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 VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts. VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts. EMBO J. (0261-4189) 2002 Nawroth R., Poell G., Ranft A., Kloep S., Samulowitz U., Fachinger G., Golding M., Shima DT., Deutsch U., Vestweber D. no Phosphatases Text_Mining partial coverage rapid curation in vivo in vivo anti tag coip anti tag coimmunoprecipitation anti tag coip monoclonal western monoclonal antibody western blot monoclonal western Nawroth R., Poell G., Ranft A., Kloep S., Samulowitz U., Fachinger G., Golding M., Shima DT., Deutsch U., Vestweber D. no Phosphatases Text_Mining EMBO J. (0261-4189) 2002 partial coverage rapid curation ctnb1_human Catenin beta-1 Beta-catenin OK/SW-cl.35 PRO2286 CTNNB1 CTNNB protein protein human Homo sapiens Human MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL DIP protein P35222 original sequence version: 187 DIP protein P35222 original sequence version: 188 DIP protein P35222 original sequence version: 180 DIP protein P35222-1 original sequence version: 181 DIP protein P35222 original sequence version: 181 DIP protein P35222 original sequence version: 107 DIP protein P35222-1 original sequence version: 107 DIP protein P35222 original sequence version: 103 DIP protein P35222-1 original sequence version: 103 DIP protein P35222 original sequence version: 175 DIP protein P35222 original sequence version: 136 DIP protein P35222 original sequence version: 135 DIP protein P35222 original sequence version: 131 DIP protein P35222-1 original sequence version: 133 DIP protein P35222 original sequence version: 133 DIP protein P35222 original sequence version: 148 DIP protein P35222-1 original sequence version: 139 DIP protein P35222 original sequence version: 139 DIP protein P35222 original sequence version: 146 DIP protein P35222 original sequence version: 196 DIP protein P35222 original sequence version: 192 DIP protein P35222 original sequence version: 185 DIP protein P35222 original sequence version: 151 DIP protein P35222-1 original sequence version: 151 DIP protein P35222-1 original sequence version: 171 DIP protein P35222-1 original sequence version: 148 DIP protein P35222 original sequence version: 177 DIP protein P35222 original sequence version: 178 DIP protein P35222-1 original sequence version: 178 CB78F165A3EEF86E jam1_mouse Junctional adhesion molecule A F11r Jam1 Jcam Jcam1 Junctional adhesion molecule 1 protein protein mouse Mus musculus Mouse MGTEGKAGRKLLFLFTSMILGSLVQGKGSVYTAQSDVQVPENESIKLTCTYSGFSSPRVEWKFVQGSTTALVCYNSQITAPYADRVTFSSSGITFSSVTRKDNGEYTCMVSEEGGQNYGEVSIHLTVLVPPSKPTISVPSSVTIGNRAVLTCSEHDGSPPSEYSWFKDGISMLTADAKKTRAFMNSSFTIDPKSGDLIFDPVTAFDSGEYYCQAQNGYGTAMRSEAAHMDAVELNVGGIVAAVLVTLILLGLLIFGVWFAYSRGYFERTKKGTAPGKKVIYSQPSTRSEGEFKQTSSFLV DIP protein O88792 original sequence version: 123 mint Seems to plays a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3. The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly. Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier. Involved in platelet activation 3CE561E8FF3B97EC ptprb_mouse Receptor-type tyrosine-protein phosphatase beta Ptprb Vascular endothelial protein tyrosine phosphatase protein protein mouse Mus musculus Mouse MLRHGALTALWITLSVVQTGVAEQVKCNFTLLESRVSSLSASIQWRTFASPCNFSLIYSSDTSGPMWCHPIRIDNFTYGCNPKDLQAGTVYNFRIVSLDGEESTLVLQTDPLPPARFEVNREKTASTTLQVRWTPSSGKVSWYEVQLFDHNNQKIQEVQVQESTTWSQYTFLNLTEGNSYKVAITAVSGEKRSFPVYINGSTVPSPVKDLGISPNPNSLLISWSRGSGNVEQYRLVLMDKGAIVQDTNVDRRDTSYAFHELTPGHLYNLTIVTMASGLQNSRWKLVRTAPMEVSNLKVTNDGRLTSLNVKWQKPPGDVDSYSITLSHQGTIKESKTLAPPVTETQFKDLVPGRLYQVTISCISGELSAEKSAAGRTVPEKVRNLVSYNEIWMKSFTVNWTPPAGDWEHYRIVLFNESLVLLNTTVGKEETHYALDGLELIPGRQYEIEVIVESGNLRNSERCQGRTVPLAVLQLRVKHANETSLGITWRAPLGEWEKYIISLMDRELLVIHKSLSKDAKEFTFTDLMPGRNYKATVTSMSGDLKQSSSIKGRTVPAQVTDLHVNNQGMTSSLFTNWTKALGDVEFYQVLLIHENVVVKNESVSSDTSRYSFRALKPGSLYSVVVTTVSGGISSRQVVAEGRTVPSSVSGVTVNNSGRNDYLSVSWLPAPGEVDHYVVSLSHEGKVDQFLIIAKSVSECSFSSLTPGRLYNVTVTTKSGNYASHSFTEERTVPDKVQGISVSNSARSDYLKVSWVHATGDFDHYEVTIKNRESFIQTKTIPKSENECEFIELVPGRLYSVTVSTKSGQYEASEQGTGRTIPEPVKDLTLLNRSTEDLHVTWSRANGDVDQYEVQLLFNDMKVFPHIHLVNTATEYKFTALTPGRHYKILVLTISGDVQQSAFIEGLTVPSTVKNIHISANGATDRLMVTWSPGGGDVDSYVVSAFRQDEKVDSQTIPKHASEHTFHRLEAGAKYRIAIVSVSGSLRNQIDALGQTVPASVQGVVAANAYSSNSLTVSWQKALGVAERYDILLLNENGLLLSNVSEPATARQHKFEDLTPGKKYKMQILTVSGGLFSKESQAEGRTVPAAVTNLRITENSSRYLSFGWTASEGELSWYNIFLYNPDRTLQERAQVDPLVQSFSFQNLLQGRMYKMVIVTHSGELSNESFIFGRTVPAAVNHLKGSHRNTTDSLWFSWSPASGDFDFYELILYNPNGTKKENWKEKDVTEWRFQGLVPGRKYTLYVVTHSGDLSNKVTGEGRTAPSPPSLLSFADVANTSLAITWKGPPDWTDYNDFELQWFPGDALTIFNPYSSRKSEGRIVYGLHPGRSYQFSVKTVSGDSWKTYSKPISGSVRTKPDKIQNLHCRPQNSTAIACSWIPPDSDFDGYSIECRKMDTQEIEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAGMTSEVVEDSTITMIDRPPQPPPHIRVNEKDVLISKSSINFTVNCSWFSDTNGAVKYFAVVVREADSMDELKPEQQHPLPSYLEYRHNASIRVYQTNYFASKCAESPDSSSKSFNIKLGAEMDSLGGKCDPSQQKFCDGPLKPHTAYRISIRAFTQLFDEDLKEFTKPLYSDTFFSMPITTESEPLFGVIEGVSAGLFLIGMLVALVAFFICRQKASHSRERPSARLSIRRDRPLSVHLNLGQKGNRKTSCPIKINQFEGHFMKLQADSNYLLSKEYEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLRAKKLRNEQENPLFPIYENVNPEYHRDAIYSRH mint 066EE7141F942887 ptprb-ctnnb1-2 1 4 monoclonal western monoclonal antibody western blot monoclonal western 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 2 monoclonal western monoclonal antibody western blot monoclonal western predetermined predetermined participant predetermined unspecified role unspecified role prey prey over-expressed over expressed level over-expressed Stoichiometry: 1.0 physical association physical association true The article mentions that in similar co-precipitation exp, interaction between these two proteins was actually found. mint ptprb-f11r 1 4 monoclonal western monoclonal antibody western blot monoclonal western 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 3 monoclonal western monoclonal antibody western blot monoclonal western predetermined predetermined participant predetermined unspecified role unspecified role prey prey over-expressed over expressed level over-expressed Stoichiometry: 1.0 physical association physical association true mint