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/ kitagawa-2011-4 Structural basis of the 9-fold symmetry of centrioles. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Kitagawa D., Vakonakis I., Olieric N., Hilbert M., Keller D., Olieric V., Bortfeld M., Erat MC., Fluckiger I., Gonczy P., Steinmetz MO. pierre.gonczy@epfl.ch Cell (0092-8674) 2011 Only protein-protein interactions imex curation kitagawa-2011-5 Structural basis of the 9-fold symmetry of centrioles. in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Kitagawa D., Vakonakis I., Olieric N., Hilbert M., Keller D., Olieric V., Bortfeld M., Erat MC., Fluckiger I., Gonczy P., Steinmetz MO. pierre.gonczy@epfl.ch Cell (0092-8674) 2011 Only protein-protein interactions imex curation kitagawa-2011-1 Structural basis of the 9-fold symmetry of centrioles. in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Kitagawa D., Vakonakis I., Olieric N., Hilbert M., Keller D., Olieric V., Bortfeld M., Erat MC., Fluckiger I., Gonczy P., Steinmetz MO. pierre.gonczy@epfl.ch Cell (0092-8674) 2011 Only protein-protein interactions imex curation kitagawa-2011-2 Structural basis of the 9-fold symmetry of centrioles. in vitro In vitro cd circular dichroism CD CD cd predetermined predetermined participant predetermined Kitagawa D., Vakonakis I., Olieric N., Hilbert M., Keller D., Olieric V., Bortfeld M., Erat MC., Fluckiger I., Gonczy P., Steinmetz MO. pierre.gonczy@epfl.ch Cell (0092-8674) 2011 Only protein-protein interactions imex curation kitagawa-2011-3 Structural basis of the 9-fold symmetry of centrioles. in vitro In vitro comigration in sds comigration in sds page comigration in sds predetermined predetermined participant predetermined Kitagawa D., Vakonakis I., Olieric N., Hilbert M., Keller D., Olieric V., Bortfeld M., Erat MC., Fluckiger I., Gonczy P., Steinmetz MO. Gel migration performed under non-reducing conditions. pierre.gonczy@epfl.ch Cell (0092-8674) 2011 Only protein-protein interactions imex curation kitagawa-2011-6 Structural basis of the 9-fold symmetry of centrioles. in vitro In vitro density sedimentation cosedimentation through density gradient density sedimentation predetermined predetermined participant predetermined Kitagawa D., Vakonakis I., Olieric N., Hilbert M., Keller D., Olieric V., Bortfeld M., Erat MC., Fluckiger I., Gonczy P., Steinmetz MO. 1% glycerol pierre.gonczy@epfl.ch Cell (0092-8674) 2011 Only protein-protein interactions imex curation sas6_caeel Spindle assembly abnormal protein 6 sas-6 Y45F10D.9 protein protein caeel Caenorhabditis elegans MTSKIALFDQTLIASLLQPLSLNQPDFKAYKTKVKLKISEQRNETSGEKELKFEISRSDDFEFLFSETLNNEKYQILARDHDLTVDFDAFPKVIIQHLLCKNIVKNLEEDGEVDARKKAGYHSIADPGKPTEINIILDAEKNFCSFELFSKTPISKGKIFSIKLHAVRGDHLISHLLKICSSQAVKLSTFYKSADELASLRQKCGDLEKQVEKLSGVKEEFEEMSEKFKELEDEVELVKEERENIRLLVEDKEDEVADLKQDTESLQKQLEENQEELEIVGNMLREEQGKVDQLQKRNVAHQKEIGKLRAELGTAQRNLEKADQLLKRNSQQQNQQSLDMRKLGELEADLKEKDSMVESLTETIGILRKELENEKLKAAENMDSFEKLSMENENLKEKIAHYRAQRFSPAPSGLPGLQTGLTNRLTPSFKPVLGPHTPYGANLNSRTPFRDNTTLNFQNSTIATPHAFRFNSQLIADETTGSSVTNTPPAQR a9cql4_chlre CrSAS-6 CHLRE_12g516950v5 protein protein chlre Chlamydomonas reinhardtii Chlamydomonas smithii MPLLLDDGDPKAQTGFDLSTATTLFWRPVPVHVKQQDREDVLEELTFRILTGVAKQNHNLRILRIHISSDSDLFFLHTLEVSEEDFQSLKNDQGILVDFASFPGKIISLLEKCILAQPGDSPRFQAVLTIRGGESVFKIVEINDFKQLPHITLAFRPGNDSVVKQFLAFRLSEVKGTCHDLSDDLSRTRDDRDSMVAQLAQCRQQLAQLREQYDKHLLEVQAQAKTQQASAHEERIREKSQLKDQFEKERGEMEGRYRDQIAALNTRLGELDTENRKLREVKYELDTKVSELSHKLGSSEGSNRSLEEETARLRSLNQQLSSSKHELEIQLNEAKAKVLALDEKAQSQGDVIEQQRGRLRDMEAALRQTEQRCADLRDTLASAEGRAKEAQAEVLKGNQAIEKLTNDLRLAKEKTKRKAAIILRQEEELQEREQSLANATRDVGVLGQQAESLRKDVASLHSENDSLRSKLEDSKQQLQSNEQMIRWLNQQVTEAQLHASGATVAGSRYAFRPSAALPGSMPPPSVAATPAVGLLAAPGPSTAYKPGGTTSRYASTLGVTGLSSGLSGAGATSVGAAVAGGSYGAGGDSSYRPGVGGAYASSGGAGGFGGSVGGGGQVGGSGSAIGAATGAGSALGTYRSSYAASTHPSPGGVTAGMGSTLTTPAVNRYAAGSYSSVSSSLSFGGGLGAARAVDATPAASKYGVGFSNAAMGVVGTVGGAGGTDAQRA sas6-7 1130238 n/a 1130244 unspecified role unspecified role neutral component neutral component purified purified O62479:p.Ser123Glu mutation mutation certain certain sequence position certain certain certain sequence position certain false cen region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false 2.1A Rworking = 21.01% Rfree = 25.74 % Supp. Table 1 crsas 1130238 n/a 1130245 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 false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false 2.1A Rworking = 18.11% Rfree = 21.83 % Table S1 crsas-7 1130238 n/a 1130245 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 false A9CQL4:p.Phe145Glu mutation mutation certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false 3.02A Rworking = 19.56% Rfree = 22.85% Table S1 sas6-8 1130239 n/a 1130244 unspecified role unspecified role neutral component neutral component purified purified cen region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false 1130239 Fig. 2E, S3A pH 7.0, Temp=7C crsas-8 1130239 n/a 1130245 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 false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false 1130239 Supp. Fig. 4D sas6-4 1130240 n/a 1130244 unspecified role unspecified role neutral component neutral component purified purified cecc region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false Fig. 1E sas6-5 1130241 n/a 1130244 unspecified role unspecified role neutral component neutral component purified purified cecc region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false 1130241 Fig. 1F pH 7.4, Temp=20C sas6-6 1130242 n/a 1130244 unspecified role unspecified role neutral component neutral component purified purified cecc region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false Fig. 1G sas6-9 1130243 n/a 1130244 unspecified role unspecified role neutral component neutral component purified purified cen region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false O62479:p.Ile154Glu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false 1130243 Fig. 2D, 2F pH 7.0, Temp=7C