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/ Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3. Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3. J. Biol. Chem. (0021-9258) 1995 imex curation Horan T., Wen J., Arakawa T., Liu N., Brankow D., Hu S., Ratzkin B., Philo JS. The purification of the proteins detected by silver-staining described in PMID: 7929212, 7876251 orchard Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Horan T., Wen J., Arakawa T., Liu N., Brankow D., Hu S., Ratzkin B., Philo JS. The purification of the proteins detected by silver-staining described in PMID: 7929212, 7876251 Accepted 2010-FEB-4 by ORCHARD. J. Biol. Chem. (0021-9258) 1995 orchard Only protein-protein interactions imex curation Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3. Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3. J. Biol. Chem. (0021-9258) 1995 imex curation Horan T., Wen J., Arakawa T., Liu N., Brankow D., Hu S., Ratzkin B., Philo JS. The purification of the proteins detected by silver-staining described in PMID: 7929212, 7876251 orchard Only protein-protein interactions in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Horan T., Wen J., Arakawa T., Liu N., Brankow D., Hu S., Ratzkin B., Philo JS. Size exclusion chromatography with on-line light scattering, refractive index used. Superose 12 columns used. The purification of the proteins detected by silver-staining described in PMID: 7929212, 7876251 Accepted 2010-FEB-4 by ORCHARD. J. Biol. Chem. (0021-9258) 1995 orchard Only protein-protein interactions imex curation Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3. Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3. J. Biol. Chem. (0021-9258) 1995 imex curation Horan T., Wen J., Arakawa T., Liu N., Brankow D., Hu S., Ratzkin B., Philo JS. The purification of the proteins detected by silver-staining described in PMID: 7929212, 7876251 orchard Only protein-protein interactions in vitro In vitro comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel weight silver stain molecular weight estimation by silver staining weight silver stain Horan T., Wen J., Arakawa T., Liu N., Brankow D., Hu S., Ratzkin B., Philo JS. The purification of the proteins detected by silver-staining described in PMID: 7929212, 7876251 Accepted 2010-FEB-4 by ORCHARD. J. Biol. Chem. (0021-9258) 1995 orchard Only protein-protein interactions imex curation q02297-7 Pro-neuregulin-1, membrane-bound isoform NRG1 GGF HGL HRGA NDF SMDF Beta2 protein protein human Homo sapiens Human MSERKEGRGKGKGKKKERGSGKKPESAAGSQSPALPPRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDSASANITIVESNEIITGMPASTEGAYVSSESPIRISVSTEGANTSSSTSTSTTGTSHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCPNEFTGDRCQNYVMASFYKAEELYQKRVLTITGICIALLVVGIMCVVAYCKTKKQRKKLHDRLRQSLRSERNNMMNIANGPHHPNPPPENVQLVNQYVSKNVISSEHIVEREAETSFSTSHYTSTAHHSTTVTQTPSHSWSNGHTESILSESHSVIVMSSVENSRHSSPTGGPRGRLNGTGGPRECNSFLRHARETPDSYRDSPHSERYVSAMTTPARMSPVDFHTPSSPKSPPSEMSPPVSSMTVSMPSMAVSPFMEEERPLLLVTPPRLREKKFDHHPQQFSSFHHNPAHDSNSLPASPLRIVEDEEYETTQEYEPAQEPVKKLANSRRAKRTKPNGHIANRLEVDSNTSSQSSNSESETEDERVGEDTPFLGIQNPLAASLEATPAFRLADSRTNPAGRFSTQEEIQARLSSVIANQDPIAV D92B25445628869D q02297-3 Pro-neuregulin-1, membrane-bound isoform NRG1 GGF HGL HRGA NDF SMDF Alpha2B protein protein human Homo sapiens Human MSERKEGRGKGKGKKKERGSGKKPESAAGSQSPALPPRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDSASANITIVESNEIITGMPASTEGAYVSSESPIRISVSTEGANTSSSTSTSTTGTSHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCQPGFTGARCTENVPMKVQNQEKAEELYQKRVLTITGICIALLVVGIMCVVAYCKTKKQRKKLHDRLRQSLRSERNNMMNIANGPHHPNPPPENVQLVNQYVSKNVISSEHIVEREAETSFSTSHYTSTAHHSTTVTQTPSHSWSNGHTESILSESHSVIVMSSVENSRHSSPTGGPRGRLNGTGGPRECNSFLRHARETPDSYRDSPHSERHNLIAELRRNKAHRSKCMQIQLSATHLRSSSIPHLGFIL 00F513509DED3269 erbb2_human Receptor tyrosine-protein kinase erbB-2 p185erbB2 MLN19 Proto-oncogene c-ErbB-2 Tyrosine kinase-type cell surface receptor HER2 Proto-oncogene Neu ERBB2 HER2 NEU NGL Metastatic lymph node gene 19 protein protein protein human Homo sapiens Human MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV DIP protein P04626 original sequence version: 198 DIP protein P04626 original sequence version: 122 DIP protein P04626 original sequence version: 206 DIP protein P04626 original sequence version: 195 DIP protein P04626 original sequence version: 150 DIP protein P04626 original sequence version: 179 DIP protein P04626 original sequence version: 146 DIP protein P04626 original sequence version: 147 39E9DFDA04DCF962 erbb3_human Receptor tyrosine-protein kinase erbB-3 Tyrosine kinase-type cell surface receptor HER3 ERBB3 HER3 Proto-oncogene-like protein c-ErbB-3 protein protein human Homo sapiens Human MRANDALQVLGLLFSLARGSEVGNSQAVCPGTLNGLSVTGDAENQYQTLYKLYERCEVVMGNLEIVLTGHNADLSFLQWIREVTGYVLVAMNEFSTLPLPNLRVVRGTQVYDGKFAIFVMLNYNTNSSHALRQLRLTQLTEILSGGVYIEKNDKLCHMDTIDWRDIVRDRDAEIVVKDNGRSCPPCHEVCKGRCWGPGSEDCQTLTKTICAPQCNGHCFGPNPNQCCHDECAGGCSGPQDTDCFACRHFNDSGACVPRCPQPLVYNKLTFQLEPNPHTKYQYGGVCVASCPHNFVVDQTSCVRACPPDKMEVDKNGLKMCEPCGGLCPKACEGTGSGSRFQTVDSSNIDGFVNCTKILGNLDFLITGLNGDPWHKIPALDPEKLNVFRTVREITGYLNIQSWPPHMHNFSVFSNLTTIGGRSLYNRGFSLLIMKNLNVTSLGFRSLKEISAGRIYISANRQLCYHHSLNWTKVLRGPTEERLDIKHNRPRRDCVAEGKVCDPLCSSGGCWGPGPGQCLSCRNYSRGGVCVTHCNFLNGEPREFAHEAECFSCHPECQPMEGTATCNGSGSDTCAQCAHFRDGPHCVSSCPHGVLGAKGPIYKYPDVQNECRPCHENCTQGCKGPELQDCLGQTLVLIGKTHLTMALTVIAGLVVIFMMLGGTFLYWRGRRIQNKRAMRRYLERGESIEPLDPSEKANKVLARIFKETELRKLKVLGSGVFGTVHKGVWIPEGESIKIPVCIKVIEDKSGRQSFQAVTDHMLAIGSLDHAHIVRLLGLCPGSSLQLVTQYLPLGSLLDHVRQHRGALGPQLLLNWGVQIAKGMYYLEEHGMVHRNLAARNVLLKSPSQVQVADFGVADLLPPDDKQLLYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWELMTFGAEPYAGLRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMARDPPRYLVIKRESGPGIAPGPEPHGLTNKKLEEVELEPELDLDLDLEAEEDNLATTTLGSALSLPVGTLNRPRGSQSLLSPSSGYMPMNQGNLGESCQESAVSGSSERCPRPVSLHPMPRGCLASESSEGHVTGSEAELQEKVSMCRSRSRSRSPRPRGDSAYHSQRHSLLTPVTPLSPPGLEEEDVNGYVMPDTHLKGTPSSREGTLSSVGLSSVLGTEEEDEDEEYEYMNRRRRHSPPHPPRPSSLEELGYEYMDVGSDLSASLGSTQSCPLHPVPIMPTAGTTPDEDYEYMNRQRDGGGPGGDYAAMGACPASEQGYEEMRAFQGPGHQAPHVHYARLKTLRSLEATDSAFDNPDYWHSRLFPKANAQRT DIP protein P21860 original sequence version: 175 DIP protein P21860 original sequence version: 125 DIP protein P21860 original sequence version: 172 DIP protein P21860 original sequence version: 130 DIP protein P21860 original sequence version: 157 DIP protein P21860 original sequence version: 137 7201E7F66CA374BD ndfb2-her3 3 4 unspecified role unspecified role unspecified role unspecified role ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role unspecified role unspecified role ecoli Escherichia coli (strain K12) direct interaction direct interaction 1 Here again, complex formation was observed only when NDFbeta2 was mixed with sHer3. ndfa2-her3 3 7 unspecified role unspecified role unspecified role unspecified role ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role unspecified role unspecified role ecoli Escherichia coli (strain K12) direct interaction direct interaction 1 In the presence of 6.8- (lane 4) or 1.7-fold (lane 8) molar excess of NDFα2, sHer3 displayed a new band slightly above the free molecules, indicating formation of a complex. ndfb2-her3-1 2 7 unspecified role unspecified role unspecified role unspecified role ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role unspecified role unspecified role ecoli Escherichia coli (strain K12) direct interaction direct interaction 2 When sHer3 was mixed with NDFβ2 at an 1:1 molar ratio, much of the NDFβ2 eluted as a complex with sHer3 Mol. weight of complex = 80,000 Da ndfb2-her3-2 1 4 unspecified role unspecified role unspecified role unspecified role ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role unspecified role unspecified role ecoli Escherichia coli (strain K12) direct interaction direct interaction 2 sHer3 and NDF bind to form 1:1 complexes gives a good fit to all the data, with nearly randomly distributed residuals, as shown in�Fig. 3, and returns a dissociation constant of 26 nM. ndfb2-her2 1 6 unspecified role unspecified role unspecified role unspecified role ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role unspecified role unspecified role ecoli Escherichia coli (strain K12) direct interaction direct interaction Figs. 2 and 3 Similar sedimentation equilibrium studies were also carried out with sHer2 and NDF. Simultaneous analysis of 18 data sets gave a reasonably good fit to the 1:1 stoichiometry model with a dissociation constant of 19.6 μM� ndfb2-her2-1 1 4 unspecified role unspecified role unspecified role unspecified role ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role unspecified role unspecified role ecoli Escherichia coli (strain K12) 6 unspecified role unspecified role unspecified role unspecified role ecoli Escherichia coli (strain K12) direct interaction direct interaction 4, 5 Instead, the binding of sHer2 actually appears to be weaker in the presence of sHer3, perhaps as a result of some overlap of their binding sites on NDF, or steric interference between the 2 receptors, or some negative cooperativity through the common ligand. Weak ternary complex observed.