IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Molecular basis for the impaired function of the natural F112L sorcin mutant: X-ray crystal structure, calcium affinity, and interaction with annexin VII and the ryanodine receptor. Molecular basis for the impaired function of the natural F112L sorcin mutant: X-ray crystal structure, calcium affinity, and interaction with annexin VII and the ryanodine receptor. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2008 imex curation Franceschini S., Ilari A., Verzili D., Zamparelli C., Antaramian A., Rueda A., Valdivia HH., Chiancone E., Colotti G. Cardiac - Interactions involving cardiac related proteins the PDBe entry has no mutation shown; email sent to them asking to reinstate mutations and querying if this was a mistake specific to this publication or an "improvement". gianni.colotti@uniroma1.it Only protein-protein interactions imex curation in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Franceschini S., Ilari A., Verzili D., Zamparelli C., Antaramian A., Rueda A., Valdivia HH., Chiancone E., Colotti G. Cardiac - Interactions involving cardiac related proteins the PDBe entry has no mutation shown; email sent to them asking to reinstate mutations and querying if this was a mistake specific to this publication or an "improvement". gianni.colotti@uniroma1.it Accepted 2015-MAY-15 by ORCHARD FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2008 Only protein-protein interactions imex curation imex curation Molecular basis for the impaired function of the natural F112L sorcin mutant: X-ray crystal structure, calcium affinity, and interaction with annexin VII and the ryanodine receptor. Molecular basis for the impaired function of the natural F112L sorcin mutant: X-ray crystal structure, calcium affinity, and interaction with annexin VII and the ryanodine receptor. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2008 imex curation Franceschini S., Ilari A., Verzili D., Zamparelli C., Antaramian A., Rueda A., Valdivia HH., Chiancone E., Colotti G. Cardiac - Interactions involving cardiac related proteins the PDBe entry has no mutation shown; email sent to them asking to reinstate mutations and querying if this was a mistake specific to this publication or an "improvement". gianni.colotti@uniroma1.it Only protein-protein interactions imex curation in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Franceschini S., Ilari A., Verzili D., Zamparelli C., Antaramian A., Rueda A., Valdivia HH., Chiancone E., Colotti G. Cardiac - Interactions involving cardiac related proteins the PDBe entry has no mutation shown; email sent to them asking to reinstate mutations and querying if this was a mistake specific to this publication or an "improvement". gianni.colotti@uniroma1.it Accepted 2015-MAY-15 by ORCHARD FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2008 Only protein-protein interactions imex curation imex curation Molecular basis for the impaired function of the natural F112L sorcin mutant: X-ray crystal structure, calcium affinity, and interaction with annexin VII and the ryanodine receptor. Molecular basis for the impaired function of the natural F112L sorcin mutant: X-ray crystal structure, calcium affinity, and interaction with annexin VII and the ryanodine receptor. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2008 imex curation Franceschini S., Ilari A., Verzili D., Zamparelli C., Antaramian A., Rueda A., Valdivia HH., Chiancone E., Colotti G. Cardiac - Interactions involving cardiac related proteins the PDBe entry has no mutation shown; email sent to them asking to reinstate mutations and querying if this was a mistake specific to this publication or an "improvement". gianni.colotti@uniroma1.it Only protein-protein interactions imex curation in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Franceschini S., Ilari A., Verzili D., Zamparelli C., Antaramian A., Rueda A., Valdivia HH., Chiancone E., Colotti G. Cardiac - Interactions involving cardiac related proteins the PDBe entry has no mutation shown; email sent to them asking to reinstate mutations and querying if this was a mistake specific to this publication or an "improvement". gianni.colotti@uniroma1.it Accepted 2015-MAY-15 by ORCHARD FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2008 Only protein-protein interactions imex curation imex curation Molecular basis for the impaired function of the natural F112L sorcin mutant: X-ray crystal structure, calcium affinity, and interaction with annexin VII and the ryanodine receptor. Molecular basis for the impaired function of the natural F112L sorcin mutant: X-ray crystal structure, calcium affinity, and interaction with annexin VII and the ryanodine receptor. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2008 imex curation Franceschini S., Ilari A., Verzili D., Zamparelli C., Antaramian A., Rueda A., Valdivia HH., Chiancone E., Colotti G. Cardiac - Interactions involving cardiac related proteins the PDBe entry has no mutation shown; email sent to them asking to reinstate mutations and querying if this was a mistake specific to this publication or an "improvement". gianni.colotti@uniroma1.it Only protein-protein interactions imex curation in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Franceschini S., Ilari A., Verzili D., Zamparelli C., Antaramian A., Rueda A., Valdivia HH., Chiancone E., Colotti G. Cardiac - Interactions involving cardiac related proteins the PDBe entry has no mutation shown; email sent to them asking to reinstate mutations and querying if this was a mistake specific to this publication or an "improvement". Spectrofluorimetric determination of the calcium ion affinity of wt- and F112L-sorcin using the fluorescent calcium chelator Fluo3;calcium binding to Fluo3 results in an increase in emission intensity. gianni.colotti@uniroma1.it Accepted 2015-MAY-15 by ORCHARD FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2008 Only protein-protein interactions imex curation imex curation calcium ion calcium ion calcium ion calcium ions small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) anxa7_human Annexin A7 ANXA7 ANX7 SNX Annexin-7 Annexin VII Synexin OK/SW-cl.95 protein protein human Homo sapiens Human MSYPGYPPTGYPPFPGYPPAGQESSFPPSGQYPYPSGFPPMGGGAYPQVPSSGYPGAGGYPAPGGYPAPGGYPGAPQPGGAPSYPGVPPGQGFGVPPGGAGFSGYPQPPSQSYGGGPAQVPLPGGFPGGQMPSQYPGGQPTYPSQINTDSFSSYPVFSPVSLDYSSEPATVTQVTQGTIRPAANFDAIRDAEILRKAMKGFGTDEQAIVDVVANRSNDQRQKIKAAFKTSYGKDLIKDLKSELSGNMEELILALFMPPTYYDAWSLRKAMQGAGTQERVLIEILCTRTNQEIREIVRCYQSEFGRDLEKDIRSDTSGHFERLLVSMCQGNRDENQSINHQMAQEDAQRLYQAGEGRLGTDESCFNMILATRSFPQLRATMEAYSRMANRDLLSSVSREFSGYVESGLKTILQCALNRPAFFAERLYYAMKGAGTDDSTLVRIVVTRSEIDLVQIKQMFAQMYQKTLGTMIAGDTSGDYRRLLLAIVGQ BFC688479D8CC2A0 p30626-1 Sorcin 22 kDa protein CP-22 V19 SRI protein protein human Homo sapiens Human MAYPGHPGAGGGYYPGGYGGAPGGPAFPGQTQDPLYGYFAAVAGQDGQIDADELQRCLTQSGIAGGYKPFNLETCRLMVSMLDRDMSGTMGFNEFKELWAVLNGWRQHFISFDTDRSGTVDPQELQKALTTMGFRLSPQAVNSIAKRYSTNGKITFDDYIACCVKLRALTDSFRRRDTAQQGVVNFPYDDFIQCVMSV DIP protein P30626-1 original sequence version: 174 A4829C7650A5E3FA sri-1 1 7 unspecified role unspecified role neutral component neutral component P30626-1:p.Phe112Leu mutation mutation certain certain sequence position certain certain certain sequence position certain F L Wed May 02 17:18:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe112leu' Wed May 02 17:47:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe112leu' Tue Jun 30 19:34:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe112Leu' ecoli Escherichia coli (strain K12) direct interaction direct interaction Table 1 2.5A R work 0.252 R free 0.289 sri-3 3 7 unspecified role unspecified role neutral component neutral component P30626-1:p.Phe112Leu mutation mutation certain certain sequence position certain certain certain sequence position certain F L Wed May 02 20:22:38 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe112leu' Tue Jun 30 19:17:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe112Leu' ecoli Escherichia coli (strain K12) direct interaction direct interaction Figure 6 sri-4 3 7 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction Figure 6i sri-5 4 7 unspecified role unspecified role neutral component neutral component P30626-1:p.Phe112Leu mutation mutation certain certain sequence position certain certain certain sequence position certain F L Wed May 02 16:46:30 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe112leu' Tue Jun 30 17:48:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe112Leu' ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role neutral component neutral component direct interaction direct interaction none- text between figs 6 and 7 The F112L mutation therefore results in a 5- to 6-fold decrease in the affinity for Ca2+. sri-6 4 5 unspecified role unspecified role neutral component neutral component 7 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction none- text between figs 6 and 7 The F112L mutation therefore results in a 5- to 6-fold decrease in the affinity for Ca2+. sri-7 2 7 unspecified role unspecified role prey prey P30626-1:p.Phe112Leu mutation mutation certain certain sequence position certain certain certain sequence position certain F L Wed May 02 18:01:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe112leu' Tue Jun 30 17:35:30 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe112Leu' ecoli Escherichia coli (strain K12) 6 unspecified role unspecified role bait bait N/A sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction Figure 7 By assuming that the sorcin dimer contains a single effective annexin VII binding site, the analysis yields KD values of 1.25 μM for wt-sorcin and 13.5 μM for F112L-sorcin. sri-8 2 6 unspecified role unspecified role bait bait N/A sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 7 unspecified role unspecified role prey prey ecoli Escherichia coli (strain K12) direct interaction direct interaction Figure 7 By assuming that the sorcin dimer contains a single effective annexin VII binding site, the analysis yields KD values of 1.25 μM for wt-sorcin and 13.5 μM for F112L-sorcin.