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 Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins. Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins. J. Biol. Chem. (0021-9258) 1996 Groisman R., Masutani H., Leibovitch MP., Robin P., Soudant I., Trouche D., Harel-Bellan A. no in vitro In vitro pull down pull down predetermined predetermined participant predetermined Groisman R., Masutani H., Leibovitch MP., Robin P., Soudant I., Trouche D., Harel-Bellan A. no J. Biol. Chem. (0021-9258) 1996 Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins. Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins. J. Biol. Chem. (0021-9258) 1996 Groisman R., Masutani H., Leibovitch MP., Robin P., Soudant I., Trouche D., Harel-Bellan A. no in vivo in vivo 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 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Groisman R., Masutani H., Leibovitch MP., Robin P., Soudant I., Trouche D., Harel-Bellan A. no J. Biol. Chem. (0021-9258) 1996 myog_human Myogenin MYOG BHLHC3 MYF4 Class C basic helix-loop-helix protein 3 Myogenic factor 4 protein protein human Homo sapiens Human MELYETSPYFYQEPRFYDGENYLPVHLQGFEPPGYERTELTLSPEAPGPLEDKGLGTPEHCPGQCLPWACKVCKRKSVSVDRRRAATLREKRRLKKVNEAFEALKRSTLLNPNQRLPKVEILRSAIQYIERLQALLSSLNQEERDLRYRGGGGPQPGVPSECSSHSASCSPEWGSALEFSANPGDHLLTADPTDAHNLHSLTSIVDSITVEDVSVAFPDETMPN 91421D69B57551FB srf_human Serum response factor SRF protein protein human Homo sapiens Human MLPTQAGAAAALGRGSALGGSLNRTPTGRPGGGGGTRGANGGRVPGNGAGLGPGRLEREAAAAAATTPAPTAGALYSGSEGDSESGEEEELGAERRGLKRSLSEMEIGMVVGGPEASAAATGGYGPVSGAVSGAKPGKKTRGRVKIKMEFIDNKLRRYTTFSKRKTGIMKKAYELSTLTGTQVLLLVASETGHVYTFATRKLQPMITSETGKALIQTCLNSPDSPPRSDPTTDQRMSATGFEETDLTYQVSESDSSGETKDTLKPAFTVTNLPGTTSTIQTAPSTSTTMQVSSGPSFPITNYLAPVSASVSPSAVSSANGTVLKSTGSGPVSSGGLMQLPTSFTLMPGGAVAQQVPVQAIQVHQAPQQASPSRDSSTDLTQTSSSGTVTLPATIMTSSVPTTVGGHMMYPSPHAVMYAPTSGLGDGSLTVLNAFSQAPSTMQVSHSQVQEPGGVPQVFLTASSGTVQIPVSAVQLHQMAVIGQQAGSSSNLTELQVVNLDTAHSTKSE DIP protein P11831 original sequence version: 178 25505828D3276F44 myod1_human Myoblast determination protein 1 Myogenic factor 3 MYOD1 MYF3 MYOD BHLHC1 Class C basic helix-loop-helix protein 1 protein protein human Homo sapiens Human MELLSPPLRDVDLTAPDGSLCSFATTDDFYDDPCFDSPDLRFFEDLDPRLMHVGALLKPEEHSHFPAAVHPAPGAREDEHVRAPSGHHQAGRCLLWACKACKRKTTNADRRKAATMRERRRLSKVNEAFETLKRCTSSNPNQRLPKVEILRNAIRYIEGLQALLRDQDAAPPGAAAAFYAPGPLPPGRGGEHYSGDSDASSPRSNCSDGMMDYSGPPSGARRRNCYEGAYYNEAPSEPRPGKSAAVSSLDCLSSIVERISTESPAAPALLLADVPSESPPRRQEAAAPSEGESSGDPTQSPDAAPQCPAGANPNPIYQVL 75E624D2ED5B0B33 srf-myod1 1 5 unspecified role unspecified role prey prey purified purified Stoichiometry: 1.0 4 unspecified role unspecified role bait bait purified purified Stoichiometry: 1.0 direct interaction direct interaction No complex could be detected between MyoD and SRF in the absence of E12. A likely interpretation of this result is that heterodimeric formation between E12 and MyoD induces a conformational change in the proteins thatunmasks a site of interaction with SRF homomint mint srf-myog 1 4 unspecified role unspecified role bait bait purified purified Stoichiometry: 1.0 3 unspecified role unspecified role prey prey purified purified Stoichiometry: 1.0 direct interaction direct interaction No complex could be detected between myogenin and SRF in the absence of E12. A likely interpretation of this result is that heterodimeric formation between E12 and myogenin induces a conformational change in the proteins that unmasks a site of interaction with SRF. homomint mint srf-myog-1 2 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined 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 Stoichiometry: 1.0 4 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined 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 Stoichiometry: 1.0 physical association physical association No complex could be detected between myogenin and SRF in the absence of E12. A likely interpretation of this result is that heterodimeric formation between E12 and myogenin induces a conformational change in the proteins that unmasks a site of interaction with SRF. homomint mint srf-myod1-1 2 4 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined 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 Stoichiometry: 1.0 5 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined 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 Stoichiometry: 1.0 physical association physical association No complex could be detected between MyoD and SRF in the absence of E12. A likely interpretation of this result is that heterodimeric formation between E12 and MyoD induces a conformational change in the proteins thatunmasks a site of interaction with SRF homomint mint