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 http://mint.bio.uniroma2.it/mint ren-2015-2 in vitro In vitro bn-page blue native page bn-page weight by staining molecular weight estimation by staining weight by staining Ren S., Sugimoto Y., Kobayashi T., Masuda S. shmasuda@bio.titech.ac.jp FEBS letters 2015 Only protein-protein interactions imex curation imex curation ren-2015-1 in vitro In vitro crosslink cross-linking study crosslink ms participant Identification by mass spectrometry ms participant Ren S., Sugimoto Y., Kobayashi T., Masuda S. shmasuda@bio.titech.ac.jp FEBS letters 2015 Only protein-protein interactions imex curation imex curation p74295_syny3 slr1694 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MSLYRLIYSSQGIPNLQPQDLKDILESSQRNNPANGITGLLCYSKPAFLQVLEGECEQVNETYHRIVQDERHHSPQIIECMPIRRRNFEVWSMQAITVNDLSTEQVKTLVLKYSGFTTLRPSAMDPEQCLNFLLDIAKIYELSDNFFLDL 54897F456CA0D571 1-62 1871042 n/a 1871044 unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 3.0 direct interaction direct interaction false false false f1b The oligomerization states of the proteins were studied by blue-native PAGE. In the absence of PixE, wild-type PixD was in equilibrium between the dimer and decamer (Fig. 1B, lane 1) as reported [6,8,10]. On the other hand, the C-terminal-truncated PixD mutant did not form a dimer, although smeared bands indicated formation of a trimer and/or tetramer (Fig. 1B, lane 2). Mixing PixE with the truncated mutant of PixD yielded no PixD–PixE complex, although wild-type PixD clearly could form the complex with PixE (Fig. 1B, lane 3, 4). The mutant PixD still could form the decamer (Fig. 1B, lane 2), however, and thus these results indicated that the C-terminus of PixD is necessary for stable dimer formation as well as complex formation with PixE but is not necessary for decamer formation. p74295_syny3-1 1871042 n/a 1871044 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false f1b The oligomerization states of the proteins were studied by blue-native PAGE. In the absence of PixE, wild-type PixD was in equilibrium between the dimer and decamer (Fig. 1B, lane 1) as reported [6,8,10]. On the other hand, the C-terminal-truncated PixD mutant did not form a dimer, although smeared bands indicated formation of a trimer and/or tetramer (Fig. 1B, lane 2). Mixing PixE with the truncated mutant of PixD yielded no PixD–PixE complex, although wild-type PixD clearly could form the complex with PixE (Fig. 1B, lane 3, 4). The mutant PixD still could form the decamer (Fig. 1B, lane 2), however, and thus these results indicated that the C-terminus of PixD is necessary for stable dimer formation as well as complex formation with PixE but is not necessary for decamer formation. 1-61 1871043 N/A 1871044 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false f1a sf2 This analysis revealed that peptide 2842 contained an intermolecular cross-link between Lys22 and Glu26.