activation, EGFR Signaling, ErbB receptors in cancer, FAP: Insulin-mediated adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, Luminal Breast Cancer, mTOR in cancer, Malignant Melanoma, MTOR Signaling, Non-small-cell lung cancer (NSCLC), Prostate Cancer, PI3K/AKT Signaling, Rhabdomyosarcoma, RTKs in cancer, Thyroid cancer, T cell activation, VEGF Signaling

Identifier	Residue	Organism
SIGNOR-75376		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	Cell Line
SIGNOR-237850		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	Cell Line
SIGNOR-266604		Homo sapiens	Endothelial Cell, Cardiac Muscle Fiber
pmid	sentence
18718903	In this study, Fstl1 was shown to activate Akt signaling in cardiac myocytes and inhibit apoptosis. Thus, Fstl1 can function as a survival factor for both cardiac myocytes and endothelial cells via the activation of Akt signaling.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-272499		Homo sapiens
pmid	sentence
35186726	ITLN1 increases Akt phosphorylation in adipocytes, osteoblasts, and mesenchymal cells. \|n mesenchymal stem cells, ITLN1 also leads to Akt-mediated proliferation, resistance to oxidative stress, and secretion of proangiogenic factors

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-255339		Homo sapiens
pmid	sentence
19357233	In the current study, it was demonstrated that myostatin inhibits activation of Akt, in both myoblasts and myotubes.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-236490		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-236509		Homo sapiens
pmid	sentence
23119004	Binding of IGF to IGF-1R activates PI3K to generate PIP3 which in turn recruits and activates proteins that contain a pleckstrin homology ph) domain, including AKT and PDK1.

Publications:

2

Organism:

Homo Sapiens

Tissue:

Prostate Gland Cancer Cell

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, miRNA in AML, AMPK Signaling, B-cell activation, EGFR Signaling, ErbB receptors in cancer, FAP: Insulin-mediated adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, mTOR in cancer, Malignant Melanoma, MTOR Signaling, Non-small-cell lung cancer (NSCLC), Prostate Cancer, Pancreatic ductal adenocarcinoma (PDA), PI3K/AKT Signaling, RTKs in cancer, Thyroid cancer, T cell activation, VEGF Signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-244403		Mus musculus	C2C12 Cell
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:

EBV infection, Hepatocellular Tumor, Non-small-cell lung cancer (NSCLC), Rhabdomyosarcoma

Identifier	Residue	Organism
SIGNOR-269944		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:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-205977		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-148675		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

Pathways:

Acute Myeloid Leukemia, FLT3 in AML, miRNA in AML

Identifier	Residue	Organism	Cell Line
SIGNOR-255942		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

Pathways:

Identifier	Residue	Organism
SIGNOR-97392		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:

AMPK Signaling, FAP: Insulin-mediated adipogenesis, Insulin Signaling, Luminal Breast Cancer, Leptin Signaling, mTOR in cancer, MTOR Signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-252459		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	Cell Line
SIGNOR-260961		Homo sapiens	Colorectal Cancer Cell Line
pmid	sentence
30518405	We further demonstrated that IMPDH2 overexpression accelerated G1/S phase cell cycle transition by inducing increased expression of cyclin D1 and Ki-67 and downregulation of p21Cip1 and p27Kip1. More importantly, G1/S phase cell cycle transition was triggered by IMPDH2 through activation of AKT activity, downregulation of mTOR and FOXO1 transcriptional activity. There is evidence that IMPDH2 interacts with the pleckstrin homology domain of PKB/AKT in the regulation of GTP biosynthesis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-275408		Homo sapiens	T-lymphocyte
pmid	sentence
16227604	Akt phosphorylation in cells stimulated by CD3/CD28/CTLA-4 or CD3/CD28/PD-1 aAPCs did not have detectable phosphorylated Akt at any time point, indicating that CTLA-4 and PD-1 signaling blocked rather than delayed Akt activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-143700		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

Pathways:

Pancreatic ductal adenocarcinoma (PDA)

Identifier	Residue	Organism
SIGNOR-261135		Homo sapiens
pmid	sentence
31609475	In our results, we also showed that re-expression of MIPOL1 is associated with suppression phosphorylation of AKT and p65, a subunit of NF-ҡB. This suggests that MIPOL1 may inhibit invasion by suppression of phosphorylation of AKT and p65 to further inhibit the expression of MMP-9

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252740		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:

1

Organism:

In Vitro

Identifier	Residue	Organism	Cell Line
SIGNOR-252351		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

Publications:

1

Organism:

Mus Musculus

Pathways:

FAP: Insulin-mediated adipogenesis, Insulin Signaling, Inhibition of Apoptosis, Leptin Signaling, Rhabdomyosarcoma, WNT/FLT3

Identifier	Residue	Organism
SIGNOR-259029		Homo sapiens
pmid	sentence
22085529	Both mitogen-activated protein kinase (MAPK)/extracellular-signal-regulated kinases (ERK) 1/2 and phosphatidylinositide-3-OH kinase (PI3K)/Akt pathways regulate activation of E-twenty-six (ETS)-like transcription factor 1 (Elk-1) in U138 glioblastoma cells. The phosphatidylinositide-3-OH kinase (PI3K)/Akt pathway was also involved in the Elk-1 activation. Activation of the Elk-1 led to an increased survival and a proliferative response with the EGF stimulation in the U138 glioblastoma cells.

Publications:

1

Organism:

Homo Sapiens

Pathways:

EGFR Signaling, Glioblastoma Multiforme, Integrin Signaling

Identifier	Residue	Organism
SIGNOR-174017		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:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-193000		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-244303		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

Identifier	Residue	Organism
SIGNOR-243185		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-66032		Homo sapiens
pmid	sentence
18394876	The phosphorylation of the two remaining akt-dependent sites inhibits foxo6 transcriptional activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-256211		Mus musculus
pmid	sentence
21723501	MTORC1 activation is not sufficient to stimulate hepatic SREBP1c in the absence of Akt signaling, revealing the existence of an additional downstream pathway also required for this induction. We provide evidence that this mTORC1-independent pathway involves Akt-mediated suppression of Insig2a, a liver-specific transcript encoding the SREBP1c inhibitor INSIG2.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-254982		Rattus norvegicus
pmid	sentence
8645147	Activated hyperphosphorylated Akt-1 bound to Ptd Ins(3,4,5)P3 -containing vesicles in a similar manner to the inactive dephosphorylated enzyme

Publications:

1

Organism:

Rattus Norvegicus

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, miRNA in AML, AMPK Signaling, B-cell activation, EGFR Signaling, ErbB receptors in cancer, FAP: Insulin-mediated adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, mTOR in cancer, Malignant Melanoma, MTOR Signaling, Non-small-cell lung cancer (NSCLC), Prostate Cancer, Pancreatic ductal adenocarcinoma (PDA), PI3K/AKT Signaling, RTKs in cancer, Thyroid cancer, T cell activation, VEGF Signaling

Identifier	Residue	Organism
SIGNOR-256446		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
SIGNOR-254978		Homo sapiens
pmid	sentence
14500912	�Foxa-2 physically interacts with Akt, a key mediator of the phosphatidylinositol 3-kinase pathway and is phosphorylated at a single conserved site (T156) that is absent in Foxa-1 and Foxa-3 proteins. This Akt phosphorylation site in Foxa-2 is highly conserved from mammals to insects. Mutant Foxa-2T156A is resistant to Akt-mediated phosphorylation, nuclear exclusion, and transcriptional inactivation of Foxa-2-regulated gene expression.

Publications:

1

Organism:

Homo Sapiens

Pathways:

FAP: Insulin-mediated adipogenesis

Identifier	Residue	Organism
SIGNOR-217586		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	Cell Line
SIGNOR-252817		Mus musculus	3T3-L1 Cell
pmid	sentence
19593385	In examining the requirements for different Akt-mediated phosphorylation sites on TSC2, we find that only TSC2 mutants lacking all five previously identified Akt sites fully block insulin-stimulated mTORC1 signaling in reconstituted Tsc2 null cells, and this mutant also inhibits adipogenesis

Publications:

2

Organism:

Homo Sapiens, Mus Musculus

Tissue:

Muscle, Skeletal Muscle, Myotube

Pathways:

AMPK Signaling, EGFR Signaling, Glioblastoma Multiforme, Insulin Signaling, Luminal Breast Cancer, mTOR in cancer, Pancreatic ductal adenocarcinoma (PDA), PI3K/AKT Signaling, Thyroid Hormone Metabolism, WNT/FLT3

Identifier	Residue	Organism
SIGNOR-244458		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:

COVID-19 Causal Network, EBV infection, Inflammosome Activation, Inhibition of Apoptosis, MTOR Signaling, SARS-COV APOPTOSIS, SARS-CoV INFLAMMATORY RESPONSE, Thyroid Hormone Metabolism

Identifier	Residue	Organism	Cell Line
SIGNOR-261522		Mus musculus	BA/F3 Cell
pmid	sentence
14981546	These data confirm previous findings that FLT3 receptors with ITD mutations efficiently trigger the activation of ERK, STAT5 and Akt in the absence of FL stimulation.

Publications:

1

Organism:

Mus Musculus

Pathways:

Acute Myeloid Leukemia, ASXL1 in AML, FLT3 in AML, miRNA in AML, AML_TRIPLETS, FLT3-ITD in AML, FLT3-ITD signaling, Triple mutant AML, NPM1_new, WNT/FLT3

Identifier	Residue	Organism	Cell Line
SIGNOR-248732		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	Organism	Cell Line
SIGNOR-275409		Homo sapiens	T-lymphocyte
pmid	sentence
16227604	Akt phosphorylation in cells stimulated by CD3/CD28/CTLA-4 or CD3/CD28/PD-1 aAPCs did not have detectable phosphorylated Akt at any time point, indicating that CTLA-4 and PD-1 signaling blocked rather than delayed Akt activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-253218		Homo sapiens
pmid	sentence
28370702	A specific subtype of non-small cell lung cancer (NSCLC) characterized with an EML4-ALK fusion gene, which drives constitutive oncogenic activation of ALK kinase. We demonstrated that exogenous introduction of EML4-ALK protein with the substitution of lysine 1610 to an alanine in these two cell lines reduced the phosphorylation levels of AKT, one of downstream oncogenic molecules in the EML4-ALK pathway, and suppressed the growth of the two cell lines.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-244439		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

Identifier	Residue	Organism	Cell Line
SIGNOR-166478		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.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, B-cell activation, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, Luminal Breast Cancer, Malignant Melanoma, MTOR Signaling, Prostate Cancer, PI3K/AKT Signaling, Thyroid cancer

Identifier	Residue	Organism
SIGNOR-244436		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	Organism	Cell Line
SIGNOR-242103		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	Cell Line
SIGNOR-244446		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-248614		Homo sapiens
pmid	sentence
18160256	Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-244281		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:

B-cell activation, COVID-19 Causal Network, EBV infection, FLT3-ITD signaling, Inflammosome Activation, Inhibition of Apoptosis, Pancreatic ductal adenocarcinoma (PDA), SARS-CoV INFLAMMATORY RESPONSE, T cell activation

Identifier	Residue	Organism
SIGNOR-227952		Homo sapiens
pmid	sentence
16293724	We show that PGE2 stimulates colon cancer cell growth through its heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptor, EP2, by a signaling route that involves the activation of phosphoinositide 3-kinase and the protein kinase Akt by free G protein betagamma subunits and the direct association of the G protein alphas subunit with the regulator of G protein signaling (RGS) domain of axin. This leads to the inactivation and release of glycogen synthase kinase 3beta from its complex with axin, thereby relieving the inhibitory phosphorylation of beta-catenin and activating its signaling pathway.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Hepatocellular Tumor

Identifier	Residue	Organism	Cell Line
SIGNOR-269459		Homo sapiens	MCF-7 Cell
pmid	sentence
27119228	NEDL2 acts as a scaffold protein to promote GDNF-stimulated Akt activation. biochemical analysis indicated that NEDL2 appears to act like a scaffold protein to recruit SHC, Grb2, PI3K (p110 and p85), PDK1 and Akt together to promote the signaling transduction. NEDL2 binds p85, p110 and Akt with different domains

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-260659		Homo sapiens	YTS-1 Cell
pmid	sentence
32164705	Taken together, these findings indicate that NEU1 overexpression reduces cell proliferation and enhances cell apoptosis through by downregulation of FN-integrin β1-mediated Akt signaling pathway.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-176043		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-236436		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

Publications:

1

Organism:

Homo Sapiens

Tissue:

Breast Cancer Cell

Pathways:

AMPK Signaling, EGFR Signaling, Glioblastoma Multiforme, Luminal Breast Cancer, mTOR in cancer, Malignant Melanoma, MTOR Signaling, Prostate Cancer, Rhabdomyosarcoma

Identifier	Residue	Organism	Cell Line
SIGNOR-267577		Homo sapiens	Cardiomyocyte Cell Line
pmid	sentence
25323588	Earlier studies found that expression of active Akt increases mitochondrial HK activity and the anti-apoptotic effect of Akt required mitoHK

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-144156		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:

Glycolysis and Gluconeogenesis, Insulin Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-269849
pmid	sentence
25309440	Different agents were used to inhibit either the PI3K/Akt or MEK/ERK pathways. The PI3K inhibitor, LY294002, and the Akt inhibitor, Akt inhibitor VIII, were used to inhibit the PI3K/Akt pathway.

Publications:

1

Identifier	Residue	Organism
SIGNOR-45117		Homo sapiens
pmid	sentence
8940145	The constitutively active Akt induced glucose uptake into adipocytes in the absence of insulin by stimulating translocation of the insulin-responsive glucose transporter 4 to the plasma membrane.

Identifier	Residue	Organism
SIGNOR-53968		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:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism	Cell Line
SIGNOR-244288		Homo sapiens	Breast Cancer Cell
pmid	sentence
12697749	Our data indicate that akt2 inhibits cisplatin-induced jnk/p38 and bax activation through phosphorylation of ask1

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, Inhibition of Apoptosis, SARS-COV APOPTOSIS

Identifier	Residue	Organism	Cell Line
SIGNOR-261218		Homo sapiens	Hepatobiliary Carcinoma Cell
pmid	sentence
30805927	Overexpression (or silence) of BZW2 in HCC cells significantly stimulates (or decreases) the activation of the PI3K/AKT/mTOR signaling pathway

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-244452		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	Cell Line
SIGNOR-119189		Homo sapiens	Prostate Gland Cancer Cell
pmid	sentence
14617782	Perifosine, a novel alkylphospholipid, inhibits protein kinase B activation.\| Our results demonstrate that Akt is an important cellular target of perifosine action. In addition, these studies show that the membrane translocation of certain PH domain-containing molecules can be greatly perturbed by the alkylphospholipid class of drugs and imply further that the PI3K/Akt pathway contributes to regulation of p21(WAF1/CIP1) expression.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-245064		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:

Acute Myeloid Leukemia, ASXL1 in AML, FLT3 in AML, miRNA in AML, AML_TRIPLETS, FLT3-ITD in AML, FLT3-ITD signaling, Triple mutant AML, NPM1_new, WNT/FLT3

Identifier	Residue	Organism
SIGNOR-72677		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-252345		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:

COVID-19 Causal Network, Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, Hepatocellular Tumor, Pancreatic ductal adenocarcinoma (PDA), Thyroid Hormone Metabolism

Identifier	Residue	Organism
SIGNOR-262212		Homo sapiens
pmid	sentence
27995049	We also investigated the potential regulation of cancer-associated signaling pathways by Anxa3 through screening for the altered expression of some common signaling molecules after Anxa3 downregulation. Decreased phosphorylation of MEK1/2, ERK1/2, Akt, and IκBα was detected after downregulating Anxa3 expression in A549 cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-252458		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

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Organism
SIGNOR-99300		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-42050		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-260215		in vitro
pmid	sentence
14663477	Multiple studies supporting the role of Akt in apoptosis suppression have connected Akt to cell death regulation either by demonstrating its downregulation following pro-apoptotic insults, or by using gene-transfer experiments that transduce both activated, anti-apoptotic and inactive, pro-apoptotic mutants of Akt.

Publications:

1

Organism:

In Vitro

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, miRNA in AML, AML_TRIPLETS, COVID-19 Causal Network, EBV infection, FLT3-ITD in AML, FLT3-ITD signaling, Inhibition of Apoptosis, Integrin Signaling, Malignant Melanoma, Triple mutant AML, NPM1_new, Pancreatic ductal adenocarcinoma (PDA), SARS-COV APOPTOSIS, Thyroid cancer

Identifier	Residue	Organism	Cell Line
SIGNOR-244413		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	Cell Line
SIGNOR-251526		Mus musculus	3T3-L1 Cell
pmid	sentence
19593385	In examining the requirements for different Akt-mediated phosphorylation sites on TSC2, we find that only TSC2 mutants lacking all five previously identified Akt sites fully block insulin-stimulated mTORC1 signaling in reconstituted Tsc2 null cells, and this mutant also inhibits adipogenesis

Publications:

1

Organism:

Mus Musculus

Pathways:

AMPK Signaling, Insulin Signaling, Luminal Breast Cancer, mTOR in cancer, MTOR Signaling

Identifier	Residue	Organism
SIGNOR-244429		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:

1

Organism:

Homo Sapiens

Pathways:

AMPK Signaling, EGFR Signaling, Glioblastoma Multiforme, Luminal Breast Cancer, mTOR in cancer, Malignant Melanoma, MTOR Signaling, Prostate Cancer, Rhabdomyosarcoma

Identifier	Residue	Organism
SIGNOR-265319		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
SIGNOR-245411		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

Pathways:

Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, RTKs in cancer

Identifier	Residue	Organism
SIGNOR-252703		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-252715		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:

2

Organism:

Homo Sapiens

Tissue:

Breast Cancer Cell

Pathways:

Acute Myeloid Leukemia, ASXL1 in AML, BCR-ABL in AML, FLT3 in AML, KIT in AML, B-cell activation, COVID-19 Causal Network, EBV infection, ErbB receptors in cancer, FAP: Insulin-mediated adipogenesis, FLT3-ITD in AML, FLT3-ITD signaling, Hepatocellular Tumor, Inflammosome Activation, Integrin Signaling, Leptin Signaling, mTOR in cancer, Non-small-cell lung cancer (NSCLC), Pancreatic ductal adenocarcinoma (PDA), PI3K/AKT Signaling, RTKs in cancer, SARS-CoV INFLAMMATORY RESPONSE, T cell activation, Thyroid Hormone Metabolism, VEGF Signaling, WNT/FLT3

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

Publications:

1

Pathways:

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

Identifier	Residue	Organism
SIGNOR-264659		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	Organism
SIGNOR-234441		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	Cell Line
SIGNOR-145113		Homo sapiens	Neuron
pmid	sentence
16537363	Indicating that akt positively regulates shh signaling by controlling pka-mediated gli inactivation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, WNT/FLT3

Identifier	Residue	Organism
SIGNOR-244461		Homo sapiens
pmid	sentence
20626350	On the other hand, p38 alfa may negatively modulate akt activity, indipendently of pi3k by regulating the interaction between caveolin 1 and pp2a through a mechanism dependent on cell attachment.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3 in AML, FLT3-ITD in AML, FLT3-ITD signaling, Hepatocellular Tumor, Pancreatic ductal adenocarcinoma (PDA), Rhabdomyosarcoma, Thyroid cancer, WNT/FLT3

Identifier	Residue	Organism
SIGNOR-244225		Homo sapiens
pmid	sentence
16293724	We show that pge2 stimulates colon cancer cell growth through its heterotrimeric guanine nucleotide-binding protein (g protein) coupled receptor, ep2, by a signaling route that involves the activation of phosphoinositide 3-kinase and the protein kinase akt by free g protein bg subunits and the direct association of the g protein as subunit with the regulator of g protein signaling (rgs) domain of axin. This leads to the inactivation and release of glycogen synthase kinase 3b from its complex with axin, thereby relieving the inhibitory phosphorylation of b-catenin and activating its signaling pathway.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-248458		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	Organism
SIGNOR-45064		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

Pathways: