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 de_paula-2005-1 Biochemical characterization of Neurospora crassa glycogenin (GNN), the self-glucosylating initiator of glycogen synthesis. yeast Saccharomyces cerevisiae 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 de Paula RM., Wilson WA., Roach PJ., Terenzi HF., Bertolini MC. FEBS Lett. (0014-5793) 2005 2009-01-08 Only protein-protein interactions imex curation q96us6_neucs Glycogen [starch] synthase gsn protein protein neucs Neurospora crassa MAHDNREPREVKNHLLFEVATEVAHRVGGIYSVLKSKAPVTTAEYGDRYTLIGPLNHQSAAVEVEELEPSNPELKATIQAMRDRGIGILYGRWLIEGAPRVLLFDTKTAYGYMNEWKTDLWNVASIPSPDNDEETNEAIVFGYLVAWFLGEFVCHEKRKAVIAHFHEWLAGVALPLTKKRQIDVTTIFTTHATLLGPYLCAGSVDFYNNLQWFDVDAEAGKRGIYHRYCIERAAAHSCDVFTTVSHITAYESEHLLKRKPDGVLPNGLNVTKFSAMHEFQNLHQQNKEKIHDFVRGHFYGHYDFEPENTLYFFTAGRYEFRNKGVDMFIESLARLNHRLKTAGSKTTVVAFIIMPAQTTSLTVEALKGQAVIKSLRDTVDVIERGIGRRIFERSVKWHEGDPLPEEKELITSQDRVLLRRRLFAMKRHTLPPIVTHNMLNDHEDPILNQIRRVQLFNHPSDRVKIVFHPEFLSSANPVLPLDYDDFVRGTHLGVFASYYEPWGYTPAECTVMGVPSITTNLSGFGCYMEELIENSSDYGIYIVDRRSKGVDDSVNQLTQYMFEFTQKSRRQRINQRNRTERLSDLLDWKRMGMEYVKARQLALRRAYPTSFNGEEEEDFIPGVEQKISRPFSVPGSPRDRTGMMTPGDFASLQESHEGLSTEDYVAWKLPEEEDPEEYPFPLTLKQRTGPGSPLDSIQGLQLNGTR mint q6q2c8_neucs gnn protein protein neucs Neurospora crassa MAITKGEDVYASLLLNDAYLPGALVLAHSLRDSGTHKKLAILITPENISNEVVEQLQTVYDYVIPVETIQNDRPANLFLMNRPDLHSAFTKINLWKQTQFRKIVYIDADVVAYRAPDELFDLPHAFSAAPDIGWPDLFNTGVMVLSPNMGDYYAMLAMAERGISFDGADQGLLNMHFRNTYNRLSFTYNVTPSAHYQYIPAYKHFQSSINLLHFIGSEKPWVQGRTQTTGSSTYDEMIGRWWAVYDRHYRGNSNKTTDVVQKFVKGEQQQQQQQQQRNVSFQLPSSQSHKTQSHQTQSQNTHSTYTSHGASWDASRHSPPAGSKPEAANFPQTHYTMSSNTQQFVPPARYPSPPKDMWYKVPEAAPTQKPAPIFPWEKQAPEPTRVFPEPPPEQGKLSAASTATPSAVASATASPTLEPKSEAVTPTTPASANPWTSFTTRGNAWDDVPEINRYVDALQKHRRSGSKGSAAATSRPTSPGRAQSRSRKSSRVTDFPTEDDRPSLTVTPAPIQGPRSSRGENERQFPAAAGVPAQSEWNPAVQLEKLAIHQQETLQKLGERPAFGGLAIGTAGKEIPARALPFGSEDARSPTYVTQYPSVLSPKPLRANTTGTNSTPSPLPTQPSVTTAPPSYQGPGVAFEKGEDFPTHETPALPTEEERDVLET mint gsn-gnn-1 182111 q96us6_neucr 182112 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role bait bait over-expressed over expressed level over-expressed tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 q6q2c8_neucr 182113 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role prey prey over-expressed over expressed level over-expressed tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 physical association physical association false false false F5 Deletion of the 51 (GNNΔ613) and 119 (GNNΔ545) C-terminal amino acids reduced the interaction between the two proteins to about 82% and 69%, respectively. Moreover, the truncated mutants GNNΔ360, GNNΔ306, and GNNΔ245 interacted much more weakly with GSN, yielding only about 10% of the reporter activity detected with wild type GNN. On the other hand, a polypeptide comprising only the C-terminus of GNN (GNN490–664), interacted poorly with GSN and this was only slightly enhanced by enlarging it to span residues 337–664 (GNN337–664).Taken together, these results argue that the C-terminal region of GNN, starting at residue 360, dominates the interaction with GSN but that interaction depends on the integrity of the N-terminus. mint gnn-gsn-1 182111 q96us6_neucr 182112 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role prey prey over-expressed over expressed level over-expressed tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 q6q2c8_neucr 182113 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role bait bait over-expressed over expressed level over-expressed tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 physical association physical association false false false F5 Deletion of the 51 (GNNΔ613) and 119 (GNNΔ545) C-terminal amino acids reduced the interaction between the two proteins to about 82% and 69%, respectively. Moreover, the truncated mutants GNNΔ360, GNNΔ306, and GNNΔ245 interacted much more weakly with GSN, yielding only about 10% of the reporter activity detected with wild type GNN. On the other hand, a polypeptide comprising only the C-terminus of GNN (GNN490–664), interacted poorly with GSN and this was only slightly enhanced by enlarging it to span residues 337–664 (GNN337–664).Taken together, these results argue that the C-terminal region of GNN, starting at residue 360, dominates the interaction with GSN but that interaction depends on the integrity of the N-terminus. mint