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/ Structural basis of membrane invagination by F-BAR domains. Structural basis of membrane invagination by F-BAR domains. Cell (0092-8674) 2008 imex curation Frost A., Perera R., Roux A., Spasov K., Destaing O., Egelman EH., De Camilli P., Unger VM. vinzenz.unger@yale.edu 25-Jun-2008: Contacted by JYOTI. davet Only protein-protein interactions 2 chlae-cos_7 Cercopithecus aethiops simian cells transformed with SV40 Grivet cos_7 cercopithecus aethiops, by transformation with SV40 fluorescence imaging fluorescence microscopy fluorescence imaging anti tag immunost anti tag immunostaining anti tag immunost Frost A., Perera R., Roux A., Spasov K., Destaing O., Egelman EH., De Camilli P., Unger VM. vinzenz.unger@yale.edu Accepted 2008-JUN-13 by DAVET. Cell (0092-8674) 2008 davet Only protein-protein interactions 2 imex curation Structural basis of membrane invagination by F-BAR domains. Structural basis of membrane invagination by F-BAR domains. Cell (0092-8674) 2008 imex curation Frost A., Perera R., Roux A., Spasov K., Destaing O., Egelman EH., De Camilli P., Unger VM. vinzenz.unger@yale.edu 25-Jun-2008: Contacted by JYOTI. davet Only protein-protein interactions 2 in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Frost A., Perera R., Roux A., Spasov K., Destaing O., Egelman EH., De Camilli P., Unger VM. Lipids were combined in mixtures composed of 85%/15% phospholipids/cholesterol (mol./mol.) to create liposomes, before adding F-BAR domains at a lipid-to-protein ratio of 2:1 mass/mass. vinzenz.unger@yale.edu Accepted 2008-JUN-13 by DAVET. 25-Jun-2008: Contacted by JYOTI. Cell (0092-8674) 2008 davet Only protein-protein interactions 2 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-fnbp1-1 1 3 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain region rfp tag red fluorescent protein tag red fluorescent protein RFP red fluorescent protein RFP rfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 4 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain region gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 7 10 colocalization colocalization namely CIP4/Toca-3 and FBP17/Toca-2, were coexpressed, they colocalized on the same tubules (Figure 1B). Figure 1B cip4-2 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 ecoli Escherichia coli (strain K12) direct interaction direct interaction Figure 2A, Supp Fig. 7 electron (cryo)micrograph of a nascent tubule generated in vitro by F-BAR domains (human CIP4, residues 1�284).