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 Actin pedestal formation by enteropathogenic Escherichia coli is regulated by IQGAP1, calcium, and calmodulin. Actin pedestal formation by enteropathogenic Escherichia coli is regulated by IQGAP1, calcium, and calmodulin. The Journal of biological chemistry 2008 imex curation Brown MD., Bry L., Li Z., Sacks DB. dsacks@rics.bwh.harvard.edu 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 fluorescence imaging fluorescence microscopy fluorescence imaging immunostaining immunostaining Brown MD., Bry L., Li Z., Sacks DB. dsacks@rics.bwh.harvard.edu Accepted 2020-JAN-10 AT 15:49 GMT AT 15:49 GMT by LUANA The Journal of biological chemistry 2008 Only protein-protein interactions imex curation imex curation Actin pedestal formation by enteropathogenic Escherichia coli is regulated by IQGAP1, calcium, and calmodulin. Actin pedestal formation by enteropathogenic Escherichia coli is regulated by IQGAP1, calcium, and calmodulin. The Journal of biological chemistry 2008 imex curation Brown MD., Bry L., Li Z., Sacks DB. dsacks@rics.bwh.harvard.edu 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Brown MD., Bry L., Li Z., Sacks DB. dsacks@rics.bwh.harvard.edu Accepted 2020-JAN-10 AT 15:49 GMT AT 15:49 GMT by LUANA The Journal of biological chemistry 2008 Only protein-protein interactions imex curation imex curation 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 iqga1_human Ras GTPase-activating-like protein IQGAP1 IQGAP1 KIAA0051 p195 protein protein human Homo sapiens Human MSAADEVDGLGVARPHYGSVLDNERLTAEEMDERRRQNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNVIQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELEKYGIQMPAFSKIGGILANELSVDEAALHAAVIAINEAIDRRIPADTFAALKNPNAMLVNLEEPLASTYQDILYQAKQDKMTNAKNRTENSERERDVYEELLTQAEIQGNINKVNTFSALANIDLALEQGDALALFRALQSPALGLRGLQQQNSDWYLKQLLSDKQQKRQSGQTDPLQKEELQSGVDAANSAAQQYQRRLAAVALINAAIQKGVAEKTVLELMNPEAQLPQVYPFAADLYQKELATLQRQSPEHNLTHPELSVAVEMLSSVALINRALESGDVNTVWKQLSSSVTGLTNIEEENCQRYLDELMKLKAQAHAENNEFITWNDIQACVDHVNLVVQEEHERILAIGLINEALDEGDAQKTLQALQIPAAKLEGVLAEVAQHYQDTLIRAKREKAQEIQDESAVLWLDEIQGGIWQSNKDTQEAQKFALGIFAINEAVESGDVGKTLSALRSPDVGLYGVIPECGETYHSDLAEAKKKKLAVGDNNSKWVKHWVKGGYYYYHNLETQEGGWDEPPNFVQNSMQLSREEIQSSISGVTAAYNREQLWLANEGLITRLQARCRGYLVRQEFRSRMNFLKKQIPAITCIQSQWRGYKQKKAYQDRLAYLRSHKDEVVKIQSLARMHQARKRYRDRLQYFRDHINDIIKIQAFIRANKARDDYKTLINAEDPPMVVVRKFVHLLDQSDQDFQEELDLMKMREEVITLIRSNQQLENDLNLMDIKIGLLVKNKITLQDVVSHSKKLTKKNKEQLSDMMMINKQKGGLKALSKEKREKLEAYQHLFYLLQTNPTYLAKLIFQMPQNKSTKFMDSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVKTRLDSSIRNMRAVTDKFLSAIVSSVDKIPYGMRFIAKVLKDSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHNDPIHELLDDLGEVPTIESLIGESSGNLNDPNKEALAKTEVSLTLTNKFDVPGDENAEMDARTILLNTKRLIVDVIRFQPGETLTEILETPATSEQEAEHQRAMQRRAIRDAKTPDKMKKSKSVKEDSNLTLQEKKEKIQTGLKKLTELGTVDPKNKYQELINDIARDIRNQRRYRQRRKAELVKLQQTYAALNSKATFYGEQVDYYKSYIKTCLDNLASKGKVSKKPREMKGKKSKKISLKYTAARLHEKGVLLEIEDLQVNQFKNVIFEISPTEEVGDFEVKAKFMGVQMETFMLHYQDLLQLQYEGVAVMKLFDRAKVNVNLLIFLLNKKFYGK DIP protein P46940 original sequence version: 158 DIP protein P46940 original sequence version: 152 A52EC629596EAC33 cdc42_human Cell division control protein 42 homolog CDC42 G25K GTP-binding protein protein protein human Homo sapiens Human MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPPEPKKSRRCVLL 51A437E22A4D8FFF cdc42-iqgap1-8 1 4 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell 5 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization fig. 2 HeLa cells were fixed before and after infection with GFP EPEC (3 h) and stained for IQGAP1 (blue) and either Rac1 or Cdc42 (red) (Fig. 2). As described previously (20, 22), IQGAP1 colocalizes with both Rac1 and Cdc42 around the periphery of noninfected cells (Fig. 2). Neither Rac1 nor Cdc42 localizes at sites of EPEC adhesion (Fig. 2). iqgap1-rac1-3 1 4 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell 3 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization fig. 2 HeLa cells were fixed before and after infection with GFP EPEC (3 h) and stained for IQGAP1 (blue) and either Rac1 or Cdc42 (red) (Fig. 2). As described previously (20, 22), IQGAP1 colocalizes with both Rac1 and Cdc42 around the periphery of noninfected cells (Fig. 2). Neither Rac1 nor Cdc42 localizes at sites of EPEC adhesion (Fig. 2). iqgap1-cdc42-5 2 3 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level 4 unspecified role unspecified role bait bait physiological level physiological level endogenous level endogenous endogenous endogenous level 5 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level association association fug. 3a,b HeLa cells were infected with EPEC.