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/ http://www.ebi.ac.uk/ wines-2006-2 A competitive mechanism for staphylococcal toxin SSL7 inhibiting the leukocyte IgA receptor, Fc alphaRI, is revealed by SSL7 binding at the C alpha2/C alpha3 interface of IgA. in vitro In vitro facs fluorescence-activated cell sorting FACS Flow cytometry facs predetermined predetermined participant predetermined Wines BD., Willoughby N., Fraser JD., Hogarth PM. BioCreative - Critical Assessment of Information Extraction systems in Biology The sequence of this IgA1 Fc cDNA fragment differs from reference sequences (accession: NG_001019, six single nucleotide polymorphisms, BC092449, seven single nucleotide polymorphisms) resulting in two amino acid differences, L271M and R392H (standard IgA1 Bur numbering), consistent with the Dakiki IgA1 being a putative allelic variant. Here the sequence corresponding to the second accession number has been used as it is longer. This corresponds to a recent entry in Uniprot (Q569J1). The R392H corresponds to position 393 and the L271M to position 411. b.wines@ari.unimelb.edu.au J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation wines-2006-1 A competitive mechanism for staphylococcal toxin SSL7 inhibiting the leukocyte IgA receptor, Fc alphaRI, is revealed by SSL7 binding at the C alpha2/C alpha3 interface of IgA. in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Wines BD., Willoughby N., Fraser JD., Hogarth PM. BioCreative - Critical Assessment of Information Extraction systems in Biology The sequence of this IgA1 Fc cDNA fragment differs from reference sequences (accession: NG_001019, six single nucleotide polymorphisms, BC092449, seven single nucleotide polymorphisms) resulting in two amino acid differences, L271M and R392H (standard IgA1 Bur numbering), consistent with the Dakiki IgA1 being a putative allelic variant. Here the sequence corresponding to the second accession number has been used as it is longer. This corresponds to a recent entry in Uniprot (Q569J1). The R392H corresponds to position 393 and the L271M to position 411. b.wines@ari.unimelb.edu.au J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation q569j1_human IGHA1 protein protein human Homo sapiens Human MDTLCSTLLLLTIPSWVLSQITLKESGPALVKPTQTLTLTCTFSGFSLSSSGLSVGWIRQPPGKALEWLALIYWNDDKRHRPSLKSRLTITKDTSKNQVVLTMTNMDPVDTATYYCAHKYSGSWNAFDIWGQGTMVTVSSASPTSPKVFPLSLCSTQPDGNVVIACLVQGFFPQEPLSVTWSESGQGVTARNFPPSQDASGDLYTTSSQLTLPATQCLAGKSVTCHVKHYTNPSQDVTVPCPVPSTPPTPSPSTPPTPSPSCCHPRLSLHRPALEDLLLGSEANLTCTLTGLRDASGVTFTWTPSSGKSAVQGPPERDLCGCYSVSSVLPGCAEPWNHGKTFTCTAAYPESKTPLTATLSKSGNTFRPEVHLLPPPSEELALNELVTLTCLARGFSPKDVLVRWLQGSQELPREKYLTWASRQEPSQGTTTFAVTSILRVAAEDWKKGDTFSCMVGHEALPLAFTQKTIDRLAGKPTHVNVSVVMAEVDGTCY The sequence has been withdrawn from uniprot. q9zfs5_staau set1 NCTC7878_00468 FPP26_02075 protein protein staau Staphylococcus aureus MKLKTLAKATLALGLLTTGVITSEGQAVQAAEKQERVQHLHDIRDLHRYYSSESFEYSNVSGKVENYNGSNVVRFNPKDQNHQLFLLGKDKEQYKEGLQGQNVFVVQELIDPNGRLSTVGGVTKKNNKTSETNTPLFVNKVNGEDLDASIDSFLIQKEEISLKELDFKIRQQLVNNYGLYKGTSKYGKIIINLKDENKVEIDLGDKLQFERMGDVLNSKDIRGISVTINQI q8r3h6_mouse Ighg AU044919 protein protein mouse Mus musculus Mouse MEWPCILLFLLSVTEGVHSQVQLLQSGPELVKPGASVKISCRASGYAFSKSWMNWVKRRPGKGLEWIGRIFPGDGDTHYSGKFQGKAKLTADKSSVTAFLQLTSLTSEDSAVYFCARDSDYGDYFDDWGQGATVTVSSAKTTPPSVYPLAPGCGDTTGSSVTLGCLVKGYFPESVTVTWNSGSLSSSVHTFPALLQSGLYTMSSSVTVPSSTWPSQTVTCSVAHPASSTTVDKKLEPSGPISTINPCPPCKECHKCPAPNLEGGPSVFIFPPNIKDVLMISLTPKVTCVVVDVSEDDPDVQISWFVNNVEVHTAQTQTHREDYNSTIRVVSALPIQHQDWMSGKEFKCKVNNKDLPSPIERTISKIKGLVRAPQVYILPPPAEQLSRKDVSLTCLVVGFNPGDISVEWTSNGHTEENYKDTAPVLDSDGSYFIYSKLDIKTSKWEKTDSFSCNVRHEGLKNYYLKKTISRSPGK set1-igha1-1 503724 N/A 503726 unspecified role unspecified role bait bait ala463arg mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false leu278met,leu279ile mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false pro_leu_ala_phe461-464his_asn_his_tyr mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false region transferrin receptor-IgA Fc fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false N/A 503727 unspecified role unspecified role prey prey ecoli Escherichia coli (strain K12) physical association physical association false false false 2 B and D, 4 The igha1 protein was fused to the human transferrin receptor (TfR). For the IgA1 Fc sequence the authors state there are two differences in sequence and have mapped L271M against the sequence corresponding to NG_001019 and R392H against the sequence corresponding to BC092449, which is a longer sequence. The TfR-IgA Fc fusion protein was expressed in insect cells as a baculovirus expression vector was used. The Fc region of the human IgA1 derived from Dakiki cells was fused to the N-terminal region of the transferrin receptor which is a type II integral membrane protein. This fusion protein was expressed on the surface of CHOP cells (CHO cells expressing the early genes of the polyoma virus). igha1-ighg 503724 n/a 503728 unspecified role unspecified role prey prey region fused to FcalphaRI ectodomains fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false region Fc region of mouse IgG2b sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. N/A 503726 unspecified role unspecified role bait bait ala463arg mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false pro_leu_ala_phe461-464his_asn_his_tyr mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false leu278met,leu279ile mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false asn284thr mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false region transferrin receptor-IgA Fc fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false physical association physical association false false false 2 C and D, 4 For the IgA1 Fc sequence the authors state there are two differences in sequence and have mapped L271M against the sequence corresponding to NG_001019 and R392H against the sequence corresponding to BC092449, which is a longer sequence. The TfR-IgA Fc fusion protein was expressed in insect cells as a baculovirus expression vector was used. The Fc region of the human IgA1 derived from Dakiki cells was fused to the N-terminal region of the transferrin receptor which is a type II integral membrane protein. This fusion protein was expressed on the surface of CHOP cells (CHO cells expressing the early genes of the polyoma virus). set1-igha1 503725 N/A 503726 unspecified role unspecified role bait bait transferrin transferrin receptor-IgA Fc fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false N/A 503727 unspecified role unspecified role prey prey ecoli Escherichia coli (strain K12) physical association physical association false false false 1 KD 6.8 plus or minus 0.8 E-9 M The igha1 protein was fused to the human transferrin receptor (TfR). The TfR-IgA Fc fusion protein was expressed in insect cells as a baculovirus expression vector was used. For the IgA1 Fc sequence the authors state there are two differences in sequence and have mapped L271M against the sequence corresponding to NG_001019 and R392H against the sequence corresponding to BC092449, which is a longer sequence.