| + |
PRKAA2 | down-regulates activity 
phosphorylation
|
HIPK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275486 |
Ser121 |
LMRRSTVsLLDTYQK |
|
|
| pmid |
sentence |
| 23871434 |
AMPKalpha2-mediated inhibition of WIP1 phosphorylation by HIPK2|Site-directed mutagenesis of Thr112 and Ser114 in the N terminus, and Thr1107 in the C terminus markedly reduced HIPK2 phosphorylation by AMPKalpha2 in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275487 |
Thr1116 |
AALGSTGtVAHLVAS |
|
|
| pmid |
sentence |
| 23871434 |
AMPKalpha2-mediated inhibition of WIP1 phosphorylation by HIPK2|Site-directed mutagenesis of Thr112 and Ser114 in the N terminus, and Thr1107 in the C terminus markedly reduced HIPK2 phosphorylation by AMPKalpha2 in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275485 |
Thr119 |
HNLMRRStVSLLDTY |
|
|
| pmid |
sentence |
| 23871434 |
AMPKalpha2-mediated inhibition of WIP1 phosphorylation by HIPK2|Site-directed mutagenesis of Thr112 and Ser114 in the N terminus, and Thr1107 in the C terminus markedly reduced HIPK2 phosphorylation by AMPKalpha2 in vitro |
|
| Publications: |
3 |
| + |
PRKAA2 | up-regulates 
phosphorylation
|
TSC2 |
0.56 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149388 |
Ser1387 |
QPLSKSSsSPELQTL |
Homo sapiens |
|
| pmid |
sentence |
| 16959574 |
We have observed that ampk directly phosphorylates tsc2, and the ampk-dependent phosphorylation of tsc2 is critical for the coordination between cell growth and cellular energy levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 | down-regulates
phosphorylation
|
CRTC2 |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140238 |
Ser171 |
SALNRTSsDSALHTS |
Homo sapiens |
|
| pmid |
sentence |
| 16148943 |
Phosphorylation on the ser171 residue of crtc2 by ampk and ampk-related kinases, including the salt-inducible kinases (siks), is critical for determining the activity, cellular localization, and degradation of crtc2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142211 |
Ser171 |
SALNRTSsDSALHTS |
Homo sapiens |
|
| pmid |
sentence |
| 16308421 |
Phosphorylation on the ser171 residue of crtc2 by ampk and ampk-related kinases, including the salt-inducible kinases (siks), is critical for determining the activity, cellular localization, and degradation of crtc2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166365 |
Ser171 |
SALNRTSsDSALHTS |
Homo sapiens |
|
| pmid |
sentence |
| 20577053 |
Phosphorylation on the ser171 residue of crtc2 by ampk and ampk-related kinases, including the salt-inducible kinases (siks), is critical for determining the activity, cellular localization, and degradation of crtc2 |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKACA | down-regulates
phosphorylation
|
PRKAA2 |
0.398 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161860 |
Ser173 |
DGEFLRTsCGSPNYA |
Homo sapiens |
|
| pmid |
sentence |
| 19942859 |
Pka associates with and phosphorylates ampk?1 At ser-173 to impede threonine thr-172 phosphorylation and thus activation of ampk1 by lkb1 in response to lipolytic signals |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 | up-regulates
phosphorylation
|
IKBKB |
0.259 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174401 |
Ser177 |
AKELDQGsLCTSFVG |
Homo sapiens |
|
| pmid |
sentence |
| 21673972 |
These results demonstrate that the ikk is a direct substrate of ampk_2 and that its phosphorylation on ser177 and ser181no initiates the activation of the ampk_2 in endothelial cells which in turn phosphorylates and activates the _-subunit of the ikk. The latter also induces a higher rate of ikk auto-inactivation and thus attenuates the activation of nf_b and the expression of inflammatory genes |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174405 |
Ser181 |
DQGSLCTsFVGTLQY |
Homo sapiens |
|
| pmid |
sentence |
| 21673972 |
These results demonstrate that the ikk is a direct substrate of ampk_2 and that its phosphorylation on ser177 and ser181no initiates the activation of the ampk_2 in endothelial cells which in turn phosphorylates and activates the _-subunit of the ikk. The latter also induces a higher rate of ikk auto-inactivation and thus attenuates the activation of nf_b and the expression of inflammatory genes |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 |
phosphorylation
|
PAK2 |
0.244 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195110 |
Ser20 |
APPVRMSsTIFSTGG |
Homo sapiens |
|
| pmid |
sentence |
| 22137581 |
Together, these results indicate that ampk phosphorylates endogenous ppp1r12c at s452 and pak2 at s20 in human cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 | down-regulates activity
phosphorylation
|
ACACB |
0.638 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250318 |
Ser222 |
PTMRPSMsGLHLVKR |
Homo sapiens |
|
| pmid |
sentence |
| 9148944 |
The results suggest that the decrease in ACC activity during muscle contraction is caused by an increase in its phosphorylation, most probably due, at least in part, to activation of the alpha2 isoform of AMPK. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250316 |
Ser222 |
PTMRPSMsGLHLVKR |
Homo sapiens |
|
| pmid |
sentence |
| 14613924 |
ACCβ(Ser221) is a known target for AMPK in human skeletal muscle |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 | up-regulates activity
phosphorylation
|
PDHA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276840 |
Ser295 |
RYHGHSMsDPGVSYR |
in vitro |
|
| pmid |
sentence |
| 33022274 |
AMPKα phosphorylates PDHA subunit on Ser295 and Ser314 to activate PDH complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276838 |
Ser314 |
IQEVRSKsDPIMLLK |
in vitro |
|
| pmid |
sentence |
| 33022274 |
AMPKα phosphorylates PDHA subunit on Ser295 and Ser314 to activate PDH complex |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKAA2 | down-regulates quantity by destabilization
phosphorylation
|
HNF4A |
0.375 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250322 |
Ser313 |
GKIKRLRsQVQVSLE |
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 12740371 |
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. Phosphorylation of HNF4α on Ser-304 reduces protein stability. |
|
| Publications: |
1 |
Organism: |
Cricetulus Griseus |
| + |
PRKAA2 | up-regulates
phosphorylation
|
ULK1 |
0.483 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186633 |
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 |
Cell Line |
| SIGNOR-170859 |
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 |
Cell Line |
| SIGNOR-186637 |
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 |
Cell Line |
| SIGNOR-170863 |
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 |
Cell Line |
| SIGNOR-186641 |
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 |
Sequence |
Organism |
Cell Line |
| SIGNOR-170867 |
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. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 | down-regulates
phosphorylation
|
VASP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176642 |
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 |
Cell Line |
| SIGNOR-150462 |
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 |
| + |
PRKAA2 | down-regulates quantity by destabilization
phosphorylation
|
DUSP1 |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276890 |
Ser334 |
AVLDRGTsTTTVFNF |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25799226 |
Taken together, these results imply that nicotine acts via AMPKα2 to phosphorylate MKP1 at Ser334, instigating MKP1 ubiquitination and proteasome-mediated degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 | down-regulates
phosphorylation
|
BAIAP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161810 |
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195102 |
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 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 | down-regulates activity
phosphorylation
|
EEF2K |
0.48 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250319 |
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 |
Cell Line |
| SIGNOR-250321 |
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 |
| + |
PRKAA2 |
phosphorylation
|
CDC27 |
0.265 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195106 |
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 |
| + |
PRKAA2 | down-regulates
phosphorylation
|
SREBF1 |
0.335 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173031 |
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 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 | up-regulates activity
phosphorylation
|
EEF2K |
0.48 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250158 |
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 |
| + |
PRKAA2 | down-regulates
phosphorylation
|
PPP1R12C |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195148 |
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 |
| + |
PRKAA2 | up-regulates activity
phosphorylation
|
PFKFB2 |
0.429 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250323 |
Ser466 |
PVRMRRNsFTPLSSS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11069105 |
AMPK phosphorylates and activates heart PFK-2 in vitro and in intact cells. activation of PFK-2 was due to the phosphorylation of Ser466 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 | up-regulates
phosphorylation
|
PLD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164293 |
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 |
| + |
PRKAA2 | down-regulates
phosphorylation
|
RPTOR |
0.681 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263045 |
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 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKAA2 | down-regulates quantity by destabilization
phosphorylation
|
PROX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277608 |
Ser79 |
KLLKRANsYEDAMMP |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 36433955 |
Furthermore, the Ser79 phosphorylation of PROX1 by AMPK enhances the recruitment of CUL4-DDB1 ubiquitin ligase to promote PROX1 degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 | down-regulates activity
phosphorylation
|
RPTOR |
0.681 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163463 |
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: |
1 |
Organism: |
Mus Musculus |
| + |
PRKAA2 | down-regulates
phosphorylation
|
ACACA |
0.685 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87583 |
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 |
| + |
PRKAA2 | down-regulates activity
phosphorylation
|
HAS2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276299 |
Thr110 |
LQSVKRLtYPGIKVV |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 21228273 |
We found that AMPK phosphorylated Thr-110 of human HAS2, which inhibits its enzymatic activity. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
STK11 | up-regulates
phosphorylation
|
PRKAA2 |
0.61 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119179 |
Thr172 |
SDGEFLRtSCGSPNY |
Homo sapiens |
|
| 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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122725 |
Thr172 |
SDGEFLRtSCGSPNY |
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 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CAMKK2 | up-regulates
phosphorylation
|
PRKAA2 |
0.606 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161929 |
Thr172 |
SDGEFLRtSCGSPNY |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19958286 |
These data indicate that the camkks function in intact cells as ampkks, predicting wider roles for these kinases in regulating ampk activity in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138364 |
Thr172 |
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: |
2 |
Organism: |
Homo Sapiens |
| + |
ATM | up-regulates activity
phosphorylation
|
PRKAA2 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275488 |
Thr172 |
SDGEFLRtSCGSPNY |
|
|
| pmid |
sentence |
| 23871434 |
ATM phosphorylates AMPKalpha2 to induce inhibitory phosphorylation of HIPK2| |
|
| Publications: |
1 |
| + |
SRC | down-regulates activity
phosphorylation
|
PRKAA2 |
0.26 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277573 |
Tyr179 |
TSCGSPNyAAPEVIS |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34673141 |
We show here that Src signaling leads to direct phosphorylation of the AMPK-α subunit on a novel site, tyrosine 179, resulting in suppression of AMPK-T172 phosphorylation and autophagy upon integrin-mediated cell adhesion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FYN | down-regulates activity
phosphorylation
|
PRKAA2 |
0.26 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277279 |
Tyr436 |
EWKVVNAyHLRVRRK |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 27626315 |
Here we identified that Fyn phosphorylates the α subunit of AMPK on Y436 and inhibits AMPK enzymatic activity without altering the assembly state of the AMPK heterotrimeric complex. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKAA2 | form complex 
binding
|
AMPK |
0.823 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| 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 |
| + |
AICA-Ribotide | up-regulates
chemical activation
|
PRKAA2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186055 |
|
|
Homo sapiens |
Myoblast |
| pmid |
sentence |
| 19491292 |
Aicar-induced ampk phosphorylation inhibits cell cycle transition, reducing differentiation of myoblasts into myotubes, through pgc-1alpha-foxo3a-p21. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle, Myotube |
| + |
metformin | up-regulates 
|
PRKAA2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-111034 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11602624 |
Here we report that metformin activates ampk in hepatocytes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ULK2 | down-regulates
phosphorylation
|
PRKAA2 |
0.309 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173089 |
|
|
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 |
| + |
ULK1 | down-regulates
phosphorylation
|
PRKAA2 |
0.483 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173050 |
|
|
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 |
| + |
PRKAA2 | up-regulates
phosphorylation
|
Gbeta |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166905 |
|
|
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 |
| + |
PRKAA2 | up-regulates
phosphorylation
|
TSC1 |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119541 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14651849 |
Under energy starvation conditions, the amp-activated protein kinase (ampk) phosphorylates tsc2 and enhances its activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Serum | down-regulates 
|
PRKAA2 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186644 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19584320 |
Ampk is activated under conditions of low energy charge and typically inhibits anabolic reactions and promotes catabolism |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAG1 | up-regulates
binding
|
PRKAA2 |
0.893 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139173 |
|
|
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 |
| + |
PRKAA2 | up-regulates
phosphorylation
|
IKK-complex |
0.258 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217457 |
|
|
Homo sapiens |
Monocyte |
| pmid |
sentence |
| 21673972 |
These results demonstrate that the ikk is a direct substrate of ampk_2 and that its phosphorylation on ser177 and ser181no initiates the activation of the ampk_2 in endothelial cells which in turn phosphorylates and activates the _-subunit of the ikk. The latter also induces a higher rate of ikk auto-inactivation and thus attenuates the activation of nf_b and the expression of inflammatory genes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 | up-regulates
phosphorylation
|
INSR |
0.379 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195324 |
|
|
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 |
3.0
PRKAA2
- 
- 