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/ Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis. Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis. Cell (0092-8674) 2007 imex curation Shimada A., Niwa H., Tsujita K., Suetsugu S., Nitta K., Hanawa-Suetsugu K., Akasaka R., Nishino Y., Toyama M., Chen L., Liu ZJ., Wang BC., Yamamoto M., Terada T., Miyazawa A., Tanaka A., Sugano S., Shirouzu M., Nagayama K., Takenawa T., Yokoyama S. takenawa@med.kobe-u.ac.jp,yokoyama@biochem.s.u-tokyo.ac.jp 07-Aug-2007: Contacted by JYOTI. davet Only protein-protein interactions 4 in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Shimada A., Niwa H., Tsujita K., Suetsugu S., Nitta K., Hanawa-Suetsugu K., Akasaka R., Nishino Y., Toyama M., Chen L., Liu ZJ., Wang BC., Yamamoto M., Terada T., Miyazawa A., Tanaka A., Sugano S., Shirouzu M., Nagayama K., Takenawa T., Yokoyama S. takenawa@med.kobe-u.ac.jp,yokoyama@biochem.s.u-tokyo.ac.jp Accepted 2007-AUG-9 by DAVET. 07-Aug-2007: Contacted by JYOTI. Cell (0092-8674) 2007 davet Only protein-protein interactions 4 imex curation Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis. Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis. Cell (0092-8674) 2007 imex curation Shimada A., Niwa H., Tsujita K., Suetsugu S., Nitta K., Hanawa-Suetsugu K., Akasaka R., Nishino Y., Toyama M., Chen L., Liu ZJ., Wang BC., Yamamoto M., Terada T., Miyazawa A., Tanaka A., Sugano S., Shirouzu M., Nagayama K., Takenawa T., Yokoyama S. takenawa@med.kobe-u.ac.jp,yokoyama@biochem.s.u-tokyo.ac.jp 07-Aug-2007: Contacted by JYOTI. davet Only protein-protein interactions 4 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Shimada A., Niwa H., Tsujita K., Suetsugu S., Nitta K., Hanawa-Suetsugu K., Akasaka R., Nishino Y., Toyama M., Chen L., Liu ZJ., Wang BC., Yamamoto M., Terada T., Miyazawa A., Tanaka A., Sugano S., Shirouzu M., Nagayama K., Takenawa T., Yokoyama S. takenawa@med.kobe-u.ac.jp,yokoyama@biochem.s.u-tokyo.ac.jp Accepted 2007-AUG-9 by DAVET. Cell (0092-8674) 2007 davet Only protein-protein interactions 4 imex curation fnbp1_human Formin-binding protein 1 FNBP1 FBP17 Formin-binding protein 17 KIAA0554 protein protein human Homo sapiens Human MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCKAFISNLNEMNDYAGQHEVISENMASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRHQMAEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQEMEERRIVRMGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVIEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSNSRGEGKPDLKFGGKSKGKLWPFIKKNKLMSLLTSPHQPPPPPPASASPSAVPNGPQSPKQQKEPLSHRFNEFMTSKPKIHCFRSLKRGLSLKLGATPEDFSNLPPEQRRKKLQQKVDELNKEIQKEMDQRDAITKMKDVYLKNPQMGDPASLDHKLAEVSQNIEKLRVETQKFEAWLAEVEGRLPARSEQARRQSGLYDSQNPPTVNNCAQDRESPDGSYTEEQSQESEMKVLATDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLYVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVCLDKNAKDS DIP protein Q96RU3 original sequence version: 122 F06E847C6E631EC3 cip4_human Cdc42-interacting protein 4 TRIP10 CIP4 Thyroid receptor-interacting protein 10 Protein Felic Salt tolerant protein STOT STP protein protein human Homo sapiens Human MDWGTELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESKFSQQQSFVQILQEVNDFAGQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELEVVPIIAKCLEGMKVAANAVDPKNDSHVLIELHKSGFARPGDVEFEDFSQPMNRAPSDSSLGTPSDGRPELRGPGRSRTKRWPFGKKNKPRPPPLSPLGGPVPSALPNGPPSPRSGRDPLAILSEISKSVKPRLASFRSLRGSRGTVVTEDFSHLPPEQQRKRLQQQLEERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESRVLSNRGDSLSRHARPPDPPASAPPDSSSNSASQDTKESSEEPPSEESQDTPIYTEFDEDFEEEPTSPIGHCVAIYHFEGSSEGTISMAEGEDLSLMEEDKGDGWTRVRRKEGGEGYVPTSYLRVTLN A9BFE85520C7ABC5 A9BFE85520C7ABC5 cip4 2 4 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 in vitro In vitro direct interaction direct interaction Table 1, Figure 1 working 22.8 percent, free 27.9 percent 2.30 A EFC NCIP4 residues 10 to 303, was expressed at the highest level and yielded crystals suitable for structure determination. fnbp1 2 3 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) direct interaction direct interaction working 21.2%, free 26.7% 2.61 Table 1, Figure 1 the crystals of a human FBP17 fragment, EFCFBP17 residues 1 to 300, were obtained and the crystal structure was determined by the molecular replacement method, using the structure of EFCΔNCIP4 as a search model. cip4-1 1 4 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 in vitro In vitro direct interaction direct interaction Figure S4 To confirm that the EFC domain exists as a dimer in solution, we measured the molar masses of the EFC-domain fragments by analytical ultracentrifugation Figure S4. Sedimentation equilibrium analyses of EFCFBP17 and EFCCIP4 yielded molecular masses of 71.5 and 72.1 kDa 72.1 kDa fnbp1-1 1 3 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) direct interaction direct interaction S4 To confirm that the EFC domain exists as a dimer in solution, we measured the molar masses of the EFC-domain fragments by analytical ultracentrifugation (Figure S4). Sedimentation equilibrium analyses of EFCFBP17 and EFCCIP4 yielded molecular masses of 71.5 and 72.1 kDa 71 kDa complex observed