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 interaction network of rhodopsin involving the heterotrimeric G protein transducin and the monomeric GTPase Rac1 is determined by distinct binding processes. The interaction network of rhodopsin involving the heterotrimeric G protein transducin and the monomeric GTPase Rac1 is determined by distinct binding processes. FEBS J. (1742-464X) 2014 imex curation Köster M., Dell Orco D., Koch K.W. karl.w.koch@uni-oldenburg.de 20-Oct-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined karl.w.koch@uni-oldenburg.de Accepted 2014-SEP-22 by LUANA 2014 imex curation 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 rac1_human Ras-related C3 botulinum toxin substrate 1 RAC1 MIG5 p21-Rac1 Ras-like protein TC25 Cell migration-inducing gene 5 protein TC25 protein protein human Homo sapiens Human MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKRKRKCLLL ACEDF83A45E5EA67 rac1-rho-1 1 rhodopsin 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified Rac1 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified direct interaction direct interaction f3 Rac1 bound to immobilized rhodopsin in a concentration dependent manner (Figure 3A). The binding process was not triggered by light, since Rac1 bound to dark-adapted rhodopsin in a similar manner as to light-activated rhodopsin and binding of Rac1 to rhodopsin was not reversed by adding GTPγS (Figure 3B), which can be used to rapidly dissociate Gt from rhodopsin that is immobilized on a sensor chip surface Further, the amount of Rac1 interacting with rhodopsin was not increased by illumination as can be seen in Figure 3C, where rhodopsin was bleached after Rac1 was injected into the flow cell and the sensorgram was compared with a recording done in darkness