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 the 9-fold symmetry of centrioles. Structural basis of the 9-fold symmetry of centrioles. Cell (0092-8674) 2011 imex curation 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 26-Sep-2011: Contacted by JYOTI. mgt Only protein-protein interactions 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 Accepted 2011-APR-05 by MGT 26-Sep-2011: Contacted by JYOTI. Cell (0092-8674) 2011 mgt Only protein-protein interactions imex curation Structural basis of the 9-fold symmetry of centrioles. Structural basis of the 9-fold symmetry of centrioles. Cell (0092-8674) 2011 imex curation 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 26-Sep-2011: Contacted by JYOTI. mgt Only protein-protein interactions 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 Accepted 2011-APR-05 by MGT 26-Sep-2011: Contacted by JYOTI. Cell (0092-8674) 2011 mgt Only protein-protein interactions imex curation Structural basis of the 9-fold symmetry of centrioles. Structural basis of the 9-fold symmetry of centrioles. Cell (0092-8674) 2011 imex curation 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 26-Sep-2011: Contacted by JYOTI. mgt Only protein-protein interactions 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 Accepted 2011-APR-05 by MGT 26-Sep-2011: Contacted by JYOTI. Cell (0092-8674) 2011 mgt Only protein-protein interactions imex curation Structural basis of the 9-fold symmetry of centrioles. Structural basis of the 9-fold symmetry of centrioles. Cell (0092-8674) 2011 imex curation 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 26-Sep-2011: Contacted by JYOTI. mgt Only protein-protein interactions 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 Accepted 2011-APR-05 by MGT 26-Sep-2011: Contacted by JYOTI. Cell (0092-8674) 2011 mgt Only protein-protein interactions imex curation Structural basis of the 9-fold symmetry of centrioles. Structural basis of the 9-fold symmetry of centrioles. Cell (0092-8674) 2011 imex curation 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 26-Sep-2011: Contacted by JYOTI. mgt Only protein-protein interactions 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 Accepted 2011-APR-05 by MGT 26-Sep-2011: Contacted by JYOTI. Cell (0092-8674) 2011 mgt Only protein-protein interactions imex curation Structural basis of the 9-fold symmetry of centrioles. Structural basis of the 9-fold symmetry of centrioles. Cell (0092-8674) 2011 imex curation 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 26-Sep-2011: Contacted by JYOTI. mgt Only protein-protein interactions 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 Accepted 2011-APR-05 by MGT 26-Sep-2011: Contacted by JYOTI. Cell (0092-8674) 2011 mgt Only protein-protein interactions imex curation sas6_caeel Spindle assembly abnormal protein 6 sas-6 Y45F10D.9 protein protein caeel Caenorhabditis elegans MTSKIALFDQTLIASLLQPLSLNQPDFKAYKTKVKLKISEQRNETSGEKELKFEISRSDDFEFLFSETLNNEKYQILARDHDLTVDFDAFPKVIIQHLLCKNIVKNLEEDGEVDARKKAGYHSIADPGKPTEINIILDAEKNFCSFELFSKTPISKGKIFSIKLHAVRGDHLISHLLKICSSQAVKLSTFYKSADELASLRQKCGDLEKQVEKLSGVKEEFEEMSEKFKELEDEVELVKEERENIRLLVEDKEDEVADLKQDTESLQKQLEENQEELEIVGNMLREEQGKVDQLQKRNVAHQKEIGKLRAELGTAQRNLEKADQLLKRNSQQQNQQSLDMRKLGELEADLKEKDSMVESLTETIGILRKELENEKLKAAENMDSFEKLSMENENLKEKIAHYRAQRFSPAPSGLPGLQTGLTNRLTPSFKPVLGPHTPYGANLNSRTPFRDNTTLNFQNSTIATPHAFRFNSQLIADETTGSSVTNTPPAQR 118ED9B5EF6357A6 a9cql4_chlre CrSAS-6 CHLRE_12g516950v5 protein protein chlre Chlamydomonas reinhardtii Chlamydomonas smithii MPLLLDDGDPKAQTGFDLSTATTLFWRPVPVHVKQQDREDVLEELTFRILTGVAKQNHNLRILRIHISSDSDLFFLHTLEVSEEDFQSLKNDQGILVDFASFPGKIISLLEKCILAQPGDSPRFQAVLTIRGGESVFKIVEINDFKQLPHITLAFRPGNDSVVKQFLAFRLSEVKGTCHDLSDDLSRTRDDRDSMVAQLAQCRQQLAQLREQYDKHLLEVQAQAKTQQASAHEERIREKSQLKDQFEKERGEMEGRYRDQIAALNTRLGELDTENRKLREVKYELDTKVSELSHKLGSSEGSNRSLEEETARLRSLNQQLSSSKHELEIQLNEAKAKVLALDEKAQSQGDVIEQQRGRLRDMEAALRQTEQRCADLRDTLASAEGRAKEAQAEVLKGNQAIEKLTNDLRLAKEKTKRKAAIILRQEEELQEREQSLANATRDVGVLGQQAESLRKDVASLHSENDSLRSKLEDSKQQLQSNEQMIRWLNQQVTEAQLHASGATVAGSRYAFRPSAALPGSMPPPSVAATPAVGLLAAPGPSTAYKPGGTTSRYASTLGVTGLSSGLSGAGATSVGAAVAGGSYGAGGDSSYRPGVGGAYASSGGAGGFGGSVGGGGQVGGSGSAIGAATGAGSALGTYRSSYAASTHPSPGGVTAGMGSTLTTPAVNRYAAGSYSSVSSSLSFGGGLGAARAVDATPAASKYGVGFSNAAMGVVGTVGGAGGTDAQRA DIP protein A9CQL4 original sequence version: 30 55E067FF0454D96B sas6-4 6 7 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 ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 1E sas6-5 2 7 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 ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 1F pH 7.4, Temp=20C sas6-6 4 7 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 ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 1G sas6-7 3 7 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 S E Wed May 02 15:35:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser123glu' Tue Jun 30 19:34:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser123Glu' 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 ecoli Escherichia coli (strain K12) direct interaction direct interaction 2.1A Rworking = 21.01% Rfree = 25.74 % Supp. Table 1 sas6-8 5 7 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 ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 2E, S3A pH 7.0, Temp=7C sas6-9 1 7 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 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 I E Wed May 02 16:14:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile154glu' Tue Jun 30 16:29:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile154Glu' ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 2D, 2F pH 7.0, Temp=7C crsas 3 8 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 2.1A Rworking = 18.11% Rfree = 21.83 % Table S1 crsas-7 3 8 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 A9CQL4:p.Phe145Glu mutation mutation certain certain sequence position certain certain certain sequence position certain F E Wed May 02 20:26:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe145glu' Tue Jun 30 17:10:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe145Glu' ecoli Escherichia coli (strain K12) direct interaction direct interaction 3.02A Rworking = 19.56% Rfree = 22.85% Table S1 crsas-8 5 8 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 Supp. Fig. 4D