IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Tetramerization of the AKT1 plant potassium channel involves its C-terminal cytoplasmic domain. Tetramerization of the AKT1 plant potassium channel involves its C-terminal cytoplasmic domain. EMBO J. (0261-4189) 1997 imex curation Daram P., Urbach S., Gaymard F., Sentenac H., Cherel I. The chromatography was carried out under non-denaturing conditions in the presence of lysophosphatidylcholine. orchard Only protein-protein interactions spofr-sf_9 Spodoptera frugiperda insect cells Fall armyworm sf_9 insect cells Derived from pupal ovarian tissue of the fall armyworm Cloned from the parent cell line, IPLB-SF-21-AE (SF-21) derived from immature ovaries of fall armyworm Spodoptera frugiperda pupae cells are susceptible to Baculovirus infection molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column western blot western blot Immuno blot Immuno blot Daram P., Urbach S., Gaymard F., Sentenac H., Cherel I. The chromatography was carried out under non-denaturing conditions in the presence of lysophosphatidylcholine. Accepted 2009-NOV-30 by ORCHARD. EMBO J. (0261-4189) 1997 orchard Only protein-protein interactions imex curation Tetramerization of the AKT1 plant potassium channel involves its C-terminal cytoplasmic domain. Tetramerization of the AKT1 plant potassium channel involves its C-terminal cytoplasmic domain. EMBO J. (0261-4189) 1997 imex curation Daram P., Urbach S., Gaymard F., Sentenac H., Cherel I. The chromatography was carried out under non-denaturing conditions in the presence of lysophosphatidylcholine. orchard Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Daram P., Urbach S., Gaymard F., Sentenac H., Cherel I. The chromatography was carried out under non-denaturing conditions in the presence of lysophosphatidylcholine. Accepted 2009-NOV-30 by ORCHARD. EMBO J. (0261-4189) 1997 orchard Only protein-protein interactions imex curation akt1_arath Potassium channel AKT1 AKT1 At2g26650 F18A8.2 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MRGGALLCGQVQDEIEQLSRESSHFSLSTGILPSLGARSNRRVKLRRFVVSPYDHKYRIWEAFLVVLVVYTAWVSPFEFGFLRKPRPPLSITDNIVNAFFAIDIIMTFFVGYLDKSTYLIVDDRKQIAFKYLRSWFLLDLVSTIPSEAAMRISSQSYGLFNMLRLWRLRRVGALFARLEKDRNFNYFWVRCAKLVCVTLFAVHCAACFYYLIAARNSNPAKTWIGANVANFLEESLWMRYVTSMYWSITTLTTVGYGDLHPVNTKEMIFDIFYMLFNLGLTAYLIGNMTNLVVHGTSRTRNFRDTIQAASNFAHRNHLPPRLQDQMLAHLCLKYRTDSEGLQQQETLDALPKAIRSSISHFLFYSLMDKVYLFRGVSNDLLFQLVSEMKAEYFPPKEDVILQNEAPTDFYILVNGTADLVDVDTGTESIVREVKAGDIIGEIGVLCYRPQLFTVRTKRLCQLLRMNRTTFLNIIQANVGDGTIIMNNLLQHLKEMNDPVMTNVLLEIENMLARGKMDLPLNLCFAAIREDDLLLHQLLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLLEHGSTIDAGDVGHFACTAAEQGNLKLLKEIVLHGGDVTRPRATGTSALHTAVCEENIEMVKYLLEQGADVNKQDMHGWTPRDLAEQQGHEDIKALFREKLHERRVHIETSSSVPILKTGIRFLGRFTSEPNIRPASREVSFRIRETRARRKTNNFDNSLFGILANQSVPKNGLATVDEGRTGNPVRVTISCAEKDDIAGKLVLLPGSFKELLELGSNKFGIVATKVMNKDNNAEIDDVDVIRDGDHLIFATDS DIP protein Q38998 original sequence version: 122 DIP protein Q38998 original sequence version: 69 28E1622BA3505F4C akt1 1 3 unspecified role unspecified role neutral component neutral component c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain physical association physical association Figure 1 Figure 2B The highest one corresponded to a complex whose molecular weight was estimated to range between 385 and 425 kDa, consistentwith that expected for a tetramer of identical 95 kDa subunits. akt1-2 1 3 unspecified role unspecified role neutral component neutral component physical association physical association Figure 1 The other two peaks could be ascribed to the presence of a dimer (mol. wt 173�213 kDa) and a monomer (81�121 kDa). akt1-4 2 3 unspecified role unspecified role prey prey region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain 3 unspecified role unspecified role bait bait region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain 11 13 physical association physical association Figure 4 Figure 5 Using the two-hybrid system, we have defined two kinds of interactions: one between identical regions 2 (amino acids 294-516), and another one between region 2 and region D4 (amino acids L777 to the last one, S857). akt1-5 2 3 unspecified role unspecified role bait bait region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain 3 unspecified role unspecified role prey prey c-terminal required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain 18 16 physical association physical association Figure 4 Figure 5 akt1-3 2 3 unspecified role unspecified role bait bait c-terminal required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain 3 unspecified role unspecified role prey prey region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain 21 23 physical association physical association Figure 4 Figure 5