MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it General interaction mode of CIDE:CIDE complex revealed by a mutation study of the Drep2 CIDE domain. General interaction mode of CIDE:CIDE complex revealed by a mutation study of the Drep2 CIDE domain. FEBS Lett. (0014-5793) 2013 Lee SM., Park HH. in vitro In vitro bn-page blue native page bn-page weight by staining molecular weight estimation by staining weight by staining Lee SM., Park HH. FEBS Lett. (0014-5793) 2013 General interaction mode of CIDE:CIDE complex revealed by a mutation study of the Drep2 CIDE domain. General interaction mode of CIDE:CIDE complex revealed by a mutation study of the Drep2 CIDE domain. FEBS Lett. (0014-5793) 2013 Lee SM., Park HH. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by staining molecular weight estimation by staining weight by staining Lee SM., Park HH. FEBS Lett. (0014-5793) 2013 q0e9b7_drome Drep3 Drep-3 Rep3 BcDNA:AT08574 CG13187 DREP-3 Dmel\CG8364 drep-3 drep3 CG8364 Dmel_CG8364 DREP3 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MTAMNADETKLAGMPQGAEEEQEPEREQKKESDGAAAAAGVQCDPDSRIVAPPPRQRTLTRTAELDADCEDIELDADDGLDDAADSITLELALSPHSSATPTPSPTTADEDFAQLDNSKPFKIKDITRNIRKAVVATTLSELRTKVSLKFERAQPAIHLDCDGTEVDDEEYFSTLEPNAELIAVFPGEQWRDPSDYNANLRRTSLDAQRLRSLVSKLQPNYMNDDDLDKLSNMDPNSLVDITGREPKDNEYSARSDAARLSTELSC 7CA5185EB8ABB04B q9u787_drome Drep2 Drep-2 Rep2 drep2 CG1975 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MAREESRGKRPLKIWDSWRNVRKGVVVGTFEELLVRGKDKLGVPASEPVRVVLECDGTQIEDGEYFRTLANNTVLLLLRQGERWYPTGVDVIKAAISAIPKIVCETIHALELHDETPSWKIMDNKGRVTVVLHWDQRQGGGSGGGESGGAGGGVGSMCSRLGSSNGLLSSDKYSPSKKGLSAQSSLDNKSVSSQSSQPRYASPQITVISDDGPASIYHPGGVVLPPGVVIPGGSRRLSKQGSSFDSTVGVGVGAVHVHTPECAHHAHTPSRAGSPSTTECDFHCCALHEEGRKIAVHKSVATSPIQDGSSSPQPQSAPSVMDPMLGGSGGGGSGSMQRRSSGAKGHVRFLDIAPERDSSESETENTVMEDDKTTTEKFLLLIDQLSVDQKRHLSIKDIGIILERLNSKILDVERLDRESESDDCYNWTIKATIRGDALRELGVIYNANYYAISEHPGYKEELEENGEEVEEEEEEDEEDRI mint 2B5D8B774715898C o61464_drome Drep1 Drep-1 Rep1 drep1 CG8357 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly METAANSGDSKKPFKVKDVTRNIKKAVCASSLEEIRSKVAEKFEKCDHLPTIHLDSDGTEIDDEEYFRTLDENTELVAVFPGEHWIDPTHYVTITTPHGNEAGTGNGELNGGGEGDTTDANNSESARIRQLVGQLQNNLCNVSVMNDADLDSLSNMDPNSLVDITGKEFMEQLKDAGRPLCAKRNAEDRLNLLKLKLLKAGAIFCSERYPEDAEAIDREIGRQLNEAESGQMSTTTTSNTRTIEVVQCDNQNTTITITVGEATTTCATASGAMGSSAAEAAANEANANPNRNPNANGDI 5A20E0E377C53138 drep_1-drep_2 2 Drep2 4 weight by staining molecular weight estimation by staining weight by staining experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Q9U787:p.Lys40Glu mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain K E Tue Jul 12 10:14:41 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 19:32:44 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys40glu' Tue Jun 30 17:38:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys40Glu' binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Drep1 5 weight by staining molecular weight estimation by staining weight by staining experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f2 mint To analyze the interaction between Drep1 and Drep2K40E, and Drep1 and Drep2R36E, we mixed the two proteins and incubated them at room temperature for one hour, after which they were loaded onto the gel-filtration column. The profiles showed that Drep2K40E was not able to form a complex with Drep1 CIDE, as indicated by a Drep2 self160 complex peak at around 12 ml (Figure 2B). SDS-PAGE showing two proteins that migrated separately supports the data obtained from gel-filtration chromatography (Figure 2B). However, Drep2R36E still interacts with Drep1 CIDE. drep-2 2 Drep2 4 weight by staining molecular weight estimation by staining weight by staining experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 8.0 direct interaction direct interaction f2 mint Drep2 CIDE forms a highly oligomeric self complex in solution 147 that elutes from the 148 gel-filtration column at around 12 ml (Figure 2A) unlike Drep1CIDE and Drep3 CIDE. Drep2 CIDE forms an octamer or decamer as the calculated 150 molecular weight of monomeric Drep2 CIDE is 11,324 drep-2 2 Drep2 4 weight by staining molecular weight estimation by staining weight by staining experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 10.0 direct interaction direct interaction f2 mint Drep2 CIDE forms a highly oligomeric self complex in solution 147 that elutes from the 148 gel-filtration column at around 12 ml (Figure 2A) unlike Drep1CIDE and Drep3 CIDE. Drep2 CIDE forms an octamer or decamer as the calculated 150 molecular weight of monomeric Drep2 CIDE is 11,324 drep_2-drep_3-2 2 Drep2 4 weight by staining molecular weight estimation by staining weight by staining experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Q9U787:p.Lys40Glu mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain K E Tue Jul 12 10:15:02 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 15:51:56 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys40glu' Tue Jun 30 19:59:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys40Glu' binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Drep3 3 weight by staining molecular weight estimation by staining weight by staining experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f3 mint drep_1-drep_2-1 1 Drep2 4 weight by staining molecular weight estimation by staining weight by staining experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Q9U787:p.Lys40Glu mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain K E Tue Jul 12 10:15:10 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 17:17:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys40glu' Tue Jun 30 15:59:40 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys40Glu' binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Drep1 5 weight by staining molecular weight estimation by staining weight by staining experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f4 mint The interactions were also confirmed using native PAGE (Figure 4). Although the mixtures of Drep1 CIDE:Drep2R36E, Drep3 CIDE:Drep2R36E, and Drep3:Drep2K40E produced complex bands, the mixture of Drep1:Drep2K40E did not (Figure 4). This result supports the fact that K40E on the basic surface side of Drep2 is crucial to the interaction with Drep1. Although the mixture of Drep3:Drep2K40E still produced complex bands, the amount of complex band was relatively small compared to the band generated by the mixture of Drep3:Drep2R36E, indicating that K40E is also important to binding with Drep3 CIDE. Previous gel191 filtration and SDS-PAGE clearly showed that Drep2K40E was not able to form a complex with Drep3 drep_2-drep_3-3 1 Drep2 4 weight by staining molecular weight estimation by staining weight by staining experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q9U787:p.Lys40Glu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain K E Tue Jul 12 10:52:35 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 20:06:46 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys40glu' Tue Jun 30 19:09:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys40Glu' Drep3 3 weight by staining molecular weight estimation by staining weight by staining experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f4 mint The interactions were also confirmed using native PAGE (Figure 4). Although the mixtures of Drep1 CIDE:Drep2R36E, Drep3 CIDE:Drep2R36E, and Drep3:Drep2K40E produced complex bands, the mixture of Drep1:Drep2K40E did not (Figure 4). This result supports the fact that K40E on the basic surface side of Drep2 is crucial to the interaction with Drep1. Although the mixture of Drep3:Drep2K40E still produced complex bands, the amount of complex band was relatively small compared to the band generated by the mixture of Drep3:Drep2R36E, indicating that K40E is also important to binding with Drep3 CIDE. Previous gel191 filtration and SDS-PAGE clearly showed that Drep2K40E was not able to form a complex with Drep3