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 STIM1 couples to ORAI1 via an intramolecular transition into an extended conformation. STIM1 couples to ORAI1 via an intramolecular transition into an extended conformation. EMBO J. (0261-4189) 2011 imex curation Muik M., Fahrner M., Schindl R., Stathopulos P., Frischauf I., Derler I., Plenk P., Lackner B., Groschner K., Ikura M., Romanin C. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Muik M., Fahrner M., Schindl R., Stathopulos P., Frischauf I., Derler I., Plenk P., Lackner B., Groschner K., Ikura M., Romanin C. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation STIM1 couples to ORAI1 via an intramolecular transition into an extended conformation. STIM1 couples to ORAI1 via an intramolecular transition into an extended conformation. EMBO J. (0261-4189) 2011 imex curation Muik M., Fahrner M., Schindl R., Stathopulos P., Frischauf I., Derler I., Plenk P., Lackner B., Groschner K., Ikura M., Romanin C. Only protein-protein interactions human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. fluorescence imaging fluorescence microscopy fluorescence imaging tag fluorescence tag visualisation by fluorescence tag fluorescence Muik M., Fahrner M., Schindl R., Stathopulos P., Frischauf I., Derler I., Plenk P., Lackner B., Groschner K., Ikura M., Romanin C. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation STIM1 couples to ORAI1 via an intramolecular transition into an extended conformation. STIM1 couples to ORAI1 via an intramolecular transition into an extended conformation. EMBO J. (0261-4189) 2011 imex curation Muik M., Fahrner M., Schindl R., Stathopulos P., Frischauf I., Derler I., Plenk P., Lackner B., Groschner K., Ikura M., Romanin C. Only protein-protein interactions human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret tag fluorescence tag visualisation by fluorescence tag fluorescence Muik M., Fahrner M., Schindl R., Stathopulos P., Frischauf I., Derler I., Plenk P., Lackner B., Groschner K., Ikura M., Romanin C. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation crcm1_human Calcium release-activated calcium channel protein 1 ORAI1 CRACM1 TMEM142A Protein orai-1 Transmembrane protein 142A protein protein human Homo sapiens Human MHPEPAPPPSRSSPELPPSGGSTTSGSRRSRRRSGDGEPPGAPPPPPSAVTYPDWIGQSYSEVMSLNEHSMQALSWRKLYLSRAKLKASSRTSALLSGFAMVAMVEVQLDADHDYPPGLLIAFSACTTVLVAVHLFALMISTCILPNIEAVSNVHNLNSVKESPHERMHRHIELAWAFSTVIGTLLFLAEVVLLCWVKFLPLKKQPGQPRPTSKPPASGAAANVSTSGITPGQAAAIASTTIMVPFGLIFIVFAVHFYRSLVSHKTDRQFQELNELAEFARLQDQLDHRGDHPLTPGSHYA DIP protein Q96D31 original sequence version: 95 DIP protein Q96D31 original sequence version: 38 DIP protein Q96D31 original sequence version: 58 DIP protein Q96D31 original sequence version: 55 DIP protein Q96D31 original sequence version: 57 DIP protein Q96D31 original sequence version: 53 DIP protein Q96D31 original sequence version: 63 DIP protein Q96D31 original sequence version: 76 DIP protein Q96D31 original sequence version: 79 DIP protein Q96D31 original sequence version: 56 F85F7C06F36628D4 stim1_human Stromal interaction molecule 1 STIM1 GOK protein protein human Homo sapiens Human MDVCVRLALWLLWGLLLHQGQSLSHSHSEKATGTSSGANSEESTAAEFCRIDKPLCHSEDEKLSFEAVRNIHKLMDDDANGDVDVEESDEFLREDLNYHDPTVKHSTFHGEDKLISVEDLWKAWKSSEVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFGPPLLTRHNHLKDFMLVVSIVIGVGGCWFAYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQIEILCGFQIVNNPGIHSLVAALNIDPSWMGSTRPNPAHFIMTDDVDDMDEEIVSPLSMQSPSLQSSVRQRLTEPQHGLGSQRDLTHSDSESSLHMSDRQRVAPKPPQMSRAADEALNAMTSNGSHRLIEGVHPGSLVEKLPDSPALAKKALLALNHGLDKAHSLMELSPSAPPGGSPHLDSSRSHSPSSPDPDTPSPVGDSRALQASRNTRIPHLAGKKAVAEEDNGSIGEETDSSPGRKKFPLKIFKKPLKK DIP protein Q13586 original sequence version: 141 DIP protein Q13586 original sequence version: 99 DIP protein Q13586 original sequence version: 108 DIP protein Q13586 original sequence version: 121 DIP protein Q13586 original sequence version: 125 DIP protein Q13586 original sequence version: 100 FFB5E7CB3D68A7A6 stim1-1 1 STIM1 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 2.0 direct interaction direct interaction f4c mint orai1-stim1-9 2 STIM1 5 tag fluorescence tag visualisation by fluorescence tag fluorescence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 4 tag fluorescence tag visualisation by fluorescence tag fluorescence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell cfp tag cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined colocalization colocalization homomint mint f6 sf6 stim1-stim1 3 STIM1 5 tag fluorescence tag visualisation by fluorescence tag fluorescence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain yfp tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined STIM1 5 tag fluorescence tag visualisation by fluorescence tag fluorescence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain cfp tag cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined proximity proximity close-contact colocalization neighbourhood interaction sf2 homomint mint This decrease of FRET was not due to a diminished intermolecular FRET, as dimerization/ oligomerization of OASF when coupled to ORAI1 slightly enhances FRET as previously shown (Muik et al, 2009) for single-labelled and uniformly double-labelled constructs (Supplementary Figure S2A and B).