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 Biochemical properties of the human guanylate binding protein 5 and a tumor-specific truncated splice variant. Biochemical properties of the human guanylate binding protein 5 and a tumor-specific truncated splice variant. FEBS J. (1742-464X) 2010 imex curation Wehner M., Herrmann C. 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 Wehner M., Herrmann C. FEBS J. (1742-464X) 2010 Only protein-protein interactions imex curation gbp5_human Guanylate-binding protein 5 Guanine nucleotide-binding protein 5 GTP-binding protein 5 GBP-TA antigen GBP5 UNQ2427/PRO4987 protein protein human Homo sapiens Human MALEIHMSDPMCLIENFNEQLKVNQEALEILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKNKGFSVASTVQSHTKGIWIWCVPHPNWPNHTLVLLDTEGLGDVEKADNKNDIQIFALALLLSSTFVYNTVNKIDQGAIDLLHNVTELTDLLKARNSPDLDRVEDPADSASFFPDLVWTLRDFCLGLEIDGQLVTPDEYLENSLRPKQGSDQRVQNFNLPRLCIQKFFPKKKCFIFDLPAHQKKLAQLETLPDDELEPEFVQQVTEFCSYIFSHSMTKTLPGGIMVNGSRLKNLVLTYVNAISSGDLPCIENAVLALAQRENSAAVQKAIAHYDQQMGQKVQLPMETLQELLDLHRTSEREAIEVFMKNSFKDVDQSFQKELETLLDAKQNDICKRNLEASSDYCSALLKDIFGPLEEAVKQGIYSKPGGHNLFIQKTEELKAKYYREPRKGIQAEEVLQKYLKSKESVSHAILQTDQALTETEKKKKEAQVKAEAEKAEAQRLAAIQRQNEQMMQERERLHQEQVRQMEIAKQNWLAEQQKMQEQQMQEQAAQLSTTFQAQNRSLLSELQHAQRTVNNDDPCVLL 95DDC02F0FB705D0 gbp5-1 1 hGBP5ta 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction f5a mint In the GTP-bound (as well as in the nucleotide-free) state a Mapp of ~120 kDa is observed, which likely corresponds to a dimer. When bound to GppNHp hGBP5ta s Mapp is increased to ~200 kDa, which corresponds to a tetramer while the presence of GTPγS leads to an oligomer size intermediate of the GTP and GppNHp runs (see Figure 5a). gbp5-1 1 hGBP5 a/b 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction f5b mint ...the hGBP5 a/b splice variant does not show a monomer species in the presence of any nucleotide. Bound to GDP or GDP·AlFx we observe a dimeric form taking an elongated shape into account. Nucleotide free or in the presence of GTP the size of the protein complex is only slightly increased. As with hGBP5ta the complex is increased to hGBP5 a/b tetramer size after binding of GppNHp while again, binding of GTPγS show an intermediate behavior (Figure5b). gbp5-1 1 hGBP5ta 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction f5a mint In the GTP-bound (as well as in the nucleotide-free) state a Mapp of ~120 kDa is observed, which likely corresponds to a dimer. When bound to GppNHp hGBP5ta s Mapp is increased to ~200 kDa, which corresponds to a tetramer while the presence of GTPγS leads to an oligomer size intermediate of the GTP and GppNHp runs (see Figure 5a). gbp5-1 1 hGBP5 a/b 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction f5b mint ...the hGBP5 a/b splice variant does not show a monomer species in the presence of any nucleotide. Bound to GDP or GDP·AlFx we observe a dimeric form taking an elongated shape into account. Nucleotide free or in the presence of GTP the size of the protein complex is only slightly increased. As with hGBP5ta the complex is increased to hGBP5 a/b tetramer size after binding of GppNHp while again, binding of GTPγS show an intermediate behavior (Figure5b).