DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structure of mammalian AMPK and its regulation by ADP. Structure of mammalian AMPK and its regulation by ADP. Nature 2011 imex curation Xiao B., Sanders MJ., Underwood E., Heath R., Mayer FV., Carmena D., Jing C., Walker PA., Eccleston JF., Haire LF., Saiu P., Howell SA., Aasland R., Martin SR., Carling D., Gamblin SJ. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Xiao B., Sanders MJ., Underwood E., Heath R., Mayer FV., Carmena D., Jing C., Walker PA., Eccleston JF., Haire LF., Saiu P., Howell SA., Aasland R., Martin SR., Carling D., Gamblin SJ. DIP original experiment: DIP-219113X Nature 2011 IMEx Structure of mammalian AMPK and its regulation by ADP. Structure of mammalian AMPK and its regulation by ADP. Structure of mammalian AMPK and its regulation by ADP. Nature 2011 imex curation Xiao B., Sanders MJ., Underwood E., Heath R., Mayer FV., Carmena D., Jing C., Walker PA., Eccleston JF., Haire LF., Saiu P., Howell SA., Aasland R., Martin SR., Carling D., Gamblin SJ. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Xiao B., Sanders MJ., Underwood E., Heath R., Mayer FV., Carmena D., Jing C., Walker PA., Eccleston JF., Haire LF., Saiu P., Howell SA., Aasland R., Martin SR., Carling D., Gamblin SJ. DIP original experiment: DIP-219112X Nature 2011 IMEx Structure of mammalian AMPK and its regulation by ADP. 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 aakb2_human 5'-AMP-activated protein kinase subunit beta-2 PRKAB2 protein protein human Homo sapiens Human MGNTTSDRVSGERHGAKAARSEGAGGHAPGKEHKIMVGSTDDPSVFSLPDSKLPGDKEFVSWQQDLEDSVKPTQQARPTVIRWSEGGKEVFISGSFNNWSTKIPLIKSHNDFVAILDLPEGEHQYKFFVDGQWVHDPSEPVVTSQLGTINNLIHVKKSDFEVFDALKLDSMESSETSCRDLSSSPPGPYGQEMYAFRSEERFKSPPILPPHLLQVILNKDTNISCDPALLPEPNHVMLNHLYALSIKDSVMVLSATHRYKKKYVTTLLYKPI DIP protein O43741 original sequence version: 121 DIP protein O43741 original sequence version: 98 DIP protein O43741 original sequence version: 112 42B23BD70B92519C 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-prkab2-10 2 5 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 407-559 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 3 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 4 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 187-272 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction prkaa1-prkab2-11 1 5 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 407-559 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 3 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 4 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 187-272 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association