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 Polypeptide in the chaperonin cage partly protrudes out and then folds inside or escapes outside. Polypeptide in the chaperonin cage partly protrudes out and then folds inside or escapes outside. EMBO J. (0261-4189) 2010 imex curation Motojima F., Yoshida M. 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 Motojima F., Yoshida M. EMBO J. (0261-4189) 2010 Only protein-protein interactions imex curation Polypeptide in the chaperonin cage partly protrudes out and then folds inside or escapes outside. Polypeptide in the chaperonin cage partly protrudes out and then folds inside or escapes outside. EMBO J. (0261-4189) 2010 imex curation Motojima F., Yoshida M. Only protein-protein interactions in vitro In vitro fluorescence fluorescence technology fluorescence predetermined predetermined participant predetermined Motojima F., Yoshida M. EMBO J. (0261-4189) 2010 Only protein-protein interactions imex curation Polypeptide in the chaperonin cage partly protrudes out and then folds inside or escapes outside. Polypeptide in the chaperonin cage partly protrudes out and then folds inside or escapes outside. EMBO J. (0261-4189) 2010 imex curation Motojima F., Yoshida M. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Motojima F., Yoshida M. EMBO J. (0261-4189) 2010 Only protein-protein interactions imex curation dyr_mouse Dihydrofolate reductase Dhfr protein protein mouse Mus musculus Mouse MVRPLNCIVAVSQNMGIGKNGDLPWPPLRNEFKYFQRMTTTSSVEGKQNLVIMGRKTWFSIPEKNRPLKDRINIVLSRELKEPPRGAHFLAKSLDDALRLIEQPELASKVDMVWIVGGSSVYQEAMNQPGHLRLFVTRIMQEFESDTFFPEIDLGKYKLLPEYPGVLSEVQEEKGIKYKFEVYEKKD mint 47AEF15F879B119C ch60_ecoli Chaperonin GroEL groEL 60 kDa chaperonin Chaperonin-60 GroEL protein groL mopA JW4103 b4143 protein protein ecoli Escherichia coli (strain K12) MAAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPLRQIVLNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKNDAADLGAAGGMGGMGGMGGMM CD3A0FB505F74AD1 CD3A0FB505F74AD1 rbl2_rhoru Ribulose bisphosphate carboxylase cbbM cbbL2 rbpL protein protein rhoru Rhodospirillum rubrum MDQSSRYVNLALKEEDLIAGGEHVLCAYIMKPKAGYGYVATAAHFAAESSTGTNVEVCTTDDFTRGVDALVYEVDEARELTKIAYPVALFHRNITDGKAMIASFLTLTMGNNQGMGDVEYAKMHDFYVPEAYRALFDGPSVNISALWKVLGRPEVDGGLVVGTIIKPKLGLRPKPFAEACHAFWLGGDFIKNDEPQGNQPFAPLRDTIALVADAMRRAQDETGEAKLFSANITADDPFEIIARGEYVLETFGENASHVALLVDGYVAGAAAITTARRRFPDNFLHYHRAGHGAVTSPQSKRGYTAFVHCKMARLQGASGIHTGTMGFGKMEGESSDRAIAYMLTQDEAQGPFYRQSWGGMKACTPIISGGMNALRMPGFFENLGNANVILTAGGGAFGHIDGPVAGARSLRQAWQAWRDGVPVLDYAREHKELARAFESFPGDADQIYPGWRKALGVEDTRSALPA mint 37D8C0076CAF7D54 thtr_human Thiosulfate sulfurtransferase TST Rhodanese protein protein human Homo sapiens Human MVHQVLYRALVSTKWLAESIRTGKLGPGLRVLDASWYSPGTREARKEYLERHVPGASFFDIEECRDTASPYEMMLPSEAGFAEYVGRLGISNHTHVVVYDGEHLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAVFKATLDRSLLKTYEQVLENLESKRFQLVDSRSQGRFLGTEPEPDAVGLDSGHIRGAVNMPFMDFLTEDGFEKGPEELRALFQTKKVDLSQPLIATCRKGVTACHVALAAYLCGKPDVAVYDGSWSEWFRRAPPESRVSQGKSEKA mint Formation of iron-sulfur complexes, cyanide detoxification or modification of sulfur-containing enzymes. Other thiol compounds, besides cyanide, can act as sulfur ion acceptors. Also has weak mercaptopyruvate sulfurtransferase (MST) activity BDAE6EE4E47A5650 ch10_ecoli Co-chaperonin GroES groES 10 kDa chaperonin Chaperonin-10 groS mopB JW4102 b4142 protein protein ecoli Escherichia coli (strain K12) MNIRPLHDRVIVKRKEVETKSAGGIVLTGSAAAKSTRGEVLAVGNGRILENGEVKPLDVKVGDIVIFNDGYGVKSEKIDNEEVLIMSESDILAIVEA 76829E09B11217EF 76829E09B11217EF groel-groes 2 Rhodanese 7 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified GroES 8 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified GroEL 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association f1 mint We examined the chaperonin-assisted folding of rhodanese by using SR398, a single-ring version of GroEL with a very slow ATP-hydrolysing mutation (D398A), supplemented with aluminium fluoride (AlFx), to allow only a single round of GroES binding. dhfr-groel 2 DHFR 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified GroEL 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified undefined mutation mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:51:32 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'mutation decreasing' Asn265Ala GroES 8 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association f5a mint As observed for rhodanese, the SR1-assisted folding of DHFR and Rubisco was interfered with trap(N265A) (Figure 5A and B). cbbm-groel 2 Rubisco 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified GroES 8 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified GroEL 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified undefined mutation mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:43:35 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'mutation decreasing' Asn265Ala physical association physical association f5b mint As observed for rhodanese, the SR1-assisted folding of DHFR and Rubisco was interfered with trap(N265A) (Figure 5A and B). groel-tst 3 Rhodanese 7 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified GroEL 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f3b mint we identified four residues, F44C, Y203C, R231C and V264C, which were cross-linked to rhodanese after the addition of ATP. groel-groes-1 1 Rhodanese 7 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified GroEL 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified GroES 8 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association f1d mint The SR398 GroES rhodaneseAlexa ternary complex was formed by addition of ATP together with antibody, trap(N265A) or trap(D87K) and, after a 30-min incubation, the solutions were applied to a gel-filtration column with monitoring of the fluorescence of Alexa...Gel-filtration analysis revealed that 0.1 mM trap(D87K) captured rhodanese in the free monomer fraction, but did not affect rhodanese in the SR398 GroES fraction (Figure 1D). cbbm-groel-1 1 Rubisco 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified GroES 8 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified GroEL 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified undefined mutation mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:28:53 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'mutation decreasing' Asn265Ala physical association physical association f5d mint Trap(N265A) bound to DHFR and Rubisco in the ternary complex, dragged out and formed large molecular weight conjugates as shown in the gel-filtration analysis (Figure 5C and D). dhfr-groel-1 1 DHFR 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified GroEL 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified undefined mutation mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:30:33 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'mutation decreasing' Asn265Ala GroES 8 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association f5c mint Trap(N265A) bound to DHFR and Rubisco in the ternary complex, dragged out and formed large molecular weight conjugates as shown in the gel-filtration analysis (Figure 5C and D).