DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural basis for AMPK activation: natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms. Structural basis for AMPK activation: natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms. Structure (London, England : 1993) 2014 imex curation Calabrese MF., Rajamohan F., Harris MS., Caspers NL., Magyar R., Withka JM., Wang H., Borzilleri KA., Sahasrabudhe PV., Hoth LR., Geoghegan KF., Han S., Brown J., Subashi TA., Reyes AR., Frisbie RK., Ward J., Miller RA., Landro JA., Londregan AT., Carpino PA., Cabral S., Smith AC., Conn EL., Cameron KO., Qiu X., Kurumbail RG. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Calabrese MF., Rajamohan F., Harris MS., Caspers NL., Magyar R., Withka JM., Wang H., Borzilleri KA., Sahasrabudhe PV., Hoth LR., Geoghegan KF., Han S., Brown J., Subashi TA., Reyes AR., Frisbie RK., Ward J., Miller RA., Landro JA., Londregan AT., Carpino PA., Cabral S., Smith AC., Conn EL., Cameron KO., Qiu X., Kurumbail RG. DIP original experiment: DIP-261976X Structure (London, England : 1993) 2014 IMEx Structural basis for AMPK activation: natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms. Structural basis for AMPK activation: natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms. Structural basis for AMPK activation: natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms. Structure (London, England : 1993) 2014 imex curation Calabrese MF., Rajamohan F., Harris MS., Caspers NL., Magyar R., Withka JM., Wang H., Borzilleri KA., Sahasrabudhe PV., Hoth LR., Geoghegan KF., Han S., Brown J., Subashi TA., Reyes AR., Frisbie RK., Ward J., Miller RA., Landro JA., Londregan AT., Carpino PA., Cabral S., Smith AC., Conn EL., Cameron KO., Qiu X., Kurumbail RG. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Calabrese MF., Rajamohan F., Harris MS., Caspers NL., Magyar R., Withka JM., Wang H., Borzilleri KA., Sahasrabudhe PV., Hoth LR., Geoghegan KF., Han S., Brown J., Subashi TA., Reyes AR., Frisbie RK., Ward J., Miller RA., Landro JA., Londregan AT., Carpino PA., Cabral S., Smith AC., Conn EL., Cameron KO., Qiu X., Kurumbail RG. DIP original experiment: DIP-261975X Structure (London, England : 1993) 2014 IMEx Structural basis for AMPK activation: natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms. Structural basis for AMPK activation: natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms. Structural basis for AMPK activation: natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms. Structure (London, England : 1993) 2014 imex curation Calabrese MF., Rajamohan F., Harris MS., Caspers NL., Magyar R., Withka JM., Wang H., Borzilleri KA., Sahasrabudhe PV., Hoth LR., Geoghegan KF., Han S., Brown J., Subashi TA., Reyes AR., Frisbie RK., Ward J., Miller RA., Landro JA., Londregan AT., Carpino PA., Cabral S., Smith AC., Conn EL., Cameron KO., Qiu X., Kurumbail RG. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Calabrese MF., Rajamohan F., Harris MS., Caspers NL., Magyar R., Withka JM., Wang H., Borzilleri KA., Sahasrabudhe PV., Hoth LR., Geoghegan KF., Han S., Brown J., Subashi TA., Reyes AR., Frisbie RK., Ward J., Miller RA., Landro JA., Londregan AT., Carpino PA., Cabral S., Smith AC., Conn EL., Cameron KO., Qiu X., Kurumbail RG. DIP original experiment: DIP-261973X Structure (London, England : 1993) 2014 IMEx Structural basis for AMPK activation: natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms. Structural basis for AMPK activation: natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms. Structural basis for AMPK activation: natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms. Structure (London, England : 1993) 2014 imex curation Calabrese MF., Rajamohan F., Harris MS., Caspers NL., Magyar R., Withka JM., Wang H., Borzilleri KA., Sahasrabudhe PV., Hoth LR., Geoghegan KF., Han S., Brown J., Subashi TA., Reyes AR., Frisbie RK., Ward J., Miller RA., Landro JA., Londregan AT., Carpino PA., Cabral S., Smith AC., Conn EL., Cameron KO., Qiu X., Kurumbail RG. Only protein-protein interactions ecolx Escherichia coli ion exchange chrom ion exchange chromatography IEC IEC ion exchange chrom predetermined predetermined participant predetermined Calabrese MF., Rajamohan F., Harris MS., Caspers NL., Magyar R., Withka JM., Wang H., Borzilleri KA., Sahasrabudhe PV., Hoth LR., Geoghegan KF., Han S., Brown J., Subashi TA., Reyes AR., Frisbie RK., Ward J., Miller RA., Landro JA., Londregan AT., Carpino PA., Cabral S., Smith AC., Conn EL., Cameron KO., Qiu X., Kurumbail RG. DIP original experiment: DIP-261974X Structure (London, England : 1993) 2014 IMEx Structural basis for AMPK activation: natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms. aakg1_rat 5'-AMP-activated protein kinase subunit gamma-1 Prkag1 protein protein rat Rattus norvegicus (Rat) Rat MESVAAESAPAPENEHSQETPESNSSVYTTFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLEAIINRLVEAEVHRLVVVDEHDVVKGIVSLSDILQALVLTGGEKKP DIP protein P80385 original sequence version: 97 DIP protein P80385 original sequence version: 79 DIP protein P80385 original sequence version: 108 DIP protein P80385 original sequence version: 89 36031E526C1F1E97 aakb1_rat 5'-AMP-activated protein kinase subunit beta-1 Prkab1 5'-AMP-activated protein kinase 40 kDa subunit protein protein rat Rattus norvegicus (Rat) Rat MGNTSSERAALERQAGHKTPRRDSSGGTKDGDRPKILMDSPEDADIFHTEEMKAPEKEEFLAWQHDLEVNEKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSQNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYISKPEERFKAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI DIP protein P80386 original sequence version: 108 DIP protein P80386 original sequence version: 137 DIP protein P80386 original sequence version: 118 aapk1_rat 5'-AMP-activated protein kinase catalytic subunit alpha-1 Prkaa1 Ampk1 Hydroxymethylglutaryl-CoA reductase kinase Tau-protein kinase PRKAA1 Acetyl-CoA carboxylase kinase protein protein rat Rattus norvegicus (Rat) Rat MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFECSEEEVLSCLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVAETPRARHTLDELNPQKSKHQGVRKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTFSKMSLQLYQVDSRTYLLDFRSIDDEITEAKSGTATPQRSGSISNYRSCQRSDSDAEAQGKPSEVSLTSSVTSLDSSPVDVAPRPGSHTIEFFEMCANLIKILAQ DIP protein P54645 original sequence version: 125 DIP protein P54645 original sequence version: 104 DIP protein P54645 original sequence version: 138 DIP protein P54645 original sequence version: 118 Responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. It also regulates cholesterol synthesis via phosphorylation and inactivation of hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase. Appears to act as a metabolic stress-sensing protein kinase switching off biosynthetic pathways when cellular ATP levels are depleted and when 5'-AMP rises in response to fuel limitation and/or hypoxia. This is a catalytic subunit mint A869C340A85785ED prkaa1-prkab1-5 3 7 unspecified role unspecified role bait bait His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Region 2-469/525-559 Region 2-469/525-559 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 5 unspecified role unspecified role prey prey ecolx Escherichia coli 6 unspecified role unspecified role prey prey Region 68-270 Region 68-270 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli association association prkaa1-prkab1-6 1 7 unspecified role unspecified role unspecified role unspecified role Region 2-469/525-559 Region 2-469/525-559 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role Region 68-270 Region 68-270 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction prkaa1-prkab1-7 2 7 unspecified role unspecified role unspecified role unspecified role Region 2-469/525-559 Region 2-469/525-559 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role Region 68-270 Region 68-270 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association prkaa1-prkab1-8 4 7 unspecified role unspecified role unspecified role unspecified role Region 2-469/525-559 Region 2-469/525-559 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role Region 68-270 Region 68-270 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association