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 Rhodopsin C terminus, the site of mutations causing retinal disease, regulates trafficking by binding to ADP-ribosylation factor 4 (ARF4). Rhodopsin C terminus, the site of mutations causing retinal disease, regulates trafficking by binding to ADP-ribosylation factor 4 (ARF4). Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2005 Deretic D., Williams AH., Ransom N., Morel V., Hargrave PA., Arendt A. suggested by aryamontry dderetic@salud.unm.edu in vitro In vitro pull down pull down predetermined predetermined participant predetermined Deretic D., Williams AH., Ransom N., Morel V., Hargrave PA., Arendt A. suggested by aryamontry dderetic@salud.unm.edu Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2005 opsd_xenla Rhodopsin rho protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MNGTEGPNFYVPMSNKTGVVRSPFDYPQYYLAEPWQYSALAAYMFLLILLGLPINFMTLFVTIQHKKLRTPLNYILLNLVFANHFMVLCGFTVTMYTSMHGYFIFGPTGCYIEGFFATLGGEVALWSLVVLAVERYIVVCKPMANFRFGENHAIMGVAFTWIMALSCAAPPLFGWSRYIPEGMQCSCGVDYYTLKPEVNNESFVIYMFIVHFTIPLIVIFFCYGRLLCTVKEAAAQQQESLTTQKAEKEVTRMVVIMVVFFLICWVPYAYVAFYIFTHQGSNFGPVFMTVPAFFAKSSAIYNPVIYIVLNKQFRNCLITTLCCGKNPFGDEDGSSAATSKTEASSVSSSQVSPA Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal mint CD18F49EC63D8FFE arf4_xenla ADP-ribosylation factor 4 arf4 protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MGLTISSLFSRLFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERIQEAAEELQKMLQEDELRDAVLLVFANKQDLPNAMAISEMTDKLTLQTLRNRTWYVQATCATQGTGLYEGLDWLSNELSKR GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus mint 91E98C2D857D7504 rho-arf4 1 Rhodopsin 2 predetermined predetermined participant predetermined 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-6826086: original sequence: 330-354 : DEDGSSAATSKTEASSVSSSQVSP biotin tagged biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ARF4 3 fingerprinting peptide massfingerprinting fingerprinting predetermined predetermined participant predetermined unspecified role unspecified role prey prey cell lysate cell lysate physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association F1C F1D mint rho-arf4-1 1 ARF4 3 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role prey prey cell lysate cell lysate physiological level physiological level endogenous level endogenous endogenous endogenous level Rhodopsin 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified biotin tagged biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-6826097: original sequence: 330-354 : DEDGSSAATSKTEASSVSSSQVSP physical association physical association F2B mint