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/ tarabykina-2000-3 Heterocomplex formation between metastasis-related protein S100A4 (Mts1) and S100A1 as revealed by the yeast two-hybrid system. in vitro In vitro ion exchange chrom ion exchange chromatography IEC IEC ion exchange chrom predetermined predetermined participant predetermined Tarabykina S., Kriajevska M., Scott DJ., Hill TJ., Lafitte D., Derrick PJ., Dodson GG., Lukanidin E., Bronstein I. Cancer - Interactions investigated in the context of cancer svetlana@mcb.molbio.ku.dk A mouse mammary adenocarcinoma cDNA library was used. FEBS Lett. (0014-5793) 2000 tarabykina-2000-4 Heterocomplex formation between metastasis-related protein S100A4 (Mts1) and S100A1 as revealed by the yeast two-hybrid system. in vitro In vitro ms of complexes mass spectrometry studies of complexes ms of complexes predetermined predetermined participant predetermined Tarabykina S., Kriajevska M., Scott DJ., Hill TJ., Lafitte D., Derrick PJ., Dodson GG., Lukanidin E., Bronstein I. Cancer - Interactions investigated in the context of cancer For the electrospray ionization Fourier transform ion cyclotron resonance (ESI-FTICR) mass spectrometry, measurements were made using a FTICR mass spectrometer (Bruker Daltonics). svetlana@mcb.molbio.ku.dk A mouse mammary adenocarcinoma cDNA library was used. FEBS Lett. (0014-5793) 2000 tarabykina-2000-1 Heterocomplex formation between metastasis-related protein S100A4 (Mts1) and S100A1 as revealed by the yeast two-hybrid system. yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Tarabykina S., Kriajevska M., Scott DJ., Hill TJ., Lafitte D., Derrick PJ., Dodson GG., Lukanidin E., Bronstein I. Cancer - Interactions investigated in the context of cancer svetlana@mcb.molbio.ku.dk A mouse mammary adenocarcinoma cDNA library was used. FEBS Lett. (0014-5793) 2000 tarabykina-2000-2 Heterocomplex formation between metastasis-related protein S100A4 (Mts1) and S100A1 as revealed by the yeast two-hybrid system. yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Tarabykina S., Kriajevska M., Scott DJ., Hill TJ., Lafitte D., Derrick PJ., Dodson GG., Lukanidin E., Bronstein I. Cancer - Interactions investigated in the context of cancer svetlana@mcb.molbio.ku.dk A mouse mammary adenocarcinoma cDNA library was used. FEBS Lett. (0014-5793) 2000 tarabykina-2000-5 Heterocomplex formation between metastasis-related protein S100A4 (Mts1) and S100A1 as revealed by the yeast two-hybrid system. in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Tarabykina S., Kriajevska M., Scott DJ., Hill TJ., Lafitte D., Derrick PJ., Dodson GG., Lukanidin E., Bronstein I. Cancer - Interactions investigated in the context of cancer The presence of the unique tryptophan residue (W90) in the C-terminus of S100A1 allowed use of fluorescence spectrometry to monitor the S100A1^S100A4 interaction by changes in tryptophan fluorescence. svetlana@mcb.molbio.ku.dk A mouse mammary adenocarcinoma cDNA library was used. FEBS Lett. (0014-5793) 2000 s10a4_mouse Protein S100-A4 S100a4 Capl Mts1 S100 calcium-binding protein A4 Metastasin Protein Mts1 Metastatic cell protein Placental calcium-binding protein Protein 18A2 PEL98 protein protein mouse Mus musculus Mouse MARPLEEALDVIVSTFHKYSGKEGDKFKLNKTELKELLTRELPSFLGKRTDEAAFQKVMSNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGCPDKEPRKK s10a1_mouse Protein S100-A1 S100a1 S-100 protein subunit alpha S-100 protein alpha chain S100 calcium-binding protein A1 protein protein mouse Mus musculus Mouse MGSELESAMETLINVFHAHSGQEGDKYKLSKKELKDLLQTELSGFLDVQKDADAVDKVMKELDENGDGEVDFKEYVVLVAALTVACNNFFWETS s100a4-s100a4-2 Anion-exchange chromatography shows S100A4 forms homodimers 671937 N/A 671942 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) N/A 671942 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) physical association physical association false false false 1 A s100a1-s100a4-1 Anion-exchange chromatography shows S100A4 forms dimers with S100A1 671937 N/A 671942 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) N/A 671943 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) physical association physical association false false false 1 A s100a1-s100a1-6 Anion-exchange chromatography shows S100A1 forms homodimers 671937 N/A 671942 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) N/A 671943 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) physical association physical association false false false 1 A s100a1-s100a4-2 S100A4 and S100A1 form a heterodimeric complex as shown by ESI-FTICR mass spectrometry 671938 N/A 671943 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 1.0 N/A 671942 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 1.0 direct interaction direct interaction false false false MW = 24 982.00 Da 2 s100a4-s100a4-3 S100A4 forms a homodimeric complex as shown by ESI-FTICR mass spectrometry 671938 N/A 671942 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false 2 s100a1-s100a1-7 S100A1 forms a homodimeric complex as shown by ESI-FTICR mass spectrometry 671938 N/A 671943 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false 2 s100a4-s100a4 S100A4 forms homodimers in a yeast two-hybrid assay 671939 N/A 671942 unspecified role unspecified role bait bait N/A 671942 unspecified role unspecified role prey prey physical association physical association false false false s100a4-s100a1-2 S100A4 interacts with S100A1 in a yeast two-hybrid assay 671939 N/A 671942 unspecified role unspecified role bait bait N/A 671943 unspecified role unspecified role prey prey physical association physical association false false false s100a4-s100a1 S100A4 interacts with S100A1 in a yeast two-hybrid assay 671940 N/A 671943 unspecified role unspecified role prey prey N/A 671942 unspecified role unspecified role bait bait P07091:p.Phe72Ala mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false P07091:p.[Cys76Ser;Cys81Ser;Cys86Ser;Cys93Ser] mutation disrupting mutation disrupting interaction mutation disrupting 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 certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false P07091:p.[Cys76Ser;Cys81Ser] mutation disrupting mutation disrupting interaction mutation disrupting 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 P07091:p.Cys76Ser mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false leu79 binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false physical association physical association false false false Table 1 s100a4-s100a4-1 S100A4 forms homodimers in a yeast two-hybrid assay 671940 N/A 671942 unspecified role unspecified role prey prey N/A 671942 unspecified role unspecified role bait bait P07091:p.Phe72Ala mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false leu79 binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false physical association physical association false false false Table 1 s100a1-s100a4-3 S1004A and S100A1 form a complex as shown by fluorescence spectrometry 671941 N/A 671942 unspecified role unspecified role prey prey ecoli Escherichia coli (strain K12) N/A 671943 unspecified role unspecified role bait bait ecoli Escherichia coli (strain K12) physical association physical association false false false 3 The results indicate that this complex forms in the presence and in the absence of calcium, suggesting that the mechanism of the S100A4/ S100A1 heterodimerization could be di�erent from that of the homodimerization of S100A4.