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 Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin. Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin. J. Biol. Chem. (0021-9258) 1993 Gurevich VV., Benovic JL. suggested by aryamontry in vitro In vitro chromatography chromatography technology column chromatography chromatography predetermined predetermined participant predetermined Gurevich VV., Benovic JL. suggested by aryamontry J. Biol. Chem. (0021-9258) 1993 arrs_bovin S-arrestin SAG Retinal S-antigen 48 kDa protein Rod photoreceptor arrestin protein protein bovin Bos taurus (Bovine) Bovine MKANKPAPNHVIFKKISRDKSVTIYLGKRDYIDHVERVEPVDGVVLVDPELVKGKRVYVSLTCAFRYGQEDIDVMGLSFRRDLYFSQVQVFPPVGASGATTRLQESLIKKLGANTYPFLLTFPDYLPCSVMLQPAPQDVGKSCGVDFEIKAFATHSTDVEEDKIPKKSSVRLLIRKVQHAPRDMGPQPRAEASWQFFMSDKPLRLAVSLSKEIYYHGEPIPVTVAVTNSTEKTVKKIKVLVEQVTNVVLYSSDYYIKTVAAEEAQEKVPPNSSLTKTLTLVPLLANNRERRGIALDGKIKHEDTNLASSTIIKEGIDKTVMGILVSYQIKVKLTVSGLLGELTSSEVATEVPFRLMHPQPEDPDTAKESFQDENFVFEEFARQNLKDAGEYKEEKTDQEAAMDE mint S-antigen induces autoimmune uveitis Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated-phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase. Isoform B plays a role in the phototransduction cascade 26B1D80B652AF1EF opsd_bovin Rhodopsin RHO protein protein bovin Bos taurus (Bovine) Bovine MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIPEGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKTSAVYNPVIYIMMNKQFRNCMVTTLCCGKNPLGDDEASTTVSKTETSQVAPA DIP protein P02699 original sequence version: 157 DIP protein P02699 original sequence version: 158 DIP protein P02699 original sequence version: 88 DIP protein P02699 original sequence version: 160 DIP protein P02699 original sequence version: 152 DIP protein P02699 original sequence version: 136 DIP protein P02699 original sequence version: 135 DIP protein P02699 original sequence version: 141 mint Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal 33FDA196803E81F3 rho-sag 1 Rhodopsin 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Arrestin 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component in vitro translated in vitro translated protein in vitro translated binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-6825313: original sequence: 1-404 : MKANKPAPNHVIFKKISRDKSVTIYLGKRDYIDHVERVEPVDGVVLVDPELVKGKRVYVSLTCAFRYGQEDIDVMGLSFRRDLYFSQVQVFPPVGASGATTRLQESLIKKLGANTYPFLLTFPDYLPCSVMLQPAPQDVGKSCGVDFEIKAFATHSTDVEEDKIPKKSSVRLLIRKVQHAPRDMGPQPRAEASWQFFMSDKPLRLAVSLSKEIYYHGEPIPVTVAVTNSTEKTVKKIKVLVEQVTNVVLYSSDYYIKTVAAEEAQEKVPPNSSLTKTLTLVPLLANNRERRGIALDGKIKHEDTNLASSTIIKEGIDKTVMGILVSYQIKVKLTVSGLLGELTSSEVATEVPFRLMHPQPEDPDTAKESFQDENFVFEEFARQNLKDAGEYKEEKTDQEAAMD physical association physical association F2B homomint mint