Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-259861	Ser102	LQTVIRTsPSSLVAF	Homo sapiens
pmid	sentence
26190112	AMPK phosphorylates GLI1 at serines 102 and 408 and threonine 1074. Mutation of these three sites into alanine prevents phosphorylation by AMPK. This in turn leads to increased GLI1 protein stability, transcriptional activity, and oncogenic potency.

Identifier	Residue	Sequence	Organism
SIGNOR-259863	Ser408	GPLPRAPsISTVEPK	Homo sapiens
pmid	sentence
26190112	AMPK phosphorylates GLI1 at serines 102 and 408 and threonine 1074. Mutation of these three sites into alanine prevents phosphorylation by AMPK. This in turn leads to increased GLI1 protein stability, transcriptional activity, and oncogenic potency.

Identifier	Residue	Sequence	Organism
SIGNOR-259860	Ser408	GPLPRAPsISTVEPK	Homo sapiens
pmid	sentence
26190112	AMPK phosphorylates GLI1 at serines 102 and 408 and threonine 1074. Mutation of these three sites into alanine prevents phosphorylation by AMPK. This in turn leads to increased GLI1 protein stability, transcriptional activity, and oncogenic potency.

Identifier	Residue	Sequence	Organism
SIGNOR-259862	Thr1074	QRGSSGHtPPPSGPP	Homo sapiens
pmid	sentence
26190112	AMPK phosphorylates GLI1 at serines 102 and 408 and threonine 1074. Mutation of these three sites into alanine prevents phosphorylation by AMPK. This in turn leads to increased GLI1 protein stability, transcriptional activity, and oncogenic potency.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-128629	Ser105	QAARKLLsREKQPPI	Homo sapiens
pmid	sentence
15342649	Ampk phosphorylated importin alpha1 on ser(105). Accordingly, expression of importin alpha1 proteins bearing k22r or s105a mutations failed to mediate the nuclear import of hur in intact cells. Our results point to importin alpha1 as a critical downstream target of ampk and key mediator of ampk-triggered hur nuclear import.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-157553	Ser108	SKLPLTRsHNNFVAI	Homo sapiens
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 amp

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-160838	Ser1177	TSRIRTQsFSLQERQ	Homo sapiens	HeLa Cell
pmid	sentence
18303014	The central finding of this report is that rosiglitazone rapidly stimulates no production and enos ser-1177 phosphorylation in an ampk-dependent manner

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250400	Ser1201	IPTLNRMsFSSNLNH	Rattus norvegicus
pmid	sentence
7907095	We have isolated and purified from rat livers a novel kinase that phosphorylates and inactivates the carboxylase Ser1200 isphosphorylated by both CAMP-dependent protein kinase and AMP-activated protein kinase

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-276467	Ser121	LMRRSTVsLLDTYQK	in vitro
pmid	sentence
23871434	These results indicate that HIPK2 is a substrate of AMPKα2 in vitro and in vivo. Site-directed mutagenesis of Thr112 and Ser114 in the N terminus, and Thr1107 in the C terminus markedly reduced HIPK2 phosphorylation by AMPKα2 in vitro (Figure S5J).

Identifier	Residue	Sequence	Organism
SIGNOR-276469	Thr1114	APAALGStGTVAHLV	in vitro
pmid	sentence
23871434	These results indicate that HIPK2 is a substrate of AMPKα2 in vitro and in vivo. Site-directed mutagenesis of Thr112 and Ser114 in the N terminus, and Thr1107 in the C terminus markedly reduced HIPK2 phosphorylation by AMPKα2 in vitro (Figure S5J).

Identifier	Residue	Sequence	Organism
SIGNOR-276468	Thr119	HNLMRRStVSLLDTY	in vitro
pmid	sentence
23871434	These results indicate that HIPK2 is a substrate of AMPKα2 in vitro and in vivo. Site-directed mutagenesis of Thr112 and Ser114 in the N terminus, and Thr1107 in the C terminus markedly reduced HIPK2 phosphorylation by AMPKα2 in vitro (Figure S5J).

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-259857	Ser122	GAKRVIIsAPSADAP	Mus musculus
pmid	sentence
26626483	Under glucose starvation, but not amino acid starvation, cytoplasmic GAPDH is phosphorylated on Ser122 by activated AMPK. This causes GAPDH to redistribute into the nucleus. Inside the nucleus, GAPDH interacts directly with Sirt1, displacing Sirt1's repressor and causing Sirt1 to become activated.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277593	Ser136	AAAGGQGsAVAAEAE	Homo sapiens	Hep-G2 Cell
pmid	sentence
35538889	Mechanistically, AMPKα1 directly phosphorylated prolyl hydroxylase domain-containing (PHD)2 at serines 61 and 136, which suppressed PHD2-dependent hydroxylation of hypoxia-inducible factor (HIF)1α and subsequent regulation of hepatic hepcidin-related iron signalling.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277592	Ser61	HKLVCQGsEGALGHG	Homo sapiens	Hep-G2 Cell
pmid	sentence
35538889	Mechanistically, AMPKα1 directly phosphorylated prolyl hydroxylase domain-containing (PHD)2 at serines 61 and 136, which suppressed PHD2-dependent hydroxylation of hypoxia-inducible factor (HIF)1α and subsequent regulation of hepatic hepcidin-related iron signalling.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-135960	Ser15	PSVEPPLsQETFSDL	Homo sapiens
pmid	sentence
15866171	Ampk activation induces phosphorylation of p53 on serine 15, and this phosphorylation is required to initiate ampk-dependent cell-cycle arrest

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-245953	Ser155	GRLKRERsMSENAVR	Homo sapiens
pmid	sentence
26816379	A screen for substrates of AMPK identified mitochondrial fission factor (MFF), a mitochondrial outer-membrane receptor for DRP1, the cytoplasmic guanosine triphosphatase that catalyzes mitochondrial fission.

Identifier	Residue	Sequence	Organism
SIGNOR-249656	Ser172	GQLVRNDsLWHRSDS	Homo sapiens
pmid	sentence
26816379	A screen for substrates of AMPK identified mitochondrial fission factor (MFF), a mitochondrial outer-membrane receptor for DRP1, the cytoplasmic guanosine triphosphatase that catalyzes mitochondrial fission.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-176487	Ser155	FPLRKTVsEPNLKLR	Homo sapiens
pmid	sentence
21892142	Another recently described set of transcriptional regulators targeted by ampk and its related family members across a range of eukaryotes are the class iia family of histone deacetylases (hdacs).

Identifier	Residue	Sequence	Organism
SIGNOR-176491	Ser358	WPLSRTRsEPLPPSA	Homo sapiens
pmid	sentence
21892142	Another recently described set of transcriptional regulators targeted by ampk and its related family members across a range of eukaryotes are the class iia family of histone deacetylases (hdacs).

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-200250	Ser158	REGTRVQsVEQIREV	Homo sapiens
pmid	sentence
23291169	We found that an activated amp-activated protein kinase (ampk) phosphorylates ctbp1 on ser-158 upon metabolic stresses. Moreover, ampk-mediated phosphorylation of ctbp1 (s158) attenuates the repressive function of ctbp1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-176426	Ser170	PSALNRTsSDSALHT	Homo sapiens
pmid	sentence
21892142	Collectively, these findings suggest ampk suppresses glucose production through two transcriptional effects:reduced expression of creb targets via crtc inactivation and reduced expression of foxo target genes via class iia hdac inactivation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265729	Ser180	GGAKRVTsIADRLNV	Homo sapiens	LK-87 Cell
pmid	sentence
29074724	We demonstrate here that glucose deprivation or hypoxia results in the AMPK-mediated phosphorylation of phosphoribosyl pyrophosphate synthetase 1 (PRPS1) S180 and PRPS2 S183, leading to conversion of PRPS hexamers to monomers and thereby inhibiting PRPS1/2 activity, nucleotide synthesis, and nicotinamide adenine dinucleotide (NAD) production.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265731	Ser180	GGAKRVTsIADRLNV	Homo sapiens	LK-87 Cell
pmid	sentence
29074724	We demonstrate here that glucose deprivation or hypoxia results in the AMPK-mediated phosphorylation of phosphoribosyl pyrophosphate synthetase 1 (PRPS1) S180 and PRPS2 S183, leading to conversion of PRPS hexamers to monomers and thereby inhibiting PRPS1/2 activity, nucleotide synthesis, and nicotinamide adenine dinucleotide (NAD) production.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-264782	Ser190	MWFIETAsFIDVDDE	in vitro
pmid	sentence
28143904	Together, these results indicate that AMPK phosphorylated DNMT1-Ser730, RBBP7-Ser314, and HAT1-Ser190\|AMPK increased HAT1 activity through phosphorylation of HAT1-Ser190 and RBBP7-Ser314

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-275439	Ser214	GGKERPGsKEEVDED	in vitro
pmid	sentence
10090741	We have studied the relationship between the phosphorylation oftau by several kinases (MARK, PKA, MAPK, GSK3) and its assembly into PHFs. By contrast, MARK and PKA phosphorylate several sites within the repeats (notably theKXGS motifs including Ser262, Ser324, and Ser356, plus Ser320); in addition PKA phosphorylates somesites in the flanking domains, notably Ser214. This type of phosphorylation strongly reduces tau’s affinityfor microtubules, and at the same time inhibits tau’s assembly into PHFs.

Identifier	Residue	Sequence	Organism
SIGNOR-275440	Ser355	EADLPEPsEKQPAAA	in vitro
pmid	sentence
10090741	We have studied the relationship between the phosphorylation oftau by several kinases (MARK, PKA, MAPK, GSK3) and its assembly into PHFs. By contrast, MARK and PKA phosphorylate several sites within the repeats (notably theKXGS motifs including Ser262, Ser324, and Ser356, plus Ser320); in addition PKA phosphorylates somesites in the flanking domains, notably Ser214. This type of phosphorylation strongly reduces tau’s affinityfor microtubules, and at the same time inhibits tau’s assembly into PHFs.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-159048	Ser237	RPMRKSFsQPGLRSL	Homo sapiens
pmid	sentence
17995453	In rat l6 myotubes, endogenous tbc1d1 is strongly phosphorylated on ser237 and binds to 14-3-3s in response to the ampk activators aicar

Publications:

1

Organism:

Homo Sapiens

Tissue:

Myotube

Identifier	Residue	Sequence	Organism
SIGNOR-183528	Ser242	SKFTRWGsQGERGKD	Homo sapiens
pmid	sentence
19170765	Amp-activated protein kinase phosphorylates glutamine : fructose-6-phosphate amidotransferase 1 at ser243 to modulate its enzymatic activityhe 2-dg induced phosphorylation of gfat1 . The assay of the gfat enzymatic activity in the cell lysates indicated that the 2-dg-treatment inhibited the enzymatic activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277299	Ser257	GLHRAEQsLHDLQER	Mus musculus	Fibroblast
pmid	sentence
31381180	STIM1 is a novel exercise‐regulated AMPK substrate. Phosphorylation of STIM1 by AMPK suppresses SOCE

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-176479	Ser259	FPLRKTAsEPNLKVR	Homo sapiens
pmid	sentence
21892142	Another recently described set of transcriptional regulators targeted by ampk and its related family members across a range of eukaryotes are the class iia family of histone deacetylases (hdacs)

Identifier	Residue	Sequence	Organism
SIGNOR-176483	Ser498	RPLSRTQsSPLPQSP	Homo sapiens
pmid	sentence
21892142	Another recently described set of transcriptional regulators targeted by ampk and its related family members across a range of eukaryotes are the class iia family of histone deacetylases (hdacs)

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-86133	Ser259	SQRQRSTsTPNVHMV	Homo sapiens
pmid	sentence
11971957	Mutation of serine 259 increased the basal raf-1 activity and rendered it largely resistant to inhibition by pka.

Identifier	Residue	Sequence	Organism
SIGNOR-47148	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. The catalytic subunit of PKA also phosphorylated Ser621 in vitro, while its overexpression in intact cells resulted in increased phosphorylation of Ser621 and decreased activity of Raf-1. These results suggest that phosphorylation of Ser621 inactivates Raf-1, but do not prove that PKA is responsible for this in vivo.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-158490	Ser261	CNLSRVDsTTCLFPV	Homo sapiens
pmid	sentence
17941647	Amp-activated protein kinase and calcium/calmodulin-dependent kinase ii were identified to phosphorylate specifically ser243 in vitro. Phosphorylation by these two kinases results in an increase of enzymatic activity by 1.4-fold. These findings suggest for the first time that hgfat1 may be regulated by kinases other than pka.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-275438	Ser267	RVQSKIGsLDNITHV	in vitro
pmid	sentence
10090741	We have studied the relationship between the phosphorylation oftau by several kinases (MARK, PKA, MAPK, GSK3) and its assembly into PHFs. By contrast, MARK and PKA phosphorylate several sites within the repeats (notably theKXGS motifs including Ser262, Ser324, and Ser356, plus Ser320); in addition PKA phosphorylates somesites in the flanking domains, notably Ser214. This type of phosphorylation strongly reduces tau’s affinityfor microtubules, and at the same time inhibits tau’s assembly into PHFs.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276837	Ser295	RYHGHSMsDPGVSYR	in vitro
pmid	sentence
33022274	AMPKα phosphorylates PDHA subunit on Ser295 and Ser314 to activate PDH complex

Identifier	Residue	Sequence	Organism
SIGNOR-276839	Ser314	IQEVRSKsDPIMLLK	in vitro
pmid	sentence
33022274	AMPKα phosphorylates PDHA subunit on Ser295 and Ser314 to activate PDH complex

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-278381	Ser30	EDLQEVLsSDENGGT	Homo sapiens
pmid	sentence
27650555	Here, we report that phosphorylation of CHOP at Ser30 by AMPK\u03b11 triggers CHOP degradation resulting in reduced macrophage apoptosis and subsequent ameliorated plaque vulnerability in vivo .\|XREF_FIG showed the deletion of Ampkalpha1 but not Ampkalpha2 significantly increased CHOP protein levels in macrophages.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-259864	Ser30	EDLQEVLsSDENGGT	Mus musculus
pmid	sentence
27650555	Here, we report that phosphorylation of CHOP at Ser30 by AMPKα1 triggers CHOP degradation resulting in reduced macrophage apoptosis and subsequent ameliorated plaque vulnerability in vivo.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-101101	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-264784	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
SIGNOR-273011	Ser326	SARKRSAsADNLTLP
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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277264	Ser347	VQMQREWsFARTHPL	Homo sapiens	U2-OS Cell
pmid	sentence
27449087	FANCA was phosphorylated by AMPK at S347 and phosphorylation increased with MMC treatment. MMC-induced FANCD2 monoubiquitination and nuclear foci formation were compromised in a U2OS cell line that stably overexpressed the S347A mutant form of FANCA compared to wild-type FANCA-overexpressing cells, indicating a requirement for FANCA phosphorylation at S347 for proper activation of the FA/BRCA pathway.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-173118	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-250402	Ser366	SPQVRTLsGSRPPLL	in vitro
pmid	sentence
14709557	AMPK can phosphorylate three sites in eEF2 kinase in vitro. Of these, Ser-398 appears to be more efficiently phosphorylated than either Ser-78 or Ser-366. Ser-78 and Ser-366 do not appear to be phosphorylated by AMPK within cells. Ser-366 serves to decrease the activity of eEF2 kinase

Identifier	Residue	Sequence	Organism
SIGNOR-250314	Ser78	SSGSPANsFHFKEAW	in vitro
pmid	sentence
14709557	AMPK can phosphorylate three sites in eEF2 kinase in vitro. Of these, Ser-398 appears to be more efficiently phosphorylated than either Ser-78 or Ser-366. Ser-78 and Ser-366 do not appear to be phosphorylated by AMPK within cells. Ser-366 serves to decrease the activity of eEF2 kinase

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-277494	Ser374	GDTLLGLsDSEVEEL	in vitro
pmid	sentence
31805502	MS-based analysis of immunoprecipitated Nrf2 revealed serine 374, 408 and 433 in human Nrf2 to be hyperphosphorylated as a function of activated AMPK. A direct phosphate-transfer by AMPK to those sites was indicated by in vitro kinase assays with recombinant proteins as well as interaction of AMPK and Nrf2 in cells, evident by co-immunoprecipitation. Mutation of serine 374, 408 and 433 to alanine did not markedly affect half-life, nuclear accumulation or induction of reporter gene expression upon Nrf2 activation with sulforaphane. However, some selected endogenous Nrf2 target genes responded with decreased induction when the identified phosphosites were mutated, whereas others remained unaffected.

Identifier	Residue	Sequence	Organism
SIGNOR-277496	Ser408	GDMVQPLsPSQGQST	in vitro
pmid	sentence
31805502	MS-based analysis of immunoprecipitated Nrf2 revealed serine 374, 408 and 433 in human Nrf2 to be hyperphosphorylated as a function of activated AMPK. A direct phosphate-transfer by AMPK to those sites was indicated by in vitro kinase assays with recombinant proteins as well as interaction of AMPK and Nrf2 in cells, evident by co-immunoprecipitation. Mutation of serine 374, 408 and 433 to alanine did not markedly affect half-life, nuclear accumulation or induction of reporter gene expression upon Nrf2 activation with sulforaphane. However, some selected endogenous Nrf2 target genes responded with decreased induction when the identified phosphosites were mutated, whereas others remained unaffected.

Identifier	Residue	Sequence	Organism
SIGNOR-277495	Ser433	PEKELPVsPGHRKTP	in vitro
pmid	sentence
31805502	MS-based analysis of immunoprecipitated Nrf2 revealed serine 374, 408 and 433 in human Nrf2 to be hyperphosphorylated as a function of activated AMPK. A direct phosphate-transfer by AMPK to those sites was indicated by in vitro kinase assays with recombinant proteins as well as interaction of AMPK and Nrf2 in cells, evident by co-immunoprecipitation. Mutation of serine 374, 408 and 433 to alanine did not markedly affect half-life, nuclear accumulation or induction of reporter gene expression upon Nrf2 activation with sulforaphane. However, some selected endogenous Nrf2 target genes responded with decreased induction when the identified phosphosites were mutated, whereas others remained unaffected.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-20971	Ser385	RRRKKRTsIETNIRV	Homo sapiens
pmid	sentence
1684878	Mitosis-specific phosphorylation site in the homeodomain of oct-1 was phosphorylated in vitro by protein kinase a. Pka-mediated phosphorylation event was identified in the cns-specific pou domain protein brn-2/n-oct-3/pou3f2 (nieto et al. 2007). In this case, the modification, at a position homologous to oct1 s385, was found to alter binding specificity for complex dimeric sites.

Identifier	Residue	Sequence	Organism
SIGNOR-53254	Ser385	RRRKKRTsIETNIRV	Homo sapiens
pmid	sentence
9368058	Mitosis-specific phosphorylation site in the homeodomain of oct-1 was phosphorylated in vitro by protein kinase a. Pka-mediated phosphorylation event was identified in the cns-specific pou domain protein brn-2/n-oct-3/pou3f2 (nieto et al. 2007). In this case, the modification, at a position homologous to oct1 s385, was found to alter binding specificity for complex dimeric sites.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-197734	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
SIGNOR-250157	Ser398	DSLPSSPsSATPHSQ	in vitro
pmid	sentence
14709557	Stimulation of the AMP-activated Protein Kinase Leads to Activation of Eukaryotic Elongation Factor 2 Kinase and to Its Phosphorylation at a Novel Site, Serine 398. phosphorylation of eEF2 kinase at Ser-398 leads to an increase in its activity.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-249667	Ser399	DNITLPPsQPSPTGG	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-249677	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-249681	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-249684	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-249687	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-238804	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	Organism
SIGNOR-219247		Caenorhabditis elegans
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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-255755
pmid	sentence
22848740	When AMPK is stimulated, pre-existing FOXO3 becomes reverted toward an active form.

Publications:

8

Organism:

Homo Sapiens, Caenorhabditis Elegans,

Identifier	Residue	Sequence	Organism
SIGNOR-252975	Ser399	DNITLPPsQPSPTGG	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-252976	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-252977	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-252978	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	Cell Line
SIGNOR-252979	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-252980	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-252983		Caenorhabditis elegans
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, Caenorhabditis Elegans

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-89760	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

Identifier	Residue	Sequence	Organism
SIGNOR-84061	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-260012	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.

Publications:

2

Organism:

Homo Sapiens, Rattus Norvegicus

Tissue:

Heart

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277471	Ser467	LQLYQVDsRTYLLDF	Homo sapiens	Endometrial Cancer Cell Line
pmid	sentence
31358902	Specifically, we found that PIM2 bound to AMPKα1, and directly phosphorylated it on Thr467. Phosphorylation of AMPKα1 by PIM2 led to decreasing AMPKα1 kinase activity, which in turn promoted aerobic glycolysis and tumor growth.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-150590	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	Cell Line
SIGNOR-256110	Ser486	DDEITEAKsGTATPQRS	Rattus norvegicus	INS-1 Cell
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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-256112	Ser491	SSTPQRSCsAAGLHRPR	Rattus norvegicus	INS-1 Cell
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.

Identifier	Residue	Sequence	Organism
SIGNOR-259865	Ser496	ATPQRSGsVSNYRSC	Homo sapiens
pmid	sentence
27784766	These data indicate a novel regulatory role of PKC to inhibit AMPKα1 in human cells. As PKC activation is associated with insulin resistance and obesity, PKC may underlie the reduced Protein kinase C phosphorylates AMP-activated protein kinase α1 Ser487. \| AMPK activity reported in response to overnutrition in insulin-resistant metabolic and vascular tissues.

Publications:

3

Organism:

Rattus Norvegicus, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-256114	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-276461	Ser496	ATPQRSGsVSNYRSC	in vitro
pmid	sentence
27784766	Purified PKC and Akt both phosphorylated AMPKα1 Ser487 in vitro with similar efficiency. PKC activation was associated with reduced AMPK activity, as inhibition of PKC increased AMPK activity and phorbol esters inhibited AMPK, an effect lost in cells expressing mutant AMPKα1 Ser487Ala. Consistent with a pathophysiological role for this modification, AMPKα1 Ser487 phosphorylation was inversely correlated with insulin sensitivity in human muscle.

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

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276460	Ser496	ATPQRSGsVSNYRSC	in vitro
pmid	sentence
27784766	Purified PKC and Akt both phosphorylated AMPKα1 Ser487 in vitro with similar efficiency. PKC activation was associated with reduced AMPK activity, as inhibition of PKC increased AMPK activity and phorbol esters inhibited AMPK, an effect lost in cells expressing mutant AMPKα1 Ser487Ala. Consistent with a pathophysiological role for this modification, AMPKα1 Ser487 phosphorylation was inversely correlated with insulin sensitivity in human muscle.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276459	Ser496	ATPQRSGsVSNYRSC	in vitro
pmid	sentence
27784766	Purified PKC and Akt both phosphorylated AMPKα1 Ser487 in vitro with similar efficiency. PKC activation was associated with reduced AMPK activity, as inhibition of PKC increased AMPK activity and phorbol esters inhibited AMPK, an effect lost in cells expressing mutant AMPKα1 Ser487Ala. Consistent with a pathophysiological role for this modification, AMPKα1 Ser487 phosphorylation was inversely correlated with insulin sensitivity in human muscle.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-259866	Ser510	SPVSRTPsLPAVDTS	Homo sapiens
pmid	sentence
27256105	Mechanically, we found that AMPKα1 directly phosphorylated protein inhibitor of activated STAT-1 (PIAS1), the SUMO E3-ligase of Runx2, at serine 510, to promote its SUMO E3-ligase activity. Finally, mutation of protein inhibitor of activated STAT-1 at serine 510 suppressed m

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-228654	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-156780	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:

Mus Musculus, Homo Sapiens

Tissue:

Skeletal Muscle, Muscle, Skeletal Muscle

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277799	Ser559	VQRKVSGsRGSFCKA	Homo sapiens	HEK-293 Cell
pmid	sentence
30279167	Thus, AMPK directly phosphorylates the  subunit of KV1.5 at Ser592 and, to a lesser extent, at Ser559

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277813	Ser559	VQRKVSGsRGSFCKA	Homo sapiens	HEK-293 Cell
pmid	sentence
30279167	Thus, AMPK directly phosphorylates the  subunit of KV1.5 at Ser592 and, to a lesser extent, at Ser559

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277800	Ser592	KCNVKAKsNVDLRRS	Homo sapiens	HEK-293 Cell
pmid	sentence
30279167	Thus, AMPK directly phosphorylates the  subunit of KV1.5 at Ser592 and, to a lesser extent, at Ser560

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277814	Ser592	KCNVKAKsNVDLRRS	Homo sapiens	HEK-293 Cell
pmid	sentence
30279167	Thus, AMPK directly phosphorylates the  subunit of KV1.5 at Ser592 and, to a lesser extent, at Ser560

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-275547	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-174681	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-188403	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-271822	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-176472	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

Identifier	Residue	Sequence	Organism
SIGNOR-264783	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-259858	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-259867	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	Cell Line
SIGNOR-277207	Ser76	DTLPRTPsYSISSTL	Homo sapiens	HCT-116 Cell
pmid	sentence
26876938	Under energy stress, USP10 activity in turn is enhanced through AMPK-mediated phosphorylation of Ser76 of USP10.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-161375	Ser792	DKMRRASsYSSLNSL	Mus musculus	MEF 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-173035		Homo sapiens
pmid	sentence
21460634	Ampk in turn inactivates mtorc1 directly by phosphorylating raptor and indirectly by phosphorylating tsc2.

Publications:

2

Organism:

Mus Musculus, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-265991	Ser801	KLRRRTFsLTEVRGQ	in vitro
pmid	sentence
28992084	We found that the strong direct substrate KIF4A is phosphorylated by AMPK at Ser801.Using in vitro kinase assays, we found that active AMPK and Aurora B phosphorylated KIF4A at Ser801 and Thr799 respectively in a time-dependent manner (Figure 5D). KIF4A is phosphoregulated by AMPK and Aurora B. Although AMPK phosphorylation increased the ATPase activity of KIF4A, Aurora B phosphorylation resulted in a stronger increase (Figure 5I), which might be consistent with the more powerful kinase function of Aurora B during mitosis.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-184052	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277475	Ser82	SLRQTYNsCARLCLN	Homo sapiens	SK-BR-3 Cell
pmid	sentence
31406304	Glucose deprivation activates AMPK kinase to phosphorylate β-TrCP1 and promotes the subsequent ubiquitination and degradation of β-TrCP1 by β-TrCP2, but does not promote β-TrCP2 degradation by β-TrCP1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-58255	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-176637	Ser89	SELLRSGsSPNLNMG	Homo sapiens	Macrophage, Leukemia Cell, Monocyte
pmid	sentence
21940946	The mechanism of ampk-mediated anti- inflammation involves the induction of p300 ser89 phosphor- ylation and subsequent inactivation of p300 hat activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-78891	Ser9	NYLRRRLsDSNFMAN	Homo sapiens
pmid	sentence
10880969	It has been reported that site 1 of syn i can be phosphorylated by pka. Pka-mediated synapsin i ser9 phosphorylation occurs in response to cgs 21680 treatment. Results show that the adenosine a2a receptor agonist, cgs 21680, increases neurotransmitter release, in particular, glutamate and noradrenaline and such response is mediated by protein kinase a activation, which in turn increased synapsin i phosphorylation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-161783	Ser92	VAELTSLsDEDSGKG	Homo sapiens
pmid	sentence
19923321	Serines 11 and 92 participate in the control of snail1 stability and positively regulate snail1 repressive function and its interaction with msin3a corepressor. Furthermore, serines 11 and 92 are required for snail1-mediated emt and cell viability, respectively. Pka and ck2 have been characterized as the main kinases responsible for in vitro snail1 phosphorylation at serine 11 and 92, respectively.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-161779	Ser92	SFLVRKPsDPNRKPN	Homo sapiens
pmid	sentence
19923321	Serines 11 and 92 participate in the control of snail1 stability and positively regulate snail1 repressive function and its interaction with msin3a corepressor. Furthermore, serines 11 and 92 are required for snail1-mediated emt and cell viability, respectively. Pka and ck2 have been characterized as the main kinases responsible for in vitro snail1 phosphorylation at serine 11 and 92, respectively.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-256134	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277432	Thr101	IVLNKGKtIFRFSAT	Homo sapiens	HEK-293T Cell
pmid	sentence
30759345	AMPK was found to phosphorylate Nav1.5 at threonine (T) 101, which then regulates the interaction between Nav1.5 and the autophagic adaptor protein, microtubule-associated protein 1 light chain 3 (LC3), by exposing the LC3-interacting region adjacent to T101 in Nav1.5.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-159639	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-275864	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
SIGNOR-122721	Thr183	SDGEFLRtSCGSPNY	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).

Identifier	Residue	Sequence	Organism
SIGNOR-139297	Thr183	SDGEFLRtSCGSPNY	in vitro
pmid	sentence
16054095	The AMP-activated protein kinase (AMPK) is a critical regulator of energy balance at both the cellular and whole-body levels. Two upstream kinases have been reported to activate AMPK in cell-free assays, i.e., the tumor suppressor LKB1 and calmodulin-dependent protein kinase kinase.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-176602	Thr183	SDGEFLRtSCGSPNY	Homo sapiens
pmid	sentence
21918180	Ampka1 activators increased phosphorylation level and cytoplasmic localization (reduced nuclear/cytoplasmic ratio). Ampka1 activators reduced rna synthesis in the nucleoli.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-138360	Thr183	SDGEFLRtSCGSPNY	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	Sequence	Organism
SIGNOR-176598	Thr183	SDGEFLRtSCGSPNY	Homo sapiens
pmid	sentence
21918180	Ampka1 activators increased phosphorylation level and cytoplasmic localization (reduced nuclear/cytoplasmic ratio). Ampka1 activators reduced rna synthesis in the nucleoli.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-176594	Thr183	SDGEFLRtSCGSPNY	Homo sapiens
pmid	sentence
21918180	Ampka1 activators increased phosphorylation level and cytoplasmic localization (reduced nuclear/cytoplasmic ratio). Ampka1 activators reduced rna synthesis in the nucleoli.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-259859	Thr198	PGLRRRQt	Mus musculus
pmid	sentence
30033086	P27Kip1-Mediated Cell Survival Is Dependent on AMPK-Specific Thr198 Phosphorylation\|AMPK-dependent phosphorylation of p27Kip1 on Thr198 promotes p27Kip1 protein stability, resulting in more autophagy and less apoptosis.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277430	Thr222	ITIAFLAtLITQFLV	Homo sapiens	HEK-293 Cell
pmid	sentence
30733434	Here we report that AMPK interacts with and mediates phosphorylation of Insig. Thr222 phosphorylation following AMPK activation is required for protein stabilization of Insig-1, inhibition of cleavage and processing of SREBP-1, and lipogenic gene expression in response to metformin or A769662. AMPKα1 subunit associates with Insig-1 in a dose-dependent manner.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271863	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
SIGNOR-251619	Thr495	TGITRKKtFKEVANA	Homo sapiens
pmid	sentence
24379783	The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273734	Thr507	TKADFDNtVAIHPTS	Homo sapiens	RKO Cell
pmid	sentence
31530934	Mechanistically, AMPKα1 regulate the glutathione reductase (GSR) phosphorylation possibly through residue Thr507 which enhances its activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-172136		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
SIGNOR-252981		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-157947		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-176494		Homo sapiens
pmid	sentence
21892142	Ampk has also been suggested to phosphorylate the glucose-sensitive transcription factor chrebpthe dna binding activity, as assayed in a gel-shift assay of the truncated chrebp, was gradually inactivated with time by treatment with ampk

Identifier	Residue	Organism
SIGNOR-112289		Homo sapiens
pmid	sentence
11724780	Ampk has also been suggested to phosphorylate the glucose-sensitive transcription factor chrebpthe dna binding activity, as assayed in a gel-shift assay of the truncated chrebp, was gradually inactivated with time by treatment with ampk

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-156786		Homo sapiens
pmid	sentence
17609368	Several in vivo studies using aicar to activate ampk chronically determined that mitochondrial enzymes [e.g., cytochrome c, uncoupling protein 3 (ucp-3)] and proteins involved in glucose uptake (glut4)are increased at the transcriptional level in skeletal muscle.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-186061		Homo sapiens	Myoblast
pmid	sentence
19491292	Activation of ampk reduced p21 protein and mrna expression, which was associated with re- duced g1/s cell cycle transition and p21 promoter activity.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle, Myotube

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-184473		Homo sapiens
pmid	sentence
19262508	The acute actions of ampk on lipid oxidation alter the balance between cellular nad+ and nadh, which acts as a messenger to activate sirt1

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle

Identifier	Residue	Organism
SIGNOR-173047		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

Identifier	Residue	Organism
SIGNOR-157941		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:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-176497		Homo sapiens
pmid	sentence
21892142	Ampk was recently found to phosphorylate a conserved serine near the cleavage site within srebp1, suppressing its activation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-173161		Homo sapiens
pmid	sentence
21478464	Tr4 transactivation is inhibited via phosphorylation by metformin-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	Organism	Cell Line
SIGNOR-173689		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-156831		Homo sapiens
pmid	sentence
17609368	Severalin vivostudies using aicar to activate ampk chronically determined that mitochondrial enzymes [e.g., cytochromec, uncoupling protein 3 (ucp-3)] (1518) and proteins involved in glucose uptake (glut4) (1820) are increased at the transcriptional level in skeletal muscle.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle

Identifier	Residue	Organism
SIGNOR-241952		Rattus norvegicus
pmid	sentence
11602624	Using a novel AMPK inhibitor, we find that AMPK activation is required for metformins inhibitory effect on glucose production by hepatocytes. In isolated rat skeletal muscles, metformin stimulates glucose uptake coincident with AMPK activation

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Organism
SIGNOR-156772		Homo sapiens
pmid	sentence
17609368	Severalin vivostudies using aicar to activate ampk chronically determined that mitochondrial enzymes [e.g., cytochromec, uncoupling protein 3 (ucp-3)] (1518) and proteins involved in glucose uptake (glut4) (1820) are increased at the transcriptional level in skeletal muscle.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle

Identifier	Residue	Organism
SIGNOR-200404		Homo sapiens
pmid	sentence
23324179	Amp-activated protein kinase inhibits tgf-__-, angiotensin ii-, aldosterone-, high glucose-, and albumin-induced epithelial-mesenchymal transition.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle

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-120827		Homo sapiens	Macrophage
pmid	sentence
14985344	Ampk by insulin-sensitizing drugs markedly inactivates in- ducible nitric-oxide synthase (inos).

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle

Identifier	Residue	Organism
SIGNOR-176422		Homo sapiens
pmid	sentence
21892142	In 2010, bungard et al., reported that ampk can target transcriptional regulation through phosphorylation of histone h2b on serine3681. Cells expressing a mutant h2b s36a blunted the induction of stress genes upregulated by ampk including p21 and cpt1c.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-130076		Homo sapiens
pmid	sentence
15509864	In muscle, it causes increased dna binding by the transcription factors nrf1 (bergeron et al., 2001) and mef2 (zheng et al., 2001), which may be involved in regulation of mitochondrial genes and glut4, respectively.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-238598		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

Identifier	Residue	Organism	Cell Line
SIGNOR-173038		Homo sapiens	HEK-293 Cell
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:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-256136		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

Identifier	Residue	Organism
SIGNOR-176475		Homo sapiens
pmid	sentence
21892142	Collectively, these findings suggest ampk suppresses glucose production through two transcriptional effects:reduced expression of creb targets via crtc inactivation and reduced expression of foxo target genes via class iia hdac inactivation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-270257		Homo sapiens
pmid	sentence
21892142	Collectively, these findings suggest ampk suppresses glucose production through two transcriptional effects:reduced expression of creb targets via crtc inactivation and reduced expression of foxo target genes via class iia hdac inactivation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-158071		Homo sapiens
pmid	sentence
17909097	We have concluded that metformin inhibits hepatic gluconeogenesis through ampk-dependent regulation of shp

Publications:

1

Organism:

Homo Sapiens

Name	PRKAA1 View Modifications
Full Name	5'-AMP-activated protein kinase catalytic subunit alpha-1
Synonyms	AMPK subunit alpha-1, Acetyl-CoA carboxylase kinase, ACACA kinase, 2.7.11.27, Hydroxymethylglutaryl-CoA reductase kinase, HMGCR kinase, 2.7.11.31, Tau-protein kinase PRKAA1, 2.7.11.26 \| AMPK1
Primary ID	Q13131
Links	- -
Type	protein
Relations	151
Function	Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes

The SIGnaling Network
Open Resource

Summary

Viewer

Search Tools

▶Modifications Tables

Relations