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 the bifunctional isocitrate dehydrogenase kinase/phosphatase. Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase. Nature 2010 imex curation Zheng J., Jia Z. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Zheng J., Jia Z. DIP original experiment: DIP-219483X Nature 2010 IMEx Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase. Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase. Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase. Nature 2010 imex curation Zheng J., Jia Z. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Zheng J., Jia Z. DIP original experiment: DIP-219482X Nature 2010 IMEx Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase. Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase. Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase. Nature 2010 imex curation Zheng J., Jia Z. Only protein-protein interactions in vitro In vitro phosphatase assay phosphatase assay predetermined predetermined participant predetermined Zheng J., Jia Z. DIP original experiment: DIP-219485X Nature 2010 IMEx Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase. Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase. Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase. Nature 2010 imex curation Zheng J., Jia Z. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Zheng J., Jia Z. DIP original experiment: DIP-219484X Nature 2010 IMEx Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase. idh_ecoli Isocitrate dehydrogenase [NADP] icd icdA icdE b1136 JW1122 Oxalosuccinate decarboxylase NADP(+)-specific ICDH IDP protein protein ecoli Escherichia coli (strain K12) MESKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVTPAMLKVVDAAVEKAYKGERKISWMEIYTGEKSTQVYGQDVWLPAETLDLIREYRVAIKGPLTTPVGGGIRSLNVALRQELDLYICLRPVRYYQGTPSPVKHPELTDMVIFRENSEDIYAGIEWKADSADAEKVIKFLREEMGVKKIRFPEHCGIGIKPCSEEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGAFKDWGYQLAREEFGGELIDGGPWLKVKNPNTGKEIVIKDVIADAFLQQILLRPAEYDVIACMNLNGDYISDALAAQVGGIGIAPGANIGDECALFEATHGTAPKYAGQDKVNPGSIILSAEMMLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGAKLLKCSEFGDAIIENM DIP protein P08200 original sequence version: 108 9A02E707C3B4FDD9 acek_ecoli Isocitrate dehydrogenase kinase/phosphatase aceK b4016 JW3976 protein protein ecoli Escherichia coli (strain K12) MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIIRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDRFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYGEMLF DIP protein P11071 original sequence version: 96 5ABD5FB5FA1D9B29 acek-icd-1 2 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction acek-icd-2 3 5 enzyme target enzyme target substrate substrate unspecified role unspecified role ecolx Escherichia coli 6 enzyme enzyme unspecified role unspecified role P11071:p.Asp477Ala D477A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain D A This feature has been corrected as a result of our quality control procedures. The original label was 'D477A'. Wed May 02 18:21:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp477ala' Tue Jun 30 20:05:31 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp477Ala' P11071:p.Lys346Glu K346E mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K346E'. Wed May 02 15:23:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys346glu' Tue Jun 30 17:04:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys346Glu' ecolx Escherichia coli dephosphorylation dephosphorylation reaction dephosphorylation acek-icd-3 1 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction acek-icd-4 4 5 enzyme target enzyme target substrate substrate unspecified role unspecified role ecolx Escherichia coli 6 enzyme enzyme unspecified role unspecified role P11071:p.Lys336Ala K336A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K A This feature has been corrected as a result of our quality control procedures. The original label was 'K336A'. Wed May 02 19:38:55 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys336ala' Tue Jun 30 15:47:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys336Ala' P11071:p.Asp475Ala D475A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain D A This feature has been corrected as a result of our quality control procedures. The original label was 'D475A'. Wed May 02 15:19:06 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp475ala' Tue Jun 30 20:23:16 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp475Ala' P11071:p.Asn462Ala N462A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain N A This feature has been corrected as a result of our quality control procedures. The original label was 'N462A'. Wed May 02 17:41:53 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn462ala' Tue Jun 30 18:17:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asn462Ala' P11071:p.[Glu497Lys;Glu499Lys] E497K/E499K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain E K certain certain sequence position certain certain certain sequence position certain E K This feature has been corrected as a result of our quality control procedures. The original label was 'E497K/E499K'. Wed May 02 17:04:01 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu497lys,glu499lys' Tue Jun 30 18:23:30 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Glu497Lys;Glu499Lys]' ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation