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/ Streptococcal protein FOG, a novel matrix adhesin interacting with collagen I in vivo. Streptococcal protein FOG, a novel matrix adhesin interacting with collagen I in vivo. J. Biol. Chem. (0021-9258) 2006 imex curation Nitsche DP., Johansson HM., Frick IM., Morgelin M. BioCreative - Critical Assessment of Information Extraction systems in Biology Human skin biopsies were extracted with SDS, separated by SDS-PAGE using bovine collagen I as a standard, and transferred to a PVDF membrane. Human skin biopsies were extracted with SDS, separated by SDS-PAGE using bovine collagen I as a standard, and transferred to a PVDF membrane. Radiolabeled FOG1-C bound only to a few discrete bands of the skin extract. Corresponding bands on the Coomassie-stained gel were excised, digested with trypsin, and analyzed by MALDI-TOF mass spectrometry. inga-maria.frick@med.lu.se 24-JAN-2007: Contacted by JYOTI. Only protein-protein interactions in vitro In vitro filter binding filter binding Filter overlay assay Filter overlay assay ms participant Identification by mass spectrometry ms participant Nitsche DP., Johansson HM., Frick IM., Morgelin M. BioCreative - Critical Assessment of Information Extraction systems in Biology Human skin biopsies were extracted with SDS, separated by SDS-PAGE using bovine collagen I as a standard, and transferred to a PVDF membrane. Human skin biopsies were extracted with SDS, separated by SDS-PAGE using bovine collagen I as a standard, and transferred to a PVDF membrane. Radiolabeled FOG1-C bound only to a few discrete bands of the skin extract. Corresponding bands on the Coomassie-stained gel were excised, digested with trypsin, and analyzed by MALDI-TOF mass spectrometry. inga-maria.frick@med.lu.se Accepted 2006-AUG-29 by JYOTI. J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation q5yb85_strsg protein protein strsg Streptococcus sp. group G RKLKKGTASVAVALTVLGAGLASHTEVKAAENTYDRWKAQTEEARTDKLIAGFANLDADVTNLGKMMDELQKLKDFSKQNNSIGEYARYLQKLNDQFQEYYEQVVGDDSRRVLAKELAKNTELNEKLSELSTTSQALAKELQEQKENYDLVKTVHADTVKKHQKLVDEITKKLGEEETERHSLQEELNKAQQELAQKQQELKDKQADYDLVVETHAYTVKEHQKLVDEITKKLGEEETERHSLQEELNKAQQELAQKQQELEAEKLAKEGIVDSLTAYVTEKEAEVKKLTDSLAAKDAEIQEKEAEKDRQQHMYEAFMSQLKEKVEKQEQELAKLKQLETINNNLLGNAKDMIAKLSAKNEQLASDKAKLEEQNKISDASRKGLRRDLNASREAKKQLEAEHQKLEEQNKISEASRKGLRRDLDASREAKKQVEKDLANLTAELDKVKEDKQISDASRKGLRRDLDASREAKKQVEKALEEANSKLAALEKLNKELEESKKLTEKEKAELQAKLEAEAKALKEKLAKQAEELAKLRAGKASDSQTPEATPGNKVVPGKGQASQAGTKPNQNKEPMKETKRQLPSTGEATNPFFTAAAL 2AB3B8D8BDE990BF co1a1_human Collagen alpha-1(I) chain Alpha-1 type I collagen COL1A1 protein protein human Homo sapiens Human MFSFVDLRLLLLLAATALLTHGQEEGQVEGQDEDIPPITCVQNGLRYHDRDVWKPEPCRICVCDNGKVLCDDVICDETKNCPGAEVPEGECCPVCPDGSESPTDQETTGVEGPKGDTGPRGPRGPAGPPGRDGIPGQPGLPGPPGPPGPPGPPGLGGNFAPQLSYGYDEKSTGGISVPGPMGPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGAPGPAGARGNDGATGAAGPPGPTGPAGPPGFPGAVGAKGEAGPQGPRGSEGPQGVRGEPGPPGPAGAAGPAGNPGADGQPGAKGANGAPGIAGAPGFPGARGPSGPQGPGGPPGPKGNSGEPGAPGSKGDTGAKGEPGPVGVQGPPGPAGEEGKRGARGEPGPTGLPGPPGERGGPGSRGFPGADGVAGPKGPAGERGSPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPPGPPGARGQAGVMGFPGPKGAAGEPGKAGERGVPGPPGAVGPAGKDGEAGAQGPPGPAGPAGERGEQGPAGSPGFQGLPGPAGPPGEAGKPGEQGVPGDLGAPGPSGARGERGFPGERGVQGPPGPAGPRGANGAPGNDGAKGDAGAPGAPGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGSPGKDGVRGLTGPIGPPGPAGAPGDKGESGPSGPAGPTGARGAPGDRGEPGPPGPAGFAGPPGADGQPGAKGEPGDAGAKGDAGPPGPAGPAGPPGPIGNVGAPGAKGARGSAGPPGATGFPGAAGRVGPPGPSGNAGPPGPPGPAGKEGGKGPRGETGPAGRPGEVGPPGPPGPAGEKGSPGADGPAGAPGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPGKQGPSGASGERGPPGPMGPPGLAGPPGESGREGAPGAEGSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKSGDRGETGPAGPTGPVGPVGARGPAGPQGPRGDKGETGEQGDRGIKGHRGFSGLQGPPGPPGSPGEQGPSGASGPAGPRGPPGSAGAPGKDGLNGLPGPIGPPGPRGRTGDAGPVGPPGPPGPPGPPGPPSAGFDFSFLPQPPQEKAHDGGRYYRADDANVVRDRDLEVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVFCNMETGETCVYPTQPSVAQKNWYISKNPKDKRHVWFGESMTDGFQFEYGGQGSDPADVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKALLLQGSNEIEIRAEGNSRFTYSVTVDGCTSHTGAWGKTVIEYKTTKTSRLPIIDVAPLDVGAPDQEFGFDVGPVCFL DIP protein P02452 original sequence version: 145 F0EC4DE778FFFC11 co1a2_human Collagen alpha-2(I) chain Alpha-2 type I collagen COL1A2 protein protein human Homo sapiens Human MLSFVDTRTLLLLAVTLCLATCQSLQEETVRKGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGNFAAQYDGKGVGLGPGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGAVGNAGPAGPAGPRGEVGLPGLSGPVGPPGNPGANGLTGAKGAAGLPGVAGAPGLPGPRGIPGPVGAAGATGARGLVGEPGPAGSKGESGNKGEPGSAGPQGPPGPSGEEGKRGPNGEAGSAGPPGPPGLRGSPGSRGLPGADGRAGVMGPPGSRGASGPAGVRGPNGDAGRPGEPGLMGPRGLPGSPGNIGPAGKEGPVGLPGIDGRPGPIGPAGARGEPGNIGFPGPKGPTGDPGKNGDKGHAGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPPGPPGFQGLPGPSGPAGEVGKPGERGLHGEFGLPGPAGPRGERGPPGESGAAGPTGPIGSRGPSGPPGPDGNKGEPGVVGAVGTAGPSGPSGLPGERGAAGIPGGKGEKGEPGLRGEIGNPGRDGARGAPGAVGAPGPAGATGDRGEAGAAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGAKGPKGENGVVGPTGPVGAAGPAGPNGPPGPAGSRGDGGPPGMTGFPGAAGRTGPPGPSGISGPPGPPGPAGKEGLRGPRGDQGPVGRTGEVGAVGPPGFAGEKGPSGEAGTAGPPGTPGPQGLLGAPGILGLPGSRGERGLPGVAGAVGEPGPLGIAGPPGARGPPGAVGSPGVNGAPGEAGRDGNPGNDGPPGRDGQPGHKGERGYPGNIGPVGAAGAPGPHGPVGPAGKHGNRGETGPSGPVGPAGAVGPRGPSGPQGIRGDKGEPGEKGPRGLPGLKGHNGLQGLPGIAGHHGDQGAPGSVGPAGPRGPAGPSGPAGKDGRTGHPGTVGPAGIRGPQGHQGPAGPPGPPGPPGPPGVSGGGYDFGYDGDFYRADQPRSAPSLRPKDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGETCIRAQPENIPAKNWYRSSKDKKHVWLGETINAGSQFEYNVEGVTSKEMATQLAFMRLLANYASQNITYHCKNSIAYMDEETGNLKKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTNEWGKTIIEYKTNKPSRLPFLDIAPLDIGGADQEFFVDIGPVCFK DIP protein P08123 original sequence version: 139 1E68A5970FB4210A q5yb85-col1a1 1 3 unspecified role unspecified role bait bait human-skin Homo sapiens skin skin 2 unspecified role unspecified role prey prey n-terminal gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region FOG1-C fragment sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region 125I radiolabelled radiolabelled radiolabel radiolabeled radiolabelled undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) physical association physical association The FOG 1-C fragment lacking the COOH-terminal membrane anchor domain was used to minimize potential self-aggregation by hydrophobic interactions. 2 A and Table 1 the combination of the MALDI-TOF fingerprint data and the migration pattern in SDS-PAGE (Fig. 2; for identification of the bands see Ref. 22) led to the assignment presented in Table 1, concluding that both collagen I -chains are targets for FOG. q5yb85-col1a2 1 2 unspecified role unspecified role prey prey region FOG1-C fragment sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region 125I radiolabelled radiolabelled radiolabel radiolabeled radiolabelled undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined n-terminal gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role bait bait human-skin Homo sapiens skin skin physical association physical association The FOG 1-C fragment lacking the COOH-terminal membrane anchor domain was used to minimize potential self-aggregation by hydrophobic interactions. 2 A and Table 1 the combination of the MALDI-TOF fingerprint data and the migration pattern in SDS-PAGE (Fig. 2; for identification of the bands see Ref. 22) led to the assignment presented in Table 1, concluding that both collagen I -chains are targets for FOG.