Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-276835	Ser295	RYHGHSMsDPGVSYR	in vitro
pmid	sentence
33022274	In vitro kinase assay revealed that PDHA could be readily phosphorylated by active AMPK complex in a dose-dependent manner (Figure 6C).

Identifier	Residue	Sequence	Organism
SIGNOR-276836	Ser314	IQEVRSKsDPIMLLK	in vitro
pmid	sentence
33022274	In vitro kinase assay revealed that PDHA could be readily phosphorylated by active AMPK complex in a dose-dependent manner (Figure 6C).

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-263106	Ser303	DPDAKGLsDPGKIKR	in vitro
pmid	sentence
12740371	Here we demonstrate that AMPK directly phosphorylates HNF4alpha and represses its transcriptional activity. AMPK-mediated phosphorylation of HNF4alpha on serine 304 had a 2-fold effect, reducing the ability of the transcription factor to form homodimers and bind DNA and increasing its degradation rate in vivo.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-216511	Ser303	DPDAKGLsDPGKIKR	Homo sapiens
pmid	sentence
12740371	Here we demonstrate that ampk directly phosphorylates hnf4 and represses its transcriptional activity. Ampk-mediated phosphorylation of hnf4 on serine 304 had a 2-fold effect

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-263031	Ser307	PARNRSAsITNLSLD	in vitro
pmid	sentence
23905686	AMPK phosphorylated PIKfyve at Ser307 both in vitro and in intact cells. We propose that PIKfyve activity is required for the stimulation of skeletal muscle glucose uptake by contraction/AMPK activation. PIKfyve is a new AMPK substrate whose phosphorylation at Ser307 could promote PIKfyve translocation to endosomes for PtdIns(3,5)P2 synthesis to facilitate GLUT4 (glucose transporter 4) translocation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276489	Ser308	GLSSRTSsMASRTSS	Rattus norvegicus	Hepatocyte
pmid	sentence
23453806	AMPK phosphorylation of TXNIP on S308 accelerates its degradation

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-264789	Ser314	LKLHTFEsHKDEIFQ	in vitro
pmid	sentence
28143904	AMPK increased HAT1 activity through phosphorylation of HAT1-Ser190 and RBBP7-Ser314\| interaction between RBBP7 and HAT1 is required for acetyltransferase activity

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-216491	Ser317	SHLASPPsLGEMQQL	Homo sapiens
pmid	sentence
19584320	In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy.

Identifier	Residue	Sequence	Organism
SIGNOR-216453	Ser317	SHLASPPsLGEMQQL	Homo sapiens
pmid	sentence
21205641	In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy.

Identifier	Residue	Sequence	Organism
SIGNOR-216457	Ser556	GLGCRLHsAPNLSDL	Homo sapiens
pmid	sentence
21205641	In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy.

Identifier	Residue	Sequence	Organism
SIGNOR-216495	Ser556	GLGCRLHsAPNLSDL	Homo sapiens
pmid	sentence
19584320	In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy.

Identifier	Residue	Sequence	Organism
SIGNOR-216461	Ser638	FDFPKTPsSQNLLAL	Homo sapiens
pmid	sentence
21205641	In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy.

Identifier	Residue	Sequence	Organism
SIGNOR-216499	Ser638	FDFPKTPsSQNLLAL	Homo sapiens
pmid	sentence
19584320	In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy.

Identifier	Residue	Organism
SIGNOR-216464		Homo sapiens
pmid	sentence
21460634	Ampk and ulk1 interact and that the latter is phosphorylated by ampk. This phosphorylation leads to the direct activation of ulk1 by ampk bypassing mtor-inhibition.

Publications:

7

Organism:

Homo Sapiens

Pathways:

MTOR Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-216568	Ser322	TTLPRMKsSSSVTTS	Homo sapiens
pmid	sentence
21945940	Here we show that phosphorylation of vasp by ampk occurs at a novel site, serine 322, and that phosphorylation at this site alters actin filament binding. We also show that inhibition of ampk activity results in the accumulation of vasp at cell-cell adhesions and a concomitant increase in cell-cell adhesion.

Identifier	Residue	Sequence	Organism
SIGNOR-216515	Thr278	LARRRKAtQVGEKTP	Homo sapiens
pmid	sentence
17082196	Pharmacological ampk inhibitors and activators and ampk mutants revealed that the kinase specifically targets residue thr-278 but not ser-157 or ser-239. Quantitative fluorescence-activated cell sorter analysis and serum response factor transcriptional reporter assays, which quantify the cellular f-/g-actin equilibrium, indicated that ampk-mediated vasp phosphorylation impaired actin stress fiber formation and altered cell morphology.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273001	Ser326	SARKRSAsADNLTLP	Homo sapiens
pmid	sentence
32723157	Our in vitro and cellular analyses supported the mass spectrometry data that implicated serine 326 (S326) as the phospho-acceptor site on CCNY by AMPK. \|Mechanistically the S326 phosphorylation by AMPK promotes the interaction of CCNY with CDK16, which in turn autophosphorylates S336, which serves as a marker for active CCNY-CDK16

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273739	Ser33	MRLCLAHsPPVKSFL	Cricetulus griseus	CHO Cell
pmid	sentence
19171932	AMPK induces the phosphorylation of residues Ser-8 and Ser-268 in R5/PTG. We now demonstrate that phosphorylation of R5/PTG at Ser-8 by AMPK accelerates its laforin/malin-dependent ubiquitination and subsequent proteasomal degradation, which results in a decrease of its glycogenic activity. Thus, our results define a novel role of AMPK in glycogen homeostasis.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276237	Ser33	MRLCLAHsPPVKSFL	Homo sapiens	HEK-293 Cell
pmid	sentence
19171932	We have recently described that the activity of R5/PTG is down-regulated by the laforin-malin complex, composed of a dual specificity phosphatase (laforin) and an E3-ubiquitin ligase (malin). We now demonstrate that phosphorylation of R5/PTG at Ser-8 by AMPK accelerates its laforin/malin-dependent ubiquitination and subsequent proteasomal degradation, which results in a decrease of its glycogenic activity.

Publications:

2

Organism:

Cricetulus Griseus, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-216537	Ser351	HVISRDQsTPIIEVE	Homo sapiens
pmid	sentence
21478464	Tr4 transactivation is inhibited via phosphorylation bymetformin-induced amp-activated protein kinase (ampk) at the amino acid serine 351, which results in the suppression of scd1 gene expression

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273929	Ser352	PRHLSNVsSTGSIDM	in vitro
pmid	sentence
21204788	AMPK phosphorylation inhibits tau binding of microtubules. In order to study further the phosphorylation of tau by AMPK, we compared phosphorylation of tau by MARK4 or AMPK using a panel of phospho-tau antibodies (Figure 2A). Five phosphorylation sites common to both kinases were identified (Thr231, Ser262, Ser356, Ser396 and Ser422). In addition, AMPK, but not MARK4, was capable of phosphorylating Ser214 (Figure 2A).

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-216608	Ser366	KTLPRSSsMAAGLER	Homo sapiens
pmid	sentence
22137581	Using this approach for ppp1r12c, baiap2, and cdc27, we found that mutation of a single serine to alanine (s452, s366, and s379 respectively) resulted in almost a complete loss of ampk phosphorylation in these proteins. Termination of irsp53 function is suggested to occur following cdc42 dissociation, kinase phosphorylation of t340 and t360, and subsequent 14-3-3 binding, which competes for sh3 partners, thus allowing filopodial retraction

Identifier	Residue	Sequence	Organism
SIGNOR-216572	Ser366	KTLPRSSsMAAGLER	Homo sapiens
pmid	sentence
19933840	Using this approach for ppp1r12c, baiap2, and cdc27, we found that mutation of a single serine to alanine (s452, s366, and s379 respectively) resulted in almost a complete loss of ampk phosphorylation in these proteins. Termination of irsp53 function is suggested to occur following cdc42 dissociation, kinase phosphorylation of t340 and t360, and subsequent 14-3-3 binding, which competes for sh3 partners, thus allowing filopodial retraction

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-216434	Ser379	NALPRRSsRLFTSDS	Homo sapiens
pmid	sentence
22137581	Using this approach for ppp1r12c, baiap2, and cdc27, we found that mutation of a single serine to alanine (s452, s366, and s379, respectively) resulted in an almost complete loss of ampk phosphorylation in these proteins

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276064	Ser389	RGAPANVsSSDLTGR	in vitro
pmid	sentence
17525164	AMPK enhances mPer2 degradation and CKIɛ activity by phosphorylating Ser-389 of CKIɛ. One of the regulators of the period length is casein kinase Iepsilon (CKIepsilon), which by phosphorylating and inducing the degradation of the circadian clock component, mPer2, shortens the period length. AMPK phosphorylates Ser-389 of CKIepsilon, resulting in increased CKIepsilon activity and degradation of mPer2.

Publications:

1

Organism:

In Vitro

Pathways:

Circadian clock, MTOR Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-216533	Ser396	TAVHKSKsLKDLVSA	Homo sapiens
pmid	sentence
21459323	Here we demonstrate that ampk interacts with and directly phosphorylates sterol regulatory element binding proteins (srebp-1c and -2). Ser372

Identifier	Residue	Organism
SIGNOR-216564		Homo sapiens
pmid	sentence
21892142	Ampk was recently found to phosphorylate a conserved serine near the cleavage site within srebp1, suppressing its activation

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-216503	Ser398	DSLPSSPsSATPHSQ	Homo sapiens
pmid	sentence
22669845	In response to genotoxic stress, eef2k was activated by ampk (adenosine monophosphate-activated protein kinase)-mediated phosphorylation on serine 398. Activated eef2k phosphorylated eef2 and induced a temporary ribosomal slowdown at the stage of elongation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252880	Ser399	DNITLPPsQPSPTGG	Homo sapiens	HEK-293 Cell
pmid	sentence
17711846	Phosphorylation by AMPK leads to the activtion of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252881	Ser413	GLMQRSSsFPYTTKG	Homo sapiens	HEK-293 Cell
pmid	sentence
17711846	Phosphorylation by AMPK leads to the activtion of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252882	Ser555	RALSNSVsNMGLSES	Homo sapiens	HEK-293 Cell
pmid	sentence
17711846	Phosphorylation by AMPK leads to the activtion of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252883	Ser588	QTLSDSLsGSSLYST	Homo sapiens	HEK-293 Cell
pmid	sentence
17711846	Phosphorylation by AMPK leads to the activtion of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252884	Ser626	SLECDMEsIIRSELM	Homo sapiens	HEK-293 Cell
pmid	sentence
17711846	Phosphorylation by AMPK leads to the activtion of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252885	Thr179	SSPDKRLtLSQIYEW	Homo sapiens	HEK-293 Cell
pmid	sentence
17711846	Phosphorylation by AMPK leads to the activtion of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.

Identifier	Residue	Organism
SIGNOR-252889		Homo sapiens
pmid	sentence
17900900	The energy sensor amp-activated protein kinase (ampk) has been shown to directly phosphorylate foxo factors at six regulatory sites that are distinct from the akt.

Publications:

7

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, IDH-TET in AML, FLT3-ITD signaling, NPM1_new

Identifier	Residue	Sequence	Organism
SIGNOR-274095	Ser399	DNITLPPsQPSPTGG	in vitro
pmid	sentence
17711846	Here, we find that AMPK directly regulates mammalian FOXO3, a member of the FOXO family of Forkhead transcription factors known to promote resistance to oxidative stress, tumor suppression, and longevity. We show that AMPK phosphorylates human FOXO3 at six previously unidentified regulatory sites.Phosphorylation by AMPK leads to the activation of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.Taken together, these results indicate that AMPK phosphorylates at least six residues of FOXO3 in vitro (Thr179, Ser399, Ser413, Ser555, Ser588, and Ser626).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249668	Ser399	DNITLPPsQPSPTGG	Homo sapiens	HEK-293 Cell
pmid	sentence
17711846	Phosphorylation by AMPK leads to the activtion of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.

Identifier	Residue	Sequence	Organism
SIGNOR-255756	Ser413	GLMQRSSsFPYTTKG	Mus musculus
pmid	sentence
22848740	When AMPK is stimulated, pre-existing FOXO3 becomes reverted toward an active form.

Identifier	Residue	Sequence	Organism
SIGNOR-274098	Ser413	GLMQRSSsFPYTTKG	in vitro
pmid	sentence
17711846	Here, we find that AMPK directly regulates mammalian FOXO3, a member of the FOXO family of Forkhead transcription factors known to promote resistance to oxidative stress, tumor suppression, and longevity. We show that AMPK phosphorylates human FOXO3 at six previously unidentified regulatory sites.Phosphorylation by AMPK leads to the activation of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.Taken together, these results indicate that AMPK phosphorylates at least six residues of FOXO3 in vitro (Thr179, Ser399, Ser413, Ser555, Ser588, and Ser626).

Identifier	Residue	Sequence	Organism
SIGNOR-249678	Ser413	GLMQRSSsFPYTTKG	Homo sapiens
pmid	sentence
17711846	Phosphorylation by AMPK leads to the activtion of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.

Identifier	Residue	Sequence	Organism
SIGNOR-249682	Ser555	RALSNSVsNMGLSES	Homo sapiens
pmid	sentence
17711846	Phosphorylation by AMPK leads to the activtion of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.

Identifier	Residue	Sequence	Organism
SIGNOR-274093	Ser555	RALSNSVsNMGLSES	in vitro
pmid	sentence
17711846	Here, we find that AMPK directly regulates mammalian FOXO3, a member of the FOXO family of Forkhead transcription factors known to promote resistance to oxidative stress, tumor suppression, and longevity. We show that AMPK phosphorylates human FOXO3 at six previously unidentified regulatory sites.Phosphorylation by AMPK leads to the activation of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.Taken together, these results indicate that AMPK phosphorylates at least six residues of FOXO3 in vitro (Thr179, Ser399, Ser413, Ser555, Ser588, and Ser626).

Identifier	Residue	Sequence	Organism
SIGNOR-249685	Ser588	QTLSDSLsGSSLYST	Homo sapiens
pmid	sentence
17711846	Phosphorylation by AMPK leads to the activtion of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.

Identifier	Residue	Sequence	Organism
SIGNOR-274096	Ser588	QTLSDSLsGSSLYST	in vitro
pmid	sentence
17711846	Here, we find that AMPK directly regulates mammalian FOXO3, a member of the FOXO family of Forkhead transcription factors known to promote resistance to oxidative stress, tumor suppression, and longevity. We show that AMPK phosphorylates human FOXO3 at six previously unidentified regulatory sites.Phosphorylation by AMPK leads to the activation of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.Taken together, these results indicate that AMPK phosphorylates at least six residues of FOXO3 in vitro (Thr179, Ser399, Ser413, Ser555, Ser588, and Ser626).

Identifier	Residue	Sequence	Organism
SIGNOR-274097	Ser626	SLECDMEsIIRSELM	in vitro
pmid	sentence
17711846	Here, we find that AMPK directly regulates mammalian FOXO3, a member of the FOXO family of Forkhead transcription factors known to promote resistance to oxidative stress, tumor suppression, and longevity. We show that AMPK phosphorylates human FOXO3 at six previously unidentified regulatory sites.Phosphorylation by AMPK leads to the activation of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.Taken together, these results indicate that AMPK phosphorylates at least six residues of FOXO3 in vitro (Thr179, Ser399, Ser413, Ser555, Ser588, and Ser626).

Identifier	Residue	Sequence	Organism
SIGNOR-249688	Ser626	SLECDMEsIIRSELM	Homo sapiens
pmid	sentence
17711846	Phosphorylation by AMPK leads to the activtion of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.

Identifier	Residue	Sequence	Organism
SIGNOR-238813	Thr179	SSPDKRLtLSQIYEW	Homo sapiens
pmid	sentence
17711846	Phosphorylation by AMPK leads to the activtion of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.

Identifier	Residue	Sequence	Organism
SIGNOR-274094	Thr179	SSPDKRLtLSQIYEW	in vitro
pmid	sentence
17711846	Here, we find that AMPK directly regulates mammalian FOXO3, a member of the FOXO family of Forkhead transcription factors known to promote resistance to oxidative stress, tumor suppression, and longevity. We show that AMPK phosphorylates human FOXO3 at six previously unidentified regulatory sites.Phosphorylation by AMPK leads to the activation of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.Taken together, these results indicate that AMPK phosphorylates at least six residues of FOXO3 in vitro (Thr179, Ser399, Ser413, Ser555, Ser588, and Ser626).

Identifier	Residue	Organism
SIGNOR-216481		Homo sapiens
pmid	sentence
17900900	We have recently found that AMPK phosphorylates human FOXO3 in mammalian cells at novel regulatory sites that are distinct from the AKT sites

Publications:

14

Organism:

In Vitro, Homo Sapiens, Mus Musculus

Pathways:

AMPK Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-266413	Ser45	LGIRSSKsAGALEEG	Homo sapiens
pmid	sentence
30631047	We validated one uncharacterized protein, ARMC10, and demonstrated that the S45 site of ARMC10 can be phosphorylated by AMPK both in vitro and in vivo. Moreover, ARMC10 overexpression was sufficient to promote mitochondrial fission, whereas ARMC10 knockout prevented AMPK-mediated mitochondrial fission. These results demonstrate that ARMC10 is an effector of AMPK that participates in dynamic regulation of mitochondrial fission and fusion.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-216600	Ser452	AGLQRSAsSSWLEGT	Homo sapiens
pmid	sentence
22137581	Ampk-induced phosphorylation is necessary for ppp1r12c interaction with 14-3-3 and phosphorylation of myosin regulatory light chain. Both ampk activity and ppp1r12c phosphorylation are increased in mitotic cells and are important for mitosis completion. The interaction between ppp1r12c and 14-3-3_ may inactivate the ppp1r12c-containing phosphatase complex in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-216639	Ser461	NPLMRRNsVTPLASP	Homo sapiens	Monocyte
pmid	sentence
12065600	Ipfk-2 was phosphorylated on the homologous serine (ser-461) and activated by ampk in vitro.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Kidney

Pathways:

Glycolysis and Gluconeogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-216623	Ser466	PVRMRRNsFTPLSSS	Homo sapiens
pmid	sentence
11069105	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-260011	Ser466	PVRMRRNsFTPLSSSN	Rattus norvegicus
pmid	sentence
11069105	AMPK phosphorylates and activates heart PFK-2 in vitro and in intact cells. AMPK-mediated PFK-2 activation is likely to be involved in the stimulation of heart glycolysis during ischaemia.

Identifier	Residue	Sequence	Organism
SIGNOR-209947	Ser466	PVRMRRNsFTPLSSS	Homo sapiens
pmid	sentence
20640476	The decreased glycogen synthesis rates upon acute AMPK activation are generally coupled to an increase in the glycolytic flux, thanks to the activation of 6-phosphofructo-2-kinase (PFK-2) through direct phosphorylation on Ser466 [35]. PFK-2 catalyzes the synthesis of fructose 2,6-bisphosphate, a potent stimulator of glycolysis. Therefore, activation of AMPK rapidly mobilizes glucose into ATP-generating processes.

Publications:

3

Organism:

Homo Sapiens, Rattus Norvegicus

Tissue:

Heart

Pathways:

AMPK Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-216519	Ser470	VAAHRSKsHPALLLA	Homo sapiens
pmid	sentence
17097062	Arebp is phosphorylated at ser(470) by ampk. Phosphorylation reduces the dna-binding activity of arebp.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-256113	Ser486	DDEITEAKsGTATPQRS	in vitro
pmid	sentence
17023420	We show that AMPK α-Ser485/491 can be a site for autophosphorylation, which may play a role in limiting AMPK activation in response to energy depletion or other regulators

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-216643	Ser505	GSVKRVTsGPSLGSL	Homo sapiens
pmid	sentence
20231899	Ampk-wild type (wt) stimulates pld activity, while ampk-dominant negative (dn) inhibits it. Ampk regulates pld1 activity through phosphorylation of the ser-505 and this phosphorylation is increased by the presence of amp.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle

Identifier	Residue	Sequence	Organism
SIGNOR-228646	Ser539	SLFNVSPsCSSFNSP	Mus musculus
pmid	sentence
17609368	AMPK phosphorylates PGC-1alpha directly both in vitro and in cells. These direct phosphorylations of the PGC-1alpha protein at threonine-177 and serine-538 are required for the PGC-1alpha-dependent induction of the PGC-1alpha promoter

Identifier	Residue	Sequence	Organism
SIGNOR-209940	Ser539	SLFNVSPsCSSFNSP	Homo sapiens
pmid	sentence
20640476	AMPK can directly phosphorylate PGC-1a at Thr177 and Ser538 in in vitro assays PGC-1a phosphorylation might not directly affect its intrinsic coactivation activity, but, rather, release it from its repressor protein p160myb [79] and/or allow deacetylation and subsequent activation by SIRT1

Identifier	Residue	Sequence	Organism
SIGNOR-228642	Thr178	NHNHRIRtNPAIVKT	Mus musculus
pmid	sentence
17609368	AMPK phosphorylates PGC-1alpha directly both in vitro and in cells. These direct phosphorylations of the PGC-1alpha protein at threonine-177 and serine-538 are required for the PGC-1alpha-dependent induction of the PGC-1alpha promoter

Identifier	Residue	Sequence	Organism
SIGNOR-209936	Thr178	NHNHRIRtNPAIVKT	Homo sapiens
pmid	sentence
20640476	AMPK can directly phosphorylate PGC-1a at Thr177 and Ser538 in in vitro assays PGC-1a phosphorylation might not directly affect its intrinsic coactivation activity, but, rather, release it from its repressor protein p160myb [79] and/or allow deacetylation and subsequent activation by SIRT1

Publications:

4

Organism:

Mus Musculus, Homo Sapiens

Tissue:

Skeletal Muscle

Pathways:

AMPK Signaling, Circadian clock, MTOR Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-216647	Ser539	SLFNVSPsCSSFNSP	Homo sapiens
pmid	sentence
17609368	Ampk phosphorylates pgc-1alpha directly both in vitro and in cells. These direct phosphorylations of the pgc-1alpha protein at threonine-177 and serine-538.

Identifier	Residue	Sequence	Organism
SIGNOR-216651	Thr178	NHNHRIRtNPAIVKT	Homo sapiens
pmid	sentence
17609368	Ampk phosphorylates pgc-1alpha directly both in vitro and in cells. These direct phosphorylations of the pgc-1alpha protein at threonine-177 and serine-538.

Publications:

2

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle

Pathways:

AMPK Signaling, Circadian clock, MTOR Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-216526	Ser556	LLRSPGsPQETVPE	Rattus norvegicus
pmid	sentence
11724780	These results strongly suggested that the fatty acid inhibition of glucose-induced l-PK transcription resulted from AMPK phosphorylation of ChREBP at Ser568, which inactivated the DNA binding activity.

Identifier	Residue	Organism
SIGNOR-216561		Rattus norvegicus
pmid	sentence
21892142	AMPK has also been suggested to phosphorylate the glucose-sensitive transcription factor ChREBP89 which dictates expression of an overlapping lipogenic gene signature with Srebp1

Publications:

2

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273736	Ser559	VQRKVSGsRGSFCKA	Homo sapiens	HEK-293 Cell
pmid	sentence
30279167	Thus, AMPK directly phosphorylates the α subunit of KV1.5 at Ser592 and, to a lesser extent, at Ser559.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273735	Ser592	KCNVKAKsNVDLRRS	Homo sapiens	HEK-293 Cell
pmid	sentence
30279167	Thus, AMPK directly phosphorylates the α subunit of KV1.5 at Ser592 and, to a lesser extent, at Ser559.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-275548	Ser57	TVHQRIAsWQNLGAV	in vitro
pmid	sentence
30858581	Cellular ATP levels drop during early mitosis, and the mitochondrial Ca2+ transients boost mitochondrial respiration to restore energy homeostasis. This is achieved through mitosis-specific MCU phosphorylation and activation by the mitochondrial translocation of energy sensor AMP-activated protein kinase (AMPK). \|In vitro kinase assays showed that AMPK immunoprecipitated from cells as well as recombinant AMPK phosphorylated MCU at Ser57

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-216468	Ser582	PRMKRASsLNFLNKS	Homo sapiens
pmid	sentence
21725060	Consistent with phosphorylation of both ser545 and ser582 of klc2 contributing to its 14-3-3 binding, a ser545ala mutant of klc2 could be phosphorylated in vitro by ampk on ser582

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-216616	Ser621	PKINRSAsEPSLHRA	Homo sapiens
pmid	sentence
9091312	Ampk also phosphorylated full-length, kinase-defective raf-1 (k375m) to generate two [32p]phosphopeptides, one co-migrating with synthetic tryptic peptide containing phospho-ser621 and the other with phospho-ser259

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-216592	Ser635	DTHFRSPsSSVGSPP	Homo sapiens
pmid	sentence
19815529	We show that ampk down-regulates rrna synthesis under glucose restriction by phosphorylating the rna polymerase i (pol i)-associated transcription factor tif-ia at a single serine residue (ser-635).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-271823	Ser659	PGLPKTRsGKIMRRV
pmid	sentence
28820290	This translocation is mediated by AMP-activated protein kinase (AMPK)-dependent ACSS2 Ser659 phosphorylation and subsequent exposure of the nuclear localization signal of ACSS2 to KPNA1/importin α5 for binding. In the nucleus, ACSS2 forms a complex with TFEB (transcription factor EB) and utilizes the acetate generated from histone deacetylation to locally produce acetyl-CoA for histone acetylation in the promoter regions of TFEB target genes.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-216546	Ser71	ANLRKLNsRLFVIRG	Homo sapiens
pmid	sentence
21892142	Ampk was shown to regulate the stability of the core clock component cry1 though phosphorylation of cry1 ser71, which stimulates the direct binding of the fbox protein fbxl3 to cry1, targeting it for ubiquitin-mediated degradation

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-264788	Ser714	DNIPEMPsPKKMHQG	in vitro
pmid	sentence
28143904	Together, these results indicate that AMPK phosphorylated DNMT1-Ser730, RBBP7-Ser314, and HAT1-Ser190\|AMPK decreased DNMT1 activity

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-263046	Ser722	PRLRSVSsYGNIRAV	Mus musculus
pmid	sentence
18439900	These results suggest that AMPK activation can induce phosphorylation of both serine 722 and serine 792.\|Raptor phosphorylation is required for inhibition of mTORC1 by AMPK

Identifier	Residue	Sequence	Organism
SIGNOR-263044	Ser792	LTQSAPAsPTNKGVH	Mus musculus
pmid	sentence
18439900	These results suggest that AMPK activation can induce phosphorylation of both serine 722 and serine 792.\|Raptor phosphorylation is required for inhibition of mTORC1 by AMPK

Publications:

2

Organism:

Mus Musculus

Pathways:

MTOR Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-250350	Ser737	EPLERRLsLVPDSEQ	Homo sapiens
pmid	sentence
19095655	AMPK phosphorylates CFTR¬†in vitro¬†at two essential serines (Ser737and Ser768) in the R domain, formerly identified as "inhibitory" PKA sites.\|Interestingly two of these sites, namely Ser737 and Ser768, have been identified as “inhibitory” R domain sites, i.e. when mutated to alanines they augment the open probability of CFTR relative to wild type\|Our present results suggest that it might be AMPK rather than PKA that is phosphorylating Ser737 and Ser768 under baseline conditions

Identifier	Residue	Sequence	Organism
SIGNOR-72708	Ser768	LQARRRQsVLNLMTH	Homo sapiens
pmid	sentence
19095655	AMPK phosphorylates CFTR¬†in vitro¬†at two essential serines (Ser737and Ser768) in the R domain, formerly identified as "inhibitory" PKA sites.\|Interestingly two of these sites, namely Ser737 and Ser768, have been identified as “inhibitory” R domain sites, i.e. when mutated to alanines they augment the open probability of CFTR relative to wild type\|Our present results suggest that it might be AMPK rather than PKA that is phosphorylating Ser737 and Ser768 under baseline conditions

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-266313	Ser75	YGAQTVRsTMNFKIG	in vitro
pmid	sentence
28628081	Glucose deficiency induces AMPK activation, which phosphorylates FH at Ser75 and promotes its binding to ATF2 and the enrichment of the FH–ATF2 complex on the promoter regions of ATF2-targeted genes.

Publications:

1

Organism:

In Vitro

Pathways:

Citric acid cycle

Identifier	Residue	Sequence	Organism
SIGNOR-266365	Ser761	QSIPRSAsYPCAAPR	Homo sapiens
pmid	sentence
25266655	Our data suggest that the localization of mammalian Atg9A to autophagosomes requires phosphorylation on the C terminus of Atg9A at S761, which creates a 14-3-3ζ docking site. Under basal conditions, this phosphorylation is maintained at a low level and is dependent on both ULK1 and AMPK.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276630	Ser77	RPLGPTPsQSRFQVD	in vitro
pmid	sentence
24702155	AMPK was found to directly phosphorylate a recombinant human-NKCC1 N-terminal fragment (1-293) with the phosphorylated site identified as S77. Mutation of Serine 77 to Alanine partially prevented the inhibitory effect of A-769662 on NKCC1 activity. In conclusion, AMPK can act to reduce NKCC1-mediated transport.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263105	Ser793	SSLRPARsVPSIAAA	Homo sapiens	HEK-293 Cell
pmid	sentence
25373897	we show that AMPK directly phosphorylates S793 of AMOTL1. AMPK activation stabilizes and increases AMOTL1 steady-state protein levels, contributing to YAP inhibition.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276326	Ser795	VDLKPNGsEIMVTNE	in vitro
pmid	sentence
21501591	The AMP-activated protein kinase (AMPK) down-regulates the inward rectifier K+ channel Kir2.1. Expression of wild type Nedd4-2 or of Nedd4-2S795A lacking an AMPK phosphorylation consensus sequence downregulated Kir2.1 currents. The effect of wild type Nedd4-2 but not of Nedd4-2S795A was significantly augmented by additional coexpression of AMPK.

Identifier	Residue	Sequence	Organism
SIGNOR-276324	Ser795	VDLKPNGsEIMVTNE	in vitro
pmid	sentence
21501591	The AMP-activated protein kinase (AMPK) down-regulates the inward rectifier K+ channel Kir2.1. Expression of wild type Nedd4-2 or of Nedd4-2S795A lacking an AMPK phosphorylation consensus sequence downregulated Kir2.1 currents. The effect of wild type Nedd4-2 but not of Nedd4-2S795A was significantly augmented by additional coexpression of AMPK.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-263101	Ser8	MLRGRSLsVTSLGGL	in vitro
pmid	sentence
22233421	Recombinant muscle GYS1 (glycogen synthase 1) and recombinant liver GYS2 were phosphorylated by recombinant AMPK (AMP-activated protein kinase) in a time-dependent manner and to a similar stoichiometry. The phosphorylation site in GYS2 was identified as Ser7, which lies in a favourable consensus for phosphorylation by AMPK. Phosphorylation of GYS1 or GYS2 by AMPK led to enzyme inactivation by decreasing the affinity for both UDP-Glc (UDP-glucose) [assayed in the absence of Glc-6-P (glucose-6-phosphate)] and Glc-6-P (assayed at low UDP-Glc concentrations).

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-263102	Ser8	MPLNRTLsMSSLPGL	in vitro
pmid	sentence
22233421	Recombinant muscle GYS1 (glycogen synthase 1) and recombinant liver GYS2 were phosphorylated by recombinant AMPK (AMP-activated protein kinase) in a time-dependent manner and to a similar stoichiometry. The phosphorylation site in GYS2 was identified as Ser7, which lies in a favourable consensus for phosphorylation by AMPK. Phosphorylation of GYS1 or GYS2 by AMPK led to enzyme inactivation by decreasing the affinity for both UDP-Glc (UDP-glucose) [assayed in the absence of Glc-6-P (glucose-6-phosphate)] and Glc-6-P (assayed at low UDP-Glc concentrations).

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-267475	Ser80	LHIRSSMsGLHLVKQ	Homo sapiens
pmid	sentence
29899443	Human ACC1 is inactivated by phosphorylation at Ser80, Ser1201 and Ser1216 by AMP-activated protein kinase (AMPK)

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-216655	Ser80	LHIRSSMsGLHLVKQ	Homo sapiens
pmid	sentence
12015362	Significant negative linear correlations between phospho-acc and acc activity were observed in all models (p < 0.01). The decline in acc activity was related to the decrease in pcr and the rise in amp. A relationship between phospho-ampk (threonine 172) and activity of ampk immunoprecipitated with anti-alpha(2) subunit antibody preparation was also observed.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle

Pathways:

Acute Myeloid Leukemia, IDH-TET in AML, NPM1_new

Identifier	Residue	Sequence	Organism
SIGNOR-216635	Ser811	IYISPLKsPYKISEG	Homo sapiens
pmid	sentence
19217427	Amp-activated protein kinase phosphorylates retinoblastoma protein. Rb phosphorylation sites, ser804 (ser811 in human), resembled the ampk consensus phosphorylation site.

Publications:

1

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling

Identifier	Residue	Sequence	Organism
SIGNOR-216507	Ser855	EPMRRSVsEAALAQP	Homo sapiens
pmid	sentence
9636039	Phosphorylation of bovine hormone-sensitive lipase by the amp-activated protein kinase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277638	Ser94	RLRKLPDsFFKPPEP	Homo sapiens	HEK-293T Cell
pmid	sentence
25751140	Moreover, AMPK directly phosphorylates YAP Ser 94, a residue essential for the interaction with TEAD, thus disrupting the YAP-TEAD interaction.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-256135	Ser99	GGIKRTVsEPSLSGLL	Homo sapiens	Peripheral Blood Mononuclear Cell
pmid	sentence
30022161	We identify the tumour suppressor TET2 as a substrate of the AMP-activated kinase (AMPK), which phosphorylates TET2 at serine 99, thereby stabilizing the tumour suppressor. Increased glucose levels impede AMPK-mediated phosphorylation at serine 99, which results in the destabilization of TET2 followed by dysregulation of both 5-hydroxymethylcytosine (5hmC) and the tumour suppressive function of TET2 in vitro and in vivo

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275769	Thr101	IVLNKGKtIFRFSAT	Homo sapiens	Neuron
pmid	sentence
33410863	Among the sites identified, only six were previously suggested to be the targets for specific kinases using in silico and/or in vitro analyses: S36 and S525 were attributed to the regulation by PKA; S484 and S664 were assigned to the serum- and glucocorticoid-inducible kinase 3 (SGK3); and S516 and S571 were ascribed to CaMKII (reviewed in Marionneau and Abriel, 2015). In marked contrast, several previously described phosphorylation sites were not detected in the present study, including the PKA-dependent S528, the CaMKII-associated T594, the PKC-dependent S1506, the adenosine monophosphate–activated protein kinase (AMPK)–dependent T101 (Liu et al., 2019), and the six Fyn-dependent tyrosines (Ahern et al., 2005; Iqbal et al., 2018).\|The simplest interpretation of these findings is that these three phosphorylation clusters, at positions S457-S460, S483-T486, and S664-S671, are likely involved in regulating the basal and/or gating properties of native cardiac NaV1.5 channels. Conversely, the other phosphorylation sites, with lower stoichiometries, may play spatially or temporally distinct roles in the physiological or more pathophysiological regulation of channel expression or gating. \| Remarkably, this MS analysis also revealed that the vast majority of identified phosphorylation sites (at least 26) are clustered, suggesting concomitant phosphorylation and roles in regulating channel expression and/or function. Unexpectedly, however, except for S664, S667, and S671, no apparent effects of phosphomimetic or phosphosilent mutations were observed on heterologously expressed (in HEK-293 cells) NaV1.5

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-216588	Thr1337	GKIHRSAtDADVVNS	Homo sapiens
pmid	sentence
18063581	These results indicate that gbf1 is a novel ampk substrate and that the ampk-mediated phosphorylation of gbf1 at thr(1337) has a critical role, presumably by attenuating the function of gbf1, in the disassembly of the golgi apparatus induced under stress conditions that lower the intracellular atp concentration.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275865	Thr153	TLTHMSItRLHEQKL
pmid	sentence
27511885	Here, the authors show that energy stress induces an AMPK-dependent phosphorylation of Sirt7, which promotes its ubiquitin-independent degradation by REGγ, resulting in the down-regulation of rRNA transcription and cell survival.\|These results strongly suggest that the phosphorylation status of SirT7 at T153 plays a crucial role in determining its subcellular distribution, degradation and binding to REGγ.

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273737	Thr32	PRGIRLYtYEQIPGS	Homo sapiens	HEK-293 Cell
pmid	sentence
26834238	Firstly, PAQR3 functions as a scaffold protein that facilitates the formation of ATG14L- but not UVRAG-linked VPS34 complex, leading to elevated capacity of PI(3)P generation ahead of starvation signals. Secondly, AMPK phosphorylates PAQR3 at threonine 32 and switches on PI(3)P production to initiate autophagosome formation swiftly after glucose starvation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271862	Thr356	GNPFDSKtEQGPQVD	Mus musculus	Macrophage
pmid	sentence
30375985	Further studies demonstrate that in the absence of LDLR, AMPK phosphorylates ALDH2 at threonine 356 and enables its nuclear translocation. Nuclear ALDH2 interacts with HDAC3 and represses transcription of a lysosomal proton pump protein ATP6V0E2, critical for maintaining lysosomal function, autophagy, and degradation of oxidized low-density lipid protein.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251618	Thr495	TGITRKKtFKEVANA	Homo sapiens	Vascular Endothelium
pmid	sentence
24379783	The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-216441		Homo sapiens
pmid	sentence
14651849	Under energy starvation conditions, the amp-activated protein kinase (ampk) phosphorylates tsc2 and enhances its activity.

Identifier	Residue	Organism
SIGNOR-216487		Homo sapiens
pmid	sentence
19584320	Under energy starvation conditions, the amp-activated protein kinase (ampk) phosphorylates tsc2 and enhances its activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-263510		Homo sapiens	Pulmonary Artery Smooth Muscle Cell
pmid	sentence
25343030	Leptin exerts an inhibitory effect on AMPK in the hypothalamus, thereby stimulating ACC and subsequently suppressing food intake.

Publications:

1

Organism:

Homo Sapiens

Pathways:

AMPK Signaling, FLT3-ITD signaling

Identifier	Residue	Organism
SIGNOR-216529		Homo sapiens
pmid	sentence
21331044	Here we show that both ampk and calcineurin modulate longevity exclusively through post-translational modification of crtc-1, the sole c. elegans crtc. We demonstrate that crtc-1 is a direct ampk target.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-217493		Homo sapiens	HeLa Cell
pmid	sentence
15980064	These data indicate that the camkks function in intact cells as ampkks, predicting wider roles for these kinases in regulating ampk activity in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-242602		in vitro
pmid	sentence
14976552	We recently demonstrated that the LKB1 tumour suppressor kinase, in complex with the pseudokinase STRAD and the scaffolding protein MO25, phosphorylates and activates AMP_activated protein kinase (AMPK).

Publications:

1

Organism:

In Vitro

Pathways:

Identifier	Residue	Organism	Cell Line
SIGNOR-139170		Homo sapiens	Adipocyte
pmid	sentence
16054041	Gamma non-catalytic subunit mediates binding to amp, adp and atp, leading to activate or inhibit ampk: amp-binding results in allosteric activation of alpha catalytic subunit (prkaa1 or prkaa2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Skeletal Muscle, Brain, Heart, Liver

Identifier	Residue	Organism
SIGNOR-216471		Homo sapiens
pmid	sentence
20647423	Ampk recruitment and h2b ser36 phosphorylation colocalized within genes activated by ampk-dependent pathways, both in promoters and in transcribed regions.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-268480		Homo sapiens	U2-OS Cell
pmid	sentence
28561066	WIPI4 is stimulated by AMPK, NUAK2 and BRSK2. This finding is supported by the results of our kinome screening, which identified AMPK and the AMKP-related kinases NUAK2 and BRSK2, all of which function downstream of LKB1 (ref. 69) and stimulate the localization of WIPI4 to nascent autophagosomes.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-260097		Homo sapiens	U-937 Cell
pmid	sentence
31900833	Inactivation of AMPK suppressed the expression of ten-eleven translocation methylcytosine dioxygenase 2 (TET2) in tumor cells. Compound C-induced AMPK suppression causes downregulation TET2 and FOXP3 expression, leading to death of parental and HQ-selected U937 cells. These results confirm the connection of AMPK with the TET2–FOXP3 axis in modulating the survival of AML cells and suggest that suppression of the AMPK–TET2–FOXP3 axis suppresses the progression of AML and HQ-induced malignant transformation of AML cells.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, IDH-TET in AML, NPM1_new

Identifier	Residue	Organism
SIGNOR-139161		Homo sapiens
pmid	sentence
16054041	Gamma non-catalytic subunit mediates binding to amp, adp and atp, leading to activate or inhibit ampk: amp-binding results in allosteric activation of alpha catalytic subunit (prkaa1 or prkaa2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252886		Homo sapiens
pmid	sentence
17900900	The energy sensor amp-activated protein kinase (ampk) has been shown to directly phosphorylate foxo factors at six regulatory sites that are distinct from the akt phosphorylation sites, resulting in foxo activation

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, IDH-TET in AML, FLT3-ITD signaling, NPM1_new

Identifier	Residue	Organism	Cell Line
SIGNOR-216415		Homo sapiens	HEK-293 Cell
pmid	sentence
11171104	In contrast, the phosphorylation site mutations, ss24, 25aa and s182a, while having no effects on enzyme activity, are associated with nuclear redistribution of the subunit.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, IDH-TET in AML, AMPK Signaling, Autophagy, Citric acid cycle, Circadian clock, FLT3-ITD signaling, Glycolysis and Gluconeogenesis, Leptin Signaling, MTOR Signaling, NPM1_new

Identifier	Residue	Organism
SIGNOR-139179		Homo sapiens
pmid	sentence
16054041	Gamma non-catalytic subunit mediates binding to amp, adp and atp, leading to activate or inhibit ampk: amp-binding results in allosteric activation of alpha catalytic subunit (prkaa1 or prkaa2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-216418		Mus musculus	MEF Cell
pmid	sentence
21460634	AMP-activated protein kinase (AMPK), which is activated by LKB1/Strad/Mo25 upon high AMP levels, stimulates autophagy by inhibiting mTORC1.

Identifier	Residue	Organism	Cell Line
SIGNOR-216430		Homo sapiens	HEK-293 Cell
pmid	sentence
18439900	The phosphorylation of raptor by ampk is required for the inhibition of mtorc1 and cell-cycle arrest induced by energy stress.

Identifier	Residue	Organism
SIGNOR-209862		Homo sapiens
pmid	sentence
23863160	AMPK inhibits mTORC1 through two means: first, through phosphorylation of TSC2 to activate its GAP (GTPase-activating protein) activity that converts Rheb into an inactive GDP-bound state, thus switching off mitogenic stimulation of mTORC1 [31], and, secondly, through phosphorylation of raptor at Ser722 and Ser792, which leads to 14-3-3 protein binding and mTORC1 inhibition

Identifier	Residue	Organism
SIGNOR-216422		Homo sapiens
pmid	sentence
20083114	A recent study revealed that ampk can inhibit mtorc1 independently of tsc2 by phosphorylating raptor at ser863.

Publications:

4

Organism:

Mus Musculus, Homo Sapiens

Pathways:

AMPK Signaling, FLT3-ITD signaling

Identifier	Residue	Organism
SIGNOR-217475		Homo sapiens
pmid	sentence
21399626	Amp binding to the gamma-regulatory domain promotes phosphorylation by the upstream kinase, protects the enzyme against dephosphorylation, as well as causing allosteric activation.Adp also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. Atp promotes dephosphorylation of catalytic subunit, rendering the ampk enzyme inactive.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-217472		Homo sapiens
pmid	sentence
14976552	We demonstrated that lkb1 phosphorylates ampk on the activation loop threonine (thr172) within the catalytic subunit and activates ampk in vitro. Here, we have investigated whether lkb1 corresponds to the major ampkk activity present in cell extracts. Ampkk purified from rat liver corresponds to lkb1, and blocking lkb1 activity in cells abolishes ampk activation in response to different stimuli

Identifier	Residue	Organism
SIGNOR-217469		in vitro
pmid	sentence
14614828	We demonstrated that lkb1 phosphorylates ampk on the activation loop threonine (thr172) within the catalytic subunit and activates ampk in vitro. Here, we have investigated whether lkb1 corresponds to the major ampkk activity present in cell extracts. Ampkk purified from rat liver corresponds to lkb1, and blocking lkb1 activity in cells abolishes ampk activation in response to different stimuli

Publications:

2

Organism:

Homo Sapiens, In Vitro

Pathways:

Identifier	Residue	Organism
SIGNOR-139167		Homo sapiens
pmid	sentence
16054041	Gamma non-catalytic subunit mediates binding to amp, adp and atp, leading to activate or inhibit ampk: amp-binding results in allosteric activation of alpha catalytic subunit (prkaa1 or prkaa2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-273665		Homo sapiens	HEK-293 Cell
pmid	sentence
32978258	Upon activation by autophagy stimuli, IGPR-1 is phosphorylated at Ser220 via IKKβ. IGPR-1 acts as a pro-autophagy signaling receptor leading to activation of AMPK.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-139158		Homo sapiens	Adipocyte
pmid	sentence
16054041	Gamma non-catalytic subunit mediates binding to amp, adp and atp, leading to activate or inhibit ampk: amp-binding results in allosteric activation of alpha catalytic subunit (prkaa1 or prkaa2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Skeletal Muscle, Brain, Heart, Liver

Identifier	Residue	Organism
SIGNOR-217481		Homo sapiens
pmid	sentence
21399626	Atp promotes dephosphorylation of catalytic subunit, rendering the ampk enzyme inactive

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-267920		Homo sapiens
pmid	sentence
28538732	In KL cells, pharmacological activation of AMPK or expression of constitutively active AMPK reduced CPS1 mRNA and protein, and silencing AMPK increased CPS1 expression even in the presence of LKB1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-217749		Mus musculus	MEF Cell
pmid	sentence
16959574	GSK3 inhibits the mTOR pathway by phosphorylating TSC2 in a manner dependent on AMPK-priming phosphorylation

Publications:

1

Organism:

Mus Musculus

Pathways:

AMPK Signaling, MTOR Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275889
pmid	sentence
30420520	AMPK induces R388 hypomethylation by disrupting the association between PRMT6 and SIRT7.\|Protein arginine methyltransferase 6 (PRMT6) directly interacts with and methylates SIRT7

Publications:

1

Identifier	Residue	Organism	Cell Line
SIGNOR-216411		Homo sapiens	HEK-293 Cell
pmid	sentence
17728241	Mutation of serine 108 to alanine, an autophosphorylation site within the glycogen binding domain of the beta1 subunit, almost completely abolishes activation of ampk by a-769662 in cells and in vitro, while only partially reducing activation by ampk

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, IDH-TET in AML, AMPK Signaling, Autophagy, Citric acid cycle, Circadian clock, FLT3-ITD signaling, Glycolysis and Gluconeogenesis, Leptin Signaling, MTOR Signaling, NPM1_new

Identifier	Residue	Organism	Cell Line
SIGNOR-256137		Mus musculus	Myoblast
pmid	sentence
18477450	Glucose restriction (GR) impaired differentiation of skeletal myoblasts and was associated with activation of the AMP-activated protein kinase (AMPK).

Publications:

1

Organism:

Mus Musculus

Pathways:

Acute Myeloid Leukemia, IDH-TET in AML

Identifier	Residue	Organism
SIGNOR-217484		Homo sapiens
pmid	sentence
21460634	Ulk1/2 in turn phosphorylates all three subunits of ampk and thereby negatively regulates its activity.

Publications:

1

Organism:

Homo Sapiens

Pathways:

MTOR Signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-217496		Homo sapiens	HeLa Cell
pmid	sentence
15980064	These data indicate that the camkks function in intact cells as ampkks, predicting wider roles for these kinases in regulating ampk activity in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-217478		Homo sapiens
pmid	sentence
16879084	The activation of the ampk pathway by exendin-4 was induced by aicar, which was inhibited by compound c.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-256111		Rattus norvegicus
pmid	sentence
17023420	These agents also enhanced phosphorylation of alpha-Ser(485/491) by the cAMP-dependent protein kinase. AMPK alpha-Ser(485/491) phosphorylation was necessary but not sufficient for inhibition of AMPK activity in response to forskolin/isobutylmethylxanthine.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Organism
SIGNOR-209913		Homo sapiens
pmid	sentence
23863160	Under energy deprivation, AMPK positively regulates ULK1 to induce autophagy, with various studies revealing that AMPK binds to and phosphorylates ULK1

Publications:

1

Organism:

Homo Sapiens

Pathways:

AMPK Signaling, Leptin Signaling, MTOR Signaling

Identifier	Residue	Organism
SIGNOR-139176		Homo sapiens
pmid	sentence
16054041	Gamma non-catalytic subunit mediates binding to amp, adp and atp, leading to activate or inhibit ampk: amp-binding results in allosteric activation of alpha catalytic subunit (prkaa1 or prkaa2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-216619		Homo sapiens
pmid	sentence
22207502	Ampk phosphorylates and activates theinsulinreceptor, providing a direct link between ampk and theinsulin pathway.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle

Pathways:

Identifier	Residue	Organism
SIGNOR-260096		Homo sapiens
pmid	sentence
30274374	AMPK inhibits the mTOR pathway through phosphorylation and activation of tuberous sclerosis protein 2 (TSC2) and causes direct activation of unc-51-like autophagy activating kinase 1 (ULK1) via phosphorylation of Ser555, thus promoting initiation of autophagy.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, IDH-TET in AML, FLT3-ITD signaling, Leptin Signaling, MTOR Signaling

Identifier	Residue	Organism
SIGNOR-209916		Homo sapiens
pmid	sentence
21460634	Here we report that ulk1/2 in turn phosphorylates all three subunits of ampk and thereby negatively regulates its activity. Thus, we propose that ulk1 is not only involved in the induction of autophagy, but also in terminating signaling events that trigger autophagy. In our model, phosphorylation of ampk by ulk1 represents a negative feedback circuit.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism	Cell Line
SIGNOR-209894		Homo sapiens	Myotube
pmid	sentence
20810907	L6 myotubes were incubated in serum-containing or serum-free medium for 3 h. Levels of phosphorylated AMPK, Akt, and ATM were greater in serum-starved cells than in control cells.

Identifier	Residue	Organism
SIGNOR-209796		Homo sapiens
pmid	sentence
23000343	Starvation-induced autophagy is regulated by mitochondrial reactive oxygen species leading to AMPK activationSTARV

Publications:

2

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, IDH-TET in AML

Identifier	Residue	Organism	Cell Line
SIGNOR-277766		Homo sapiens	Pancreatic Cancer Cell
pmid	sentence
29572236	The discovery that AMPK activation is a general requirement for macropinosome formation in cancer cells dramatically extends our understanding of the regulation of this process. By increasing RAC1-GTP levels, AMPK activation stimulates macropinosome formation (Fig. 2I–K; Supplementary Fig. S5).

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia

Identifier	Residue	Organism
SIGNOR-277765		Homo sapiens
pmid	sentence
32745890	Glucose deprivation, activates the glucose level–sensing kinase, AMPK, which in turn influences Rac1-dependent macropinocytosis. In this context macropinosomes take up necrotic cell debris as a rich nutrient source to fuel tumor cell growth

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-216484		Homo sapiens
pmid	sentence
17900900	The energy sensor amp-activated protein kinase (ampk) has been shown to directly phosphorylate foxo factors at six regulatory sites that are distinct from the akt phosphorylation sites, resulting in foxo activation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-255951		Mus musculus
pmid	sentence
20660302	P38 MAPK mediates the effect of AMPK on Gr induced transcriptional activity

Publications:

1

Organism:

Mus Musculus

Pathways:

FLT3-ITD signaling

Identifier	Residue	Organism
SIGNOR-255338		Mus musculus
pmid	sentence
23531613	AMPK phosphorylation was increased nearly fourfold (Fig. 2C) with the high dose of IL-6

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-238824		Mus musculus
pmid	sentence
18477450	Activated AMPK was required to promote GR-induced transcription of the NAD+ biosynthetic enzyme Nampt

Publications:

1

Organism:

Mus Musculus

Pathways:

Identifier	Residue	Organism
SIGNOR-217487		Homo sapiens
pmid	sentence
21460634	We could prove that ulk1-mediated phosphorylation of ampk reduced its level of phosphorylation at t172 of the _-subunit and hence interferes with its catalytic activity. I

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-216658		Homo sapiens	Neuron
pmid	sentence
21565617	We show here that in liver, class iia hdacs (hdac4, 5, and 7) are phosphorylated and excluded from the nucleus by ampk family kinases.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle

Identifier	Residue	Organism
SIGNOR-209929		Homo sapiens
pmid	sentence
20640476	The decreased glycogen synthesis rates upon acute AMPK activation are generally coupled to an increase in the glycolytic flux, thanks to the activation of 6-phosphofructo-2-kinase (PFK-2) through direct phosphorylation on Ser466 [35]. PFK-2 catalyzes the synthesis of fructose 2,6-bisphosphate, a potent stimulator of glycolysis. Therefore, activation of AMPK rapidly mobilizes glucose into ATP-generating processes.

Publications:

1

Organism:

Homo Sapiens

Pathways:

AMPK Signaling

Identifier	Residue	Organism
SIGNOR-139164		Homo sapiens
pmid	sentence
16054041	Gamma non-catalytic subunit mediates binding to amp, adp and atp, leading to activate or inhibit ampk: amp-binding results in allosteric activation of alpha catalytic subunit (prkaa1 or prkaa2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-216478		Homo sapiens
pmid	sentence
18394876	The energy sensor AMP-activated protein kinase (AMPK) has been shown to directly phosphorylate FoxO factors at six regulatory sites that are distinct from the Akt phosphorylation sites, resulting in FoxO activation.

Publications:

1

Organism:

Homo Sapiens

Pathways: