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 The neural cell adhesion molecule binds to fibroblast growth factor receptor 2. The neural cell adhesion molecule binds to fibroblast growth factor receptor 2. FEBS Lett. (0014-5793) 2006 imex curation Christensen C., Lauridsen JB., Berezin V., Bock E., Kiselyov VV. 2009-01-08 Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Christensen C., Lauridsen JB., Berezin V., Bock E., Kiselyov VV. FEBS Lett. (0014-5793) 2006 2009-01-08 Only protein-protein interactions imex curation fgfr1_mouse Fibroblast growth factor receptor 1 Fgfr1 Flg Basic fibroblast growth factor receptor 1 MFR Proto-oncogene c-Fgr protein protein mouse Mus musculus Mouse MWGWKCLLFWAVLVTATLCTARPAPTLPEQAQPWGVPVEVESLLVHPGDLLQLRCRLRDDVQSINWLRDGVQLVESNRTRITGEEVEVRDSIPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRRPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMLGSVIIYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSIPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHPTQLANSGLKRR DIP protein P16092 original sequence version: 162 DIP protein P16092 original sequence version: 124 mint Receptor for basic fibroblast growth factor. A shorter form of the receptor could be a receptor for FGF1 (aFGF) homomint D5A4695FA680926B ncam1_rat Neural cell adhesion molecule 1 Ncam1 Ncam protein protein rat Rattus norvegicus (Rat) Rat MLRTKDLIWTLFFLGTAVSLQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLSPNQQRISVVWNDDDSSTLTIYNANIDDAGIYKCVVTAEDGTQSEATVNVKIFQKLMFKNAPTPQEFKEGEDAVIVCDVVSSLPPTIIWKHKGRDVILKKDVRFIVLSNNYLQIRGIKKTDEGTYRCEGRILARGEINFKDIQVIVNVPPTVQARQSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQDASIHLKVFAKPKITYVENQTAMELEEQVTLTCEASGDPIPSITWRTSTRNISSEEKASWTRPEKQETLDGHMVVRSHARVSSLTLKSIQYTDAGEYICTASNTIGQDSQSMYLEVQYAPKLQGPVAVYTWEGNQVNITCEVFAYPSATISWFRDGQLLPSSNYSNIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQESLEFILVQADTPSSPSIDRVEPYSSTAQVQFDEPEATGGVPILKYKAEWKSLGEEAWHSKWYDAKEANMEGIVTIMGLKPETRYAVRLAALNGKGLGEISAATEFKTQPVREPSAPKLEGQMGEDGNSIKVNLIKQDDGGSPIRHYLVKYRALASEWKPEIRLPSGSDHVMLKSLDWNAEYEVYVVAENQQGKSKAAHFVFRTSAQPTAIPANGSPTAGLSTGAIVGILIVIFVLLLVVMDITCYFLNKCGLLMCIAVNLCGKAGPGAKGKDMEEGKAAFSKDESKEPIVEVRTEEERTPNHDGGKHTEPNETTPLTEPEKGPVETKSEPQESEAKPAPTEVKTVPNEATQTKENESKA EA1A06A4EA0550F6 fgf1_rat Fibroblast growth factor 1 Fgf1 Fgf-1 Fgfa Heparin-binding growth factor 1 Acidic fibroblast growth factor protein protein rat Rattus norvegicus (Rat) Rat MAEGEITTFAALTERFNLPLGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESAGEVYIKGTETGQYLAMDTEGLLYGSQTPNEECLFLERLEENHYNTYTSKKHAEKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLPVSSD mint The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors 8880E4FF0FBA4161 q63237_rat Receptor protein-tyrosine kinase Fgfr2 protein protein rat Rattus norvegicus (Rat) Rat MLPTNISVQMGLTSTWRYGTGPGIGTVTMVSWGRFICLVLVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEACVVAPGESLELRCMLKDAAVISWTKDGVHLGPNNRTVLIGEYLQIKGATPRDSGLYACAAARTVDSETLYFMVNVTDAISSGDDEDDTDSSEDFVSENRSNQRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCLVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLPAPVREKEITASPDYLEIAIYSIGVFLIACMVVTVIFCRMKTTTKKPDFSSQPAVHKL fragmentation type: fragment mint A8C3BFD1D7DBB123 fgfr2-fgf1 1 4 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified Stoichiometry: 1.0 5 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-2635574: original sequence: 166-384 : DSSEDFVSENRSNQRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCLVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSA Stoichiometry: 1.0 direct interaction direct interaction F1 To test if the FGFR2 fragment was expressed in a functionally active form, the protein was immobilized on the surface of a CM-5 sensor chip, and its binding to FGF1 was studied by SPR and compared to that of the corresponding FGFR1 fragment. kd 5 nanomolar FEBS-Letters mint fgfr1-fgf1-1 1 4 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified Stoichiometry: 1.0 2 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-2635579: original sequence: 141-365 : TDNTKPNRRPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEE Stoichiometry: 1.0 direct interaction direct interaction F1 To test if the FGFR2 fragment was expressed in a functionally active form, the protein was immobilized on the surface of a CM-5 sensor chip, and its binding to FGF1 was studied by SPR and compared to that of the corresponding FGFR1 fragment. kd 5 nanomolar FEBS-Letters homomint mint fgfr2-ncam1 1 5 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-2635641: original sequence: 166-384 : DSSEDFVSENRSNQRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCLVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSA Stoichiometry: 1.0 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-2635698: original sequence: 507-705 : QADTPSSPSIDRVEPYSSTAQVQFDEPEATGGVPILKYKAEWKSLGEEAWHSKWYDAKEANMEGIVTIMGLKPETRYAVRLAALNGKGLGEISAATEFKTQPVREPSAPKLEGQMGEDGNSIKVNLIKQDDGGSPIRHYLVKYRALASEWKPEIRLPSGSDHVMLKSLDWNAEYEVYVVAENQQGKSKAAHFVFRTSA Stoichiometry: 1.0 direct interaction direct interaction T1 F2 Therefore, binding of the immobilized FGFR2 Ig modules 2 3 to soluble NCAM F3 modules 1 2 was studied by SPR (Fig. 2A). In order to determine the Kd value of the NCAM FGFR2 interaction, the equilibrium binding level of the F3 modules was plotted versus the concentration of the F3 modules in solution and fitted with an equation describing the single-site receptor ligand equilibrium binding (Fig. 2B).In comparison to the NCAM FGFR1 binding, the NCAM FGFR2 binding is characterized by much faster association and dissociation phases and approximately the same affinity. A detailed comparison of the kinetic parameters for the two interactions is shown in Table 1. kd 9,21 micromolar FEBS-Letters mint fgfr1-ncam1 1 2 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-2635686: original sequence: 141-365 : TDNTKPNRRPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEE Stoichiometry: 1.0 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-2635733: original sequence: 507-705 : QADTPSSPSIDRVEPYSSTAQVQFDEPEATGGVPILKYKAEWKSLGEEAWHSKWYDAKEANMEGIVTIMGLKPETRYAVRLAALNGKGLGEISAATEFKTQPVREPSAPKLEGQMGEDGNSIKVNLIKQDDGGSPIRHYLVKYRALASEWKPEIRLPSGSDHVMLKSLDWNAEYEVYVVAENQQGKSKAAHFVFRTSA Stoichiometry: 1.0 direct interaction direct interaction T1 F2 Therefore, binding of the immobilized FGFR2 Ig modules 2 3 to soluble NCAM F3 modules 1 2 was studied by SPR (Fig. 2A). In order to determine the Kd value of the NCAM FGFR2 interaction, the equilibrium binding level of the F3 modules was plotted versus the concentration of the F3 modules in solution and fitted with an equation describing the single-site receptor ligand equilibrium binding (Fig. 2B).In comparison to the NCAM FGFR1 binding, the NCAM FGFR2 binding is characterized by much faster association and dissociation phases and approximately the same affinity. A detailed comparison of the kinetic parameters for the two interactions is shown in Table 1. kd 9,97 micromolar FEBS-Letters homomint mint fgfr2-ncam1-1 1 5 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-2635730: original sequence: 166-384 : DSSEDFVSENRSNQRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCLVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSA Stoichiometry: 1.0 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-2635719: original sequence: 612-705 : PSAPKLEGQMGEDGNSIKVNLIKQDDGGSPIRHYLVKYRALASEWKPEIRLPSGSDHVMLKSLDWNAEYEVYVVAENQQGKSKAAHFVFRTSA Stoichiometry: 1.0 direct interaction direct interaction T1 F2 We also tested binding of the FGFR2 fragment to the FGL peptide (Fig. 2C), previously shown to bind FGFR1 [6]. The FGL peptide corresponds to a binding site for FGFR1 in NCAM (the FG loop region of the NCAM F3 module 2). The calculated Kd value for the FGFR2-FGL interaction was very similar to that for the FGFR1-FGL interaction (see Table 1). kd 1,75 micromolar FEBS-Letters mint fgfr1-ncam1-1 1 2 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-2635750: original sequence: 141-365 : TDNTKPNRRPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEE Stoichiometry: 1.0 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-2635743: original sequence: 612-705 : PSAPKLEGQMGEDGNSIKVNLIKQDDGGSPIRHYLVKYRALASEWKPEIRLPSGSDHVMLKSLDWNAEYEVYVVAENQQGKSKAAHFVFRTSA Stoichiometry: 1.0 direct interaction direct interaction T1 F2 kd 2,58 micromolar We also tested binding of the FGFR2 fragment to the FGL peptide (Fig. 2C), previously shown to bind FGFR1 [6]. The FGL peptide corresponds to a binding site for FGFR1 in NCAM (the FG loop region of the NCAM F3 module 2). The calculated Kd value for the FGFR2-FGL interaction was very similar to that for the FGFR1-FGL interaction (see Table 1). FEBS-Letters homomint mint