DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structure (London, England : 1993) 2013 imex curation Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. DIP original experiment: DIP-255858X Structure (London, England : 1993) 2013 IMEx Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structure (London, England : 1993) 2013 imex curation Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. DIP original experiment: DIP-255862X Structure (London, England : 1993) 2013 IMEx Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structure (London, England : 1993) 2013 imex curation Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. DIP original experiment: DIP-255857X Structure (London, England : 1993) 2013 IMEx Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structure (London, England : 1993) 2013 imex curation Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. Only protein-protein interactions in vitro In vitro dls dynamic light scattering dls predetermined predetermined participant predetermined Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. DIP original experiment: DIP-255859X Structure (London, England : 1993) 2013 IMEx Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structure (London, England : 1993) 2013 imex curation Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. 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 Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. DIP original experiment: DIP-255861X Structure (London, England : 1993) 2013 IMEx Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structure (London, England : 1993) 2013 imex curation Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. DIP original experiment: DIP-255854X Structure (London, England : 1993) 2013 IMEx Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structure (London, England : 1993) 2013 imex curation Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. Only protein-protein interactions in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. DIP original experiment: DIP-255855X Structure (London, England : 1993) 2013 IMEx Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structure (London, England : 1993) 2013 imex curation Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight by staining molecular weight estimation by staining weight by staining Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. DIP original experiment: DIP-255856X Structure (London, England : 1993) 2013 IMEx Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structure (London, England : 1993) 2013 imex curation Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. 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 Hatzopoulos GN., Erat MC., Cutts E., Rogala KB., Slater LM., Stansfeld PJ., Vakonakis I. DIP original experiment: DIP-255860X Structure (London, England : 1993) 2013 IMEx Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. stil_human SCL-interrupting locus protein STIL SIL TAL-1-interrupting locus protein protein protein human Homo sapiens Human MEPIYPFARPQMNTRFPSSRMVPFHFPPSKCALWNPTPTGDFIYLHLSYYRNPKLVVTEKTIRLAYRHAKQNKKNSSCFLLGSLTADEDEEGVTLTVDRFDPGREVPECLEITPTASLPGDFLIPCKVHTQELCSREMIVHSVDDFSSALKALQCHICSKDSLDCGKLLSLRVHITSRESLDSVEFDLHWAAVTLANNFKCTPVKPIPIIPTALARNLSSNLNISQVQGTYKYGYLTMDETRKLLLLLESDPKVYSLPLVGIWLSGITHIYSPQVWACCLRYIFNSSVQERVFSESGNFIIVLYSMTHKEPEFYECFPCDGKIPDFRFQLLTSKETLHLFKNVEPPDKNPIRCELSAESQNAETEFFSKASKNFSIKRSSQKLSSGKMPIHDHDSGVEDEDFSPRPIPSPHPVSQKISKIQPSVPELSLVLDGNFIESNPLPTPLEMVNNENPPLINHLEHLKPLQPQLYDEKHSPEVEAGEPSLRGIPNQLNQDKPALLRHCKVRQPPAYKKGNPHTRNSIKPSSHNGPSHDIFEKLQTVSAGNVQNEEYPIRPSTLNSRQSSLAPQSQPHDFVFSPHNSGRPMELQIPTPPLPSYCSTNVCRCCQHHSHIQYSPLNSWQGANTVGSIQDVQSEALQKHSLFHPSGCPALYCNAFCSSSSPIALRPQGDMGSCSPHSNIEPSPVARPPSHMDLCNPQPCTVCMHTPKTESDNGMMGLSPDAYRFLTEQDRQLRLLQAQIQRLLEAQSLMPCSPKTTAVEDTVQAGRQMELVSVEAQSSPGLHMRKGVSIAVSTGASLFWNAAGEDQEPDSQMKQDDTKISSEDMNFSVDINNEVTSLPGSASSLKAVDIPSFEESNIAVEEEFNQPLSVSNSSLVVRKEPDVPVFFPSGQLAESVSMCLQTGPTGGASNNSETSEEPKIEHVMQPLLHQPSDNQKIYQDLLGQVNHLLNSSSKETEQPSTKAVIISHECTRTQNVYHTKKKTHHSRLVDKDCVLNATLKQLRSLGVKIDSPTKVKKNAHNVDHASVLACISPEAVISGLNCMSFANVGMSGLSPNGVDLSMEANAIALKYLNENQLSQLSVTRSNQNNCDPFSLLHINTDRSTVGLSLISPNNMSFATKKYMKRYGLLQSSDNSEDEEEPPDNADSKSEYLLNQNLRSIPEQLGGQKEPSKNDHEIINCSNCESVGTNADTPVLRNITNEVLQTKAKQQLTEKPAFLVKNLKPSPAVNLRTGKAEFTQHPEKENEGDITIFPESLQPSETLKQMNSMNSVGTFLDVKRLRQLPKLF DIP protein Q15468 original sequence version: 93 mint homomint 7F15BEDA8717659C e7fcy1_danre cenpj protein protein danre Danio rerio (Zebrafish) Brachydanio rerio Zebrafish MMSSPAGLQQGQINFISHWVPDSTRAGVILHGSPGDASSGSVRSSGSLVVQDPDDSFISQFAPLPISRSSSCASVDMCSLGGGSKTPGETQLSDASLNSEMQSIQDILRNTRDLPLIAKLEQLKQMQYRMQEQLKAHQQEQLLRQQREPQRLLAIPQNTAETTVCNREPSVVALNTEHDSHYEFEESLQSTTEDQTMYRKESDSEPQDRPIKSGFGGRTFEEILEEQLKMENQKLTNENPPAKSVKVKRPFLKRGEGLARFTRGKATVPSNRKSPPNPKPSSGQNPKKSQVLDMKSKRNSINKSEGSKSTHPMIQRKTAVLNKENFPQNKTTGPVTKMTLQPHVLVAHQGQNMGSISAQILPKPDPLSNMKINNATPTDCNKERECNRIKDNASVAENSFEVWFTERREHWEQDHKRERAELGEFELLERAADEISFSSNSSFISTLLQRDRRRLSSTPIKSTGQSTLPSQALGPTAAPGLMLGHRAPAPPINTAIQKDIVSIELKELCHEETDEKFDDSSCSNSELEPLSNISNPPINHFQVPITLPYDKRTYQDRDGASSPEGDDRNSSHNEDSTLKDSRTQLEFDDDDTWNDPEDESSCPVEESPSERMLKRKVAFSKGVKPVGGSPKAGANRNEAPSTSQLVAKLFPALKPKPSPVMMPEPQNKPSEEGAAQSRLLRERLVELETEIERFKSENAALARLKQENQDIRENLKKDKADFEKKRIEETAKWEEYKSEEYKKMQREKKLFEKHAATVRARPDKQERDEIQALKQQLNMMQEDLRKREARWSNTQKRLRQQVESLSSENTSLRDQVRTLEKLRLSAWKSAEKEKEKGRSSTSSSRTSTGSKPTDSKSPSHSSKGNSSRKGSPETQISLTDSAFFPEVKETQSFKSELSPLVNQSSGVLVMNERSQDAPLNNSFPKLTITGQTNEKQEEIMQSDSKIEKMLPDGGRLVVFPNGTRKELSADGQTVKVMFFNGDVKHTMPDQRVIYYYAEAQTTHITYPDGMEVLQFPNNQTEKHFPDGRKEITFPDQTVKTLHPDGREESVLTDGTIIQLNPDGSKVIQFNTGQREIHTADFKRREYPDGTVKTVYSDGRQETQYPTGRVRLKDPQGKVIMDTKA DIP protein E7FCY1 original sequence version: 18 571F89A0F8F3B65D stil_danre SCL-interrupting locus protein homolog stil sill zgc:110502 protein protein danre Danio rerio (Zebrafish) Brachydanio rerio Zebrafish MNRVQVDFKGLPAHILENSIAAESLQNTRSSDNVLTPLTFPKSKVALWDPSANGEVVSLHFSYYRNPRLFLVEKALRLAHRHARQTNKPRFFCFLLGTLAVDSDEEGVTITLDRFDPGREQTGCLGKAPTALLPGDILVPCVFEAQHAASSTVHSSEDLNISFKMLQHFCCSKELLELSKLLTLRAQLSCSENMDRLTFNLSWAAVTLACTLDAVPIRAVPIIPTALARNLSSPAGVTQNSKRGFLTMDQTRKLLLILESDPKAYTLPLVGIWLSGVTHIHNPLVWAWCLRYLHSSSLQDKVLSEGGTFLVVLYSLTHRDPEFYQCKPSTGQQQLSFQLLTSRDSLTLYKNVEPSEGRPLQFELSSENQNQETVLFEEVLSQSVLTGTTLGAASAAPQNKLSISDHDSGVEDEDLSPRPSPNPHPVSQQTKRVHPLVPELSMVLDGSFLDGSVVNTQGSTPLSHSQSNVHRRNSSPALQGLSVLRPLVQGSVTKPPPIRRPLTPILSQPKNKLHPNPSQQTPQHSVSRKSLPSMRRSREGSSASSVSSSSSSSSTKNASPNGSFHQQRQRLSQGFPNKPQLIYSGPPTSGHSSAKKSSSVPSQTPVPHPSQHRIFHSTPAVNPCNCCTNHPSVAPLYQNNTWQGTPGYPTAVHSPCVFHCSPETVPPGDHCLSPSRQSLGCRVSPTKSPVCYHSTPPHYSPSSGPCVPTIISNKGLVEQTPSCQAQCCQVKGSKEPCLDTPMGLLPADAYRMLIDQERQLKLLQLQIQKLLESQSKVPEVSSEQNAQQQRPNQVPASPPKRTSVSIAVGTGASLFWSTPQETSTHEASSLEWQTETEPKSGCQNDSTVTSRDRSESACHYSEEHCPGSPQHPTSPQHNTSSGFGVQMFQSPVLGESASMYYQSQSQSKDLSENREIDDPRFYHELLGQVQSRLQDSVIVEDKVEQDQQSLLKTQSLSPVVHQSRKPLTTSSIPQTQKTKQPSSPPNQDRVLSATLKQLQQFGVNIDLDSSQEKTTRATVESASTLACINPEAVIPRLALSEPVGASIWGPSGSVDLSLEANAIALKYLSDSQLSRLSLGSQSSSPHSDPSTILLRRPAVEKSNVALSILSPSNMSLATCKYMKKYGLIEGEISSEEEQEDPIQVDSALGCSVQHETSKTISLGQEREEQNTAVLKNITNKPVVNLHTSPIDSQEQILQDLRPKMQLLLRGGTNSEKENATKRNLIERRSSLTENQRTQEVVDPQGSVGNFLDLSRLRQLPKLF DIP protein Q8JGS1 original sequence version: 54 F8C0FFFA169927F4 cenpj_human Centromere protein J CENPJ CPAP LAP LIP1 Centrosomal P4.1-associated protein LAG-3-associated protein LYST-interacting protein 1 protein protein human Homo sapiens Human MFLMPTSSELNSGQNFLTQWMTNPSRAGVILNRGFPILEADKEKRAAVDISTSFPIKGTHFSDSFSFINEEDSLLEEQKLESNNPYKPQSDKSETHTAFPCIKKGPQVAACHSAPGHQEENKNDFIPDLASEFKEGAYKDPLFKKLEQLKEVQQKKQEQLKRQQLEQLQRLMEEQEKLLTMVSGQCTLPGLSLLPDDQSQKHRSPGNTTTGERATCCFPSYVYPDPTQEETYPSNILSHEQSNFCRTAHGDFVLTSKRASPNLFSEAQYQEAPVEKNNLKEENRNHPTGESILCWEKVTEQIQEANDKNLQKHDDSSEVANIEERPIKAAIGERKQTFEDYLEEQIQLEEQELKQKQLKEAEGPLPIKAKPKQPFLKRGEGLARFTNAKSKFQKGKESKLVTNQSTSEDQPLFKMDRQQLQRKTALKNKELCADNPILKKDSKARTKSGSVTLSQKPKMLKCSNRKSLSPSGLKIQTGKKCDGQFRDQIKFENKVTSNNKENVTECPKPCDTGCTGWNKTQGKDRLPLSTGPASRLAAKSPIRETMKESESSLDVSLQKKLETWEREKEKENLELDEFLFLEQAADEISFSSNSSFVLKILERDQQICKGHRMSSTPVKAVPQKTNPADPISHCNRSEDLDHTAREKESECEVAPKQLHSLSSADELREQPCKIRKAVQKSTSENQTEWNARDDEGVPNSDSSTDSEEQLDVTIKPSTEDRERGISSREDSPQVCDDKGPFKDTRTQEDKRRDVDLDLSDKDYSSDESIMESIKHKVSEPSRSSSLSLSKMDFDDERTWTDLEENLCNHDVVLGNESTYGTPQTCYPNNEIGILDKTIKRKIAPVKRGEDLSKSRRSRSPPTSELMMKFFPSLKPKPKSDSHLGNELKLNISQDQPPGDNARSQVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFKKEEMRKLQKERKVFEKYTTAARTFPDKKEREEIQTLKQQIADLREDLKRKETKWSSTHSRLRSQIQMLVRENTDLREEIKVMERFRLDAWKRAEAIESSLEVEKKDKLANTSVRFQNSQISSGTQVEKYKKNYLPMQGNPPRRSKSAPPRDLGNLDKGQAASPREPLEPLNFPDPEYKEEEEDQDIQGEISHPDGKVEKVYKNGCRVILFPNGTRKEVSADGKTITVTFFNGDVKQVMPDQRVIYYYAAAQTTHTTYPEGLEVLHFSSGQIEKHYPDGRKEITFPDQTVKNLFPDGQEESIFPDGTIVRVQRDGNKLIEFNNGQRELHTAQFKRREYPDGTVKTVYANGHQETKYRSGRIRVKDKEGNVLMDTEL DIP protein Q9HC77 original sequence version: 70 DIP protein Q9HC77 original sequence version: 99 B4E6531B62A30F2D cenpj-1 6 13 unspecified role unspecified role unspecified role unspecified role Region 897-1056 Region 897-1056 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction cenpj-stil-6 3 10 unspecified role unspecified role unspecified role unspecified role Region 385-433 Region 385-433 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain FAM-label FAM-label fluorescein fluorescein label fluorescein n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role Region 1142-1338 Region 1142-1338 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9HC77:p.Tyr1208Ala Y1208A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y1208A'. Wed May 02 18:14:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr1208ala' Tue Jun 30 17:55:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr1208Ala' Q9HC77:p.Tyr1210Ala Y1210A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y1210A'. Wed May 02 16:40:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr1210ala' Tue Jun 30 19:05:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr1210Ala' Q9HC77:p.Phe1229Ala F1229A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain F A This feature has been corrected as a result of our quality control procedures. The original label was 'F1229A'. Wed May 02 16:09:25 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe1229ala' Tue Jun 30 18:58:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe1229Ala' Q9HC77:p.Glu1235Val E1235V/K mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain E V Wed May 02 20:17:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu1235val' Tue Jun 30 19:51:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu1235Val' Q9HC77:p.Glu1235Lys mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain E K Wed May 02 18:28:56 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu1235lys' Tue Jun 30 17:35:51 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu1235Lys' ecolx Escherichia coli direct interaction direct interaction cenpj-stil-7 5 12 unspecified role unspecified role unspecified role unspecified role Region 414-428 Region 414-428 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 11 unspecified role unspecified role unspecified role unspecified role Region 943-1121 Region 943-1121 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction cenpj-2 7 13 unspecified role unspecified role unspecified role unspecified role Region 897-1056 Region 897-1056 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction cenpj-3 8 13 unspecified role unspecified role unspecified role unspecified role Region 897-1056 Region 897-1056 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction cenpj-4 4 11 unspecified role unspecified role unspecified role unspecified role Region 943-1121 Region 943-1121 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction cenpj-stil-8 1 10 unspecified role unspecified role unspecified role unspecified role FAM-label FAM-label fluorescein fluorescein label fluorescein n-term range n-terminal range n-term range n-term range n-terminal range n-term range Region 420-475 Region 420-475 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q15468:p.Arg405Ile R405I mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain R I This feature has been corrected as a result of our quality control procedures. The original label was 'R405I'. Wed May 02 17:59:39 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg405ile' Tue Jun 30 18:02:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg405Ile' Q15468:p.Lys419Glu K419E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K419E'. Wed May 02 17:34:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys419glu' Tue Jun 30 15:48:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys419Glu' Region 385-433 Region 385-433 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role Region 1142-1338 Region 1142-1338 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction cenpj-stil-9 9 12 unspecified role unspecified role unspecified role unspecified role Region 398-450 Region 398-450 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role Region 943-1121 Region 943-1121 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction cenpj-stil-10 2 12 unspecified role unspecified role unspecified role unspecified role Region 398-450 Region 398-450 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role Region 943-1121 Region 943-1121 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction