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/ Long-Pentraxin 3 Derivative as a Small-Molecule FGF Trap for Cancer Therapy. Long-Pentraxin 3 Derivative as a Small-Molecule FGF Trap for Cancer Therapy. Cancer cell 2015 imex curation Ronca R., Giacomini A., Di Salle E., Coltrini D., Pagano K., Ragona L., Matarazzo S., Rezzola S., Maiolo D., Torrella R., Moroni E., Mazzieri R., Escobar G., Mor M., Colombo G., Presta M. Cancer - Interactions investigated in the context of cancer The authors have stated that sFGFR1(IIIc)/Fc chimera was supplied from Reliatech;blasting the sequence shows the N-terminal FGFR1 part of this protein corresponds to Human FGFR1, P11362 (canonical isoform P11362-1) amino acids 22-376, the extra cellular domain, which has been entered here. The authors also state that FGF2 was “home made” (self produced) and the full length molecule of the 18kDa isoform of FGF2. This would correspond to FGF2 Isoform 3 (identifier: P09038-2) which is made up of 155 amino acids. marco.presta@unibs.it 22-Feb-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Ronca R., Giacomini A., Di Salle E., Coltrini D., Pagano K., Ragona L., Matarazzo S., Rezzola S., Maiolo D., Torrella R., Moroni E., Mazzieri R., Escobar G., Mor M., Colombo G., Presta M. Cancer - Interactions investigated in the context of cancer The authors have stated that sFGFR1(IIIc)/Fc chimera was supplied from Reliatech;blasting the sequence shows the N-terminal FGFR1 part of this protein corresponds to Human FGFR1, P11362 (canonical isoform P11362-1) amino acids 22-376, the extra cellular domain, which has been entered here. The authors also state that FGF2 was “home made” (self produced) and the full length molecule of the 18kDa isoform of FGF2. This would correspond to FGF2 Isoform 3 (identifier: P09038-2) which is made up of 155 amino acids. marco.presta@unibs.it Accepted 2016-JAN-27 AT 11:27 GMT AT 11:27 GMT by ORCHARD Cancer cell 2015 Only protein-protein interactions imex curation imex curation altered; done Long-Pentraxin 3 Derivative as a Small-Molecule FGF Trap for Cancer Therapy. Long-Pentraxin 3 Derivative as a Small-Molecule FGF Trap for Cancer Therapy. Cancer cell 2015 imex curation Ronca R., Giacomini A., Di Salle E., Coltrini D., Pagano K., Ragona L., Matarazzo S., Rezzola S., Maiolo D., Torrella R., Moroni E., Mazzieri R., Escobar G., Mor M., Colombo G., Presta M. Cancer - Interactions investigated in the context of cancer The authors have stated that sFGFR1(IIIc)/Fc chimera was supplied from Reliatech;blasting the sequence shows the N-terminal FGFR1 part of this protein corresponds to Human FGFR1, P11362 (canonical isoform P11362-1) amino acids 22-376, the extra cellular domain, which has been entered here. The authors also state that FGF2 was “home made” (self produced) and the full length molecule of the 18kDa isoform of FGF2. This would correspond to FGF2 Isoform 3 (identifier: P09038-2) which is made up of 155 amino acids. marco.presta@unibs.it 22-Feb-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro biosensor biosensor predetermined predetermined participant predetermined Ronca R., Giacomini A., Di Salle E., Coltrini D., Pagano K., Ragona L., Matarazzo S., Rezzola S., Maiolo D., Torrella R., Moroni E., Mazzieri R., Escobar G., Mor M., Colombo G., Presta M. Cancer - Interactions investigated in the context of cancer Is this going to need a new Interaction Detection Method? COntact Angle MOlecular REcognition (CONAMORE). Molecular interactions supported by a solid phase result in a shift in the solid-solution surface tension equilibrium, which can be tracked by the alteration of of the contact angle. Methodology is similar to SPR with one interactor immobilised on a chip and the alteration of contact angle monitored optically after addition of proposed interactor(s) in solution. The authors have stated that sFGFR1(IIIc)/Fc chimera was supplied from Reliatech;blasting the sequence shows the N-terminal FGFR1 part of this protein corresponds to Human FGFR1, P11362 (canonical isoform P11362-1) amino acids 22-376, the extra cellular domain, which has been entered here. The authors also state that FGF2 was “home made” (self produced) and the full length molecule of the 18kDa isoform of FGF2. This would correspond to FGF2 Isoform 3 (identifier: P09038-2) which is made up of 155 amino acids. marco.presta@unibs.it Accepted 2016-JAN-27 AT 11:27 GMT AT 11:27 GMT by ORCHARD Cancer cell 2015 Only protein-protein interactions imex curation imex curation altered; done Long-Pentraxin 3 Derivative as a Small-Molecule FGF Trap for Cancer Therapy. Long-Pentraxin 3 Derivative as a Small-Molecule FGF Trap for Cancer Therapy. Cancer cell 2015 imex curation Ronca R., Giacomini A., Di Salle E., Coltrini D., Pagano K., Ragona L., Matarazzo S., Rezzola S., Maiolo D., Torrella R., Moroni E., Mazzieri R., Escobar G., Mor M., Colombo G., Presta M. Cancer - Interactions investigated in the context of cancer The authors have stated that sFGFR1(IIIc)/Fc chimera was supplied from Reliatech;blasting the sequence shows the N-terminal FGFR1 part of this protein corresponds to Human FGFR1, P11362 (canonical isoform P11362-1) amino acids 22-376, the extra cellular domain, which has been entered here. The authors also state that FGF2 was “home made” (self produced) and the full length molecule of the 18kDa isoform of FGF2. This would correspond to FGF2 Isoform 3 (identifier: P09038-2) which is made up of 155 amino acids. marco.presta@unibs.it 22-Feb-2016: Contacted by IntAct-Help. 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 Ronca R., Giacomini A., Di Salle E., Coltrini D., Pagano K., Ragona L., Matarazzo S., Rezzola S., Maiolo D., Torrella R., Moroni E., Mazzieri R., Escobar G., Mor M., Colombo G., Presta M. Cancer - Interactions investigated in the context of cancer It is stated that all FGFs were obtained from Peprotech - however FGF3 and FGF22 could not be found on their website. The authors have stated that sFGFR1(IIIc)/Fc chimera was supplied from Reliatech;blasting the sequence shows the N-terminal FGFR1 part of this protein corresponds to Human FGFR1, P11362 (canonical isoform P11362-1) amino acids 22-376, the extra cellular domain, which has been entered here. The authors also state that FGF2 was “home made” (self produced) and the full length molecule of the 18kDa isoform of FGF2. This would correspond to FGF2 Isoform 3 (identifier: P09038-2) which is made up of 155 amino acids. marco.presta@unibs.it Accepted 2016-JAN-27 AT 11:27 GMT AT 11:27 GMT by ORCHARD Cancer cell 2015 Only protein-protein interactions imex curation imex curation altered; done fgfr2_human Fibroblast growth factor receptor 2 FGFR2 BEK KSAM Keratinocyte growth factor receptor KGFR K-sam protein protein human Homo sapiens Human MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGEYLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLPAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITTRLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT 6CD5001C960ED82F p09038-2 Fibroblast growth factor 2 FGF2 Basic fibroblast growth factor FGFB Heparin-binding growth factor 2 protein protein human Homo sapiens Human MAAGSITTLPALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS BE6CE13373007129 fgf3_human Fibroblast growth factor 3 FGF3 INT2 Heparin-binding growth factor 3 Proto-oncogene Int-2 protein protein human Homo sapiens Human MGLIWLLLLSLLEPGWPAAGPGARLRRDAGGRGGVYEHLGGAPRRRKLYCATKYHLQLHPSGRVNGSLENSAYSILEITAVEVGIVAIRGLFSGRYLAMNKRGRLYASEHYSAECEFVERIHELGYNTYASRLYRTVSSTPGARRQPSAERLWYVSVNGKGRPRRGFKTRRTQKSSLFLPRVLDHRDHEMVRQLQSGLPRPPGKGVQPRRRRQKQSPDNLEPSHVQASRLGSQLEASAH 8DBEF17D2B2E3C63 fgf20_human Fibroblast growth factor 20 FGF20 protein protein human Homo sapiens Human MAPLAEVGGFLGGLEGLGQQVGSHFLLPPAGERPPLLGERRSAAERSARGGPGAAQLAHLHGILRRRQLYCRTGFHLQILPDGSVQGTRQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSECIFREQFEENWYNTYSSNIYKHGDTGRRYFVALNKDGTPRDGARSKRHQKFTHFLPRPVDPERVPELYKDLLMYT AB04608C16060CC1 p08620-1 Fibroblast growth factor 4 FGF4 HST HSTF1 KS3 Heparin secretory-transforming protein 1 Heparin-binding growth factor 4 Transforming protein KS3 protein protein human Homo sapiens Human MSGPGTAAVALLPAVLLALLAPWAGRGGAAAPTAPNGTLEAELERRWESLVALSLARLPVAAQPKEAAVQSGAGDYLLGIKRLRRLYCNVGIGFHLQALPDGRIGGAHADTRDSLLELSPVERGVVSIFGVASRFFVAMSSKGKLYGSPFFTDECTFKEILLPNNYNAYESYKYPGMFIALSKNGKTKKGNRVSPTMKVTHFLPRL C7FD54A0272A1569 heparin Heparin small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) fgf2_human Fibroblast growth factor 2 Basic fibroblast growth factor FGF2 FGFB Heparin-binding growth factor 2 protein protein human Homo sapiens Human MVGVGGGDVEDVTPRPGGCQISGRGARGCNGIPGAAAWEAALPRRRPRRHPSVNPRSRAAGSPRTRGRRTEERPSGSRLGDRGRGRALPGGRLGGRGRGRAPERVGGRGRGRGTAAPRAAPAARGSRPGPAGTMAAGSITTLPALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS DIP protein P09038 original sequence version: 169 DIP protein P09038 original sequence version: 129 EAE98552A39D5E19 fgf6_human Fibroblast growth factor 6 FGF6 HST2 HSTF2 Heparin secretory-transforming protein 2 Heparin-binding growth factor 6 protein protein human Homo sapiens Human MALGQKLFITMSRGAGRLQGTLWALVFLGILVGMVVPSPAGTRANNTLLDSRGWGTLLSRSRAGLAGEIAGVNWESGYLVGIKRQRRLYCNVGIGFHLQVLPDGRISGTHEENPYSLLEISTVERGVVSLFGVRSALFVAMNSKGRLYATPSFQEECKFRETLLPNNYNAYESDLYQGTYIALSKYGRVKRGSKVSPIMTVTHFLPRI 79EF44685B324322 fgf16_human Fibroblast growth factor 16 FGF16 protein protein human Homo sapiens Human MAEVGGVFASLDWDLHGFSSSLGNVPLADSPGFLNERLGQIEGKLQRGSPTDFAHLKGILRRRQLYCRTGFHLEIFPNGTVHGTRHDHSRFGILEFISLAVGLISIRGVDSGLYLGMNERGELYGSKKLTRECVFREQFEENWYNTYASTLYKHSDSERQYYVALNKDGSPREGYRTKRHQKFTHFLPRPVDPSKLPSMSRDLFHYR D8AD160BDABDB5F8 fgf18_human Fibroblast growth factor 18 FGF18 zFGF5 UNQ420/PRO856 protein protein human Homo sapiens Human MYSAPSACTCLCLHFLLLCFQVQVLVAEENVDFRIHVENQTRARDDVSRKQLRLYQLYSRTSGKHIQVLGRRISARGEDGDKYAQLLVETDTFGSQVRIKGKETEFYLCMNRKGKLVGKPDGTSKECVFIEKVLENNYTALMSAKYSGWYVGFTKKGRPRKGPKTRENQQDVHFMKRYPKGQPELQKPFKYTTVTKRSRRIRPTHPA 57F69E7B30181500 fgfr1_human Fibroblast growth factor receptor 1 FGFR1 FGFBR FLG FLT2 Fms-like tyrosine kinase 2 Proto-oncogene c-Fgr BFGFR CEK HBGFR Basic fibroblast growth factor receptor 1 N-sam protein protein human Homo sapiens Human MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQDSVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHPAQLANGGLKRR DIP protein P11362 original sequence version: 154 DIP protein P11362 original sequence version: 160 DIP protein P11362 original sequence version: 180 DIP protein P11362 original sequence version: 170 93A01B5D78C3E72C nsc12 NSC12 small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) fgf22_human Fibroblast growth factor 22 FGF22 UNQ2500/PRO5800 protein protein human Homo sapiens Human MRRRLWLGLAWLLLARAPDAAGTPSASRGPRSYPHLEGDVRWRRLFSSTHFFLRVDPGGRVQGTRWRHGQDSILEIRSVHVGVVVIKAVSSGFYVAMNRRGRLYGSRLYTVDCRFRERIEENGHNTYASQRWRRRGQPMFLALDRRGGPRPGGRTRRYHLSAHFLPVLVS CB88918C2D5A4CE7 p55075-3 Fibroblast growth factor 8 FGF8 AIGF Androgen-induced growth factor Heparin-binding growth factor 8 protein protein human Homo sapiens Human MGSPRSALSCLLLHLLVLCLQAQVTVQSSPNFTQHVREQSLVTDQLSRRLIRTYQLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSRVRVRGAETGLYICMNKKGKLIAKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRLPRGHHTTEQSLRFEFLNYPPFTRSLRGSQRTWAPEPR A39424271EF7CBFF heparin-fgf2-2 3 5 unspecified role unspecified role prey prey 9 unspecified role unspecified role bait bait region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined direct interaction direct interaction 4C-1 CHEBI:90931 causes no change to the binding of CHEBI:28304 to P09038 fgfr1-fgf2-1 3 14 unspecified role unspecified role bait bait ecd sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain c_terminus fc-igg tag fc-igg tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. 10 unspecified role unspecified role prey prey direct interaction direct interaction 4C-1i fgfr1-fgf2-2 3 15 inhibitor inhibitor neutral component neutral component 14 unspecified role unspecified role bait bait ecd sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain c_terminus fc-igg tag fc-igg tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. 5 unspecified role unspecified role prey prey direct interaction direct interaction 4C-1ii NSC12 - CHEBI:90931 ID50 ~30 μM Fig 4C:I think the "ID50" is meant to be "IC50" but in case it is not, I have added as an annotation, not as a parameter. CHEBI:90931 decreases the binding of p11362 to P09038 fgf2-nsc12-1 3 5 unspecified role unspecified role bait bait 15 unspecified role unspecified role prey prey direct interaction direct interaction 4D fgf2-nsc12-2 2 15 unspecified role unspecified role prey prey 5 unspecified role unspecified role bait bait direct interaction direct interaction 4Dii No nanomechanical effect is seen when NSC12 is run onto a urea-denatured FGF2 chip. fgf3-nsc12-1 3 6 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 15 unspecified role unspecified role prey prey direct interaction direct interaction 4F-1 fgf4-nsc12-1 3 8 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 15 unspecified role unspecified role prey prey direct interaction direct interaction 4F-2 fgf6-nsc12-1 3 11 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 15 unspecified role unspecified role prey prey direct interaction direct interaction 4F-3 fgf8-nsc12-1 3 17 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 15 unspecified role unspecified role prey prey direct interaction direct interaction 4F-4 fgf16-nsc12-1 3 12 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 15 unspecified role unspecified role prey prey direct interaction direct interaction 4F-5 fgf18-nsc12-1 3 13 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 15 unspecified role unspecified role prey prey direct interaction direct interaction 4F-6 fgf20-nsc12-1 3 7 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 15 unspecified role unspecified role prey prey direct interaction direct interaction 4F-7 fgf20-nsc12-2 3 16 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 15 unspecified role unspecified role prey prey direct interaction direct interaction 4F-8 fgf2-fgfr2-4 1 5 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component d2_region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region 15n label 15n label 15N N15 15N N15 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 75 73 direct interaction direct interaction Supp 3B fgf2-fgfr2-7 1 15 inhibitor inhibitor neutral component neutral component 5 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component d2_region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region 15n label 15n label 15N N15 15N N15 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 82 80 direct interaction direct interaction Supp 3Bi NSC12 (CHEBI:90931) CHEBI:90931 decreases the binding between P09038 and P21802