DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. Structure (London, England : 1993) 2009 imex curation Bolanos-Garcia VM., Kiyomitsu T., D'Arcy S., Chirgadze DY., Grossmann JG., Matak-Vinkovic D., Venkitaraman AR., Yanagida M., Robinson CV., Blundell TL. Only protein-protein interactions ecolx Escherichia coli saxs x ray scattering saxs predetermined predetermined participant predetermined Bolanos-Garcia VM., Kiyomitsu T., D'Arcy S., Chirgadze DY., Grossmann JG., Matak-Vinkovic D., Venkitaraman AR., Yanagida M., Robinson CV., Blundell TL. DIP original experiment: DIP-132163X Structure (London, England : 1993) 2009 IMEx The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. Structure (London, England : 1993) 2009 imex curation Bolanos-Garcia VM., Kiyomitsu T., D'Arcy S., Chirgadze DY., Grossmann JG., Matak-Vinkovic D., Venkitaraman AR., Yanagida M., Robinson CV., Blundell TL. Only protein-protein interactions ecolx Escherichia coli cd circular dichroism CD CD cd predetermined predetermined participant predetermined Bolanos-Garcia VM., Kiyomitsu T., D'Arcy S., Chirgadze DY., Grossmann JG., Matak-Vinkovic D., Venkitaraman AR., Yanagida M., Robinson CV., Blundell TL. DIP original experiment: DIP-132165X Structure (London, England : 1993) 2009 IMEx The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. Structure (London, England : 1993) 2009 imex curation Bolanos-Garcia VM., Kiyomitsu T., D'Arcy S., Chirgadze DY., Grossmann JG., Matak-Vinkovic D., Venkitaraman AR., Yanagida M., Robinson CV., Blundell TL. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Bolanos-Garcia VM., Kiyomitsu T., D'Arcy S., Chirgadze DY., Grossmann JG., Matak-Vinkovic D., Venkitaraman AR., Yanagida M., Robinson CV., Blundell TL. DIP original experiment: DIP-132162X Structure (London, England : 1993) 2009 IMEx The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. Structure (London, England : 1993) 2009 imex curation Bolanos-Garcia VM., Kiyomitsu T., D'Arcy S., Chirgadze DY., Grossmann JG., Matak-Vinkovic D., Venkitaraman AR., Yanagida M., Robinson CV., Blundell TL. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Bolanos-Garcia VM., Kiyomitsu T., D'Arcy S., Chirgadze DY., Grossmann JG., Matak-Vinkovic D., Venkitaraman AR., Yanagida M., Robinson CV., Blundell TL. DIP original experiment: DIP-132166X Structure (London, England : 1993) 2009 IMEx The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. Structure (London, England : 1993) 2009 imex curation Bolanos-Garcia VM., Kiyomitsu T., D'Arcy S., Chirgadze DY., Grossmann JG., Matak-Vinkovic D., Venkitaraman AR., Yanagida M., Robinson CV., Blundell TL. Only protein-protein interactions ecolx Escherichia coli ms of complexes mass spectrometry studies of complexes ms of complexes predetermined predetermined participant predetermined Bolanos-Garcia VM., Kiyomitsu T., D'Arcy S., Chirgadze DY., Grossmann JG., Matak-Vinkovic D., Venkitaraman AR., Yanagida M., Robinson CV., Blundell TL. DIP original experiment: DIP-132164X Structure (London, England : 1993) 2009 IMEx The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. Structure (London, England : 1993) 2009 imex curation Bolanos-Garcia VM., Kiyomitsu T., D'Arcy S., Chirgadze DY., Grossmann JG., Matak-Vinkovic D., Venkitaraman AR., Yanagida M., Robinson CV., Blundell TL. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Bolanos-Garcia VM., Kiyomitsu T., D'Arcy S., Chirgadze DY., Grossmann JG., Matak-Vinkovic D., Venkitaraman AR., Yanagida M., Robinson CV., Blundell TL. DIP original experiment: DIP-132167X Structure (London, England : 1993) 2009 IMEx The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. bub1_yeast Checkpoint serine/threonine-protein kinase BUB1 YGR188C G7542 BUB1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MNLDLGSTVRGYESDKDTFPQSKGVSSSQKEQHSQLNQTKIAYEQRLLNDLEDMDDPLDLFLDYMIWISTSYIEVDSESGQEVLRSTMERCLIYIQDMETYRNDPRFLKIWIWYINLFLSNNFHESENTFKYMFNKGIGTKLSLFYEEFSKLLENAQFFLEAKVLLELGAENNCRPYNRLLRSLSNYEDRLREMNIVENQNSVPDSRERLKGRLIYRTAPFFIRKFLTSSLMTDDKENRANLNSNVGVGKSAPNVYQDSIVVADFKSETERLNLNSSKQPSNQRLKNGNKKTSIYADQKQSNNPVYKLINTPGRKPERIVFNFNLIYPENDEEFNTEEILAMIKGLYKVQRRGKKHTEDYTSDKNRKKRKLDVLVERRQDLPSSQPPVVPKSTRIEVFKDDDNPSQSTHHKNTQVQVQTTTSILPLKPVVDGNLAHETPVKPSLTSNASRSPTVTAFSKDAINEVFSMFNQHYSTPGALLDGDDTTTSKFNVFENFTQEFTAKNIEDLTEVKDPKQETVSQQTTSTNETNDRYERLSNSSTRPEKADYMTPIKETTETDVVPIIQTPKEQIRTEDKKSGDNTETQTQLTSTTIQSSPFLTQPEPQAEKLLQTAEHSEKSKEHYPTIIPPFTKIKNQPPVIIENPLSNNLRAKFLSEISPPLFQYNTFYNYNQELKMSSLLKKIHRVSRNENKNPIVDFKKTGDLYCIRGELGEGGYATVYLAESSQGHLRALKVEKPASVWEYYIMSQVEFRLRKSTILKSIINASALHLFLDESYLVLNYASQGTVLDLINLQREKAIDGNGIMDEYLCMFITVELMKVLEKIHEVGIIHGDLKPDNCMIRLEKPGEPLGAHYMRNGEDGWENKGIYLIDFGRSFDMTLLPPGTKFKSNWKADQQDCWEMRAGKPWSYEADYYGLAGVIHSMLFGKFIETIQLQNGRCKLKNPFKRYWKKEIWGVIFDLLLNSGQASNQALPMTEKIVEIRNLIESHLEQHAENHLRNVILSIEEELSHFQYKGKPSRRF 6D76FC980775D3F9 6D76FC980775D3F9 q8ng31-2 Kinetochore scaffold 1 KNL1 ALL1-fused gene from chromosome 15q14 protein Bub-linking kinetochore protein CASC5 Cancer susceptibility candidate gene 5 protein Cancer/testis antigen 29 KIAA1570 Kinetochore-null protein 1 Protein CASC5 Protein D40/AF15q14 protein protein human Homo sapiens Human MDGVSSEANEENDNIERPVRRRHSSILKPPRSPLQDLRGGNERVQESNALRNKKNSRRVSFADTIKVFQTESHMKIVRKSEMEETETGENLLLIQNKKLEDNYCEITGMNTLLSAPIHTQMQQKEFSIIEHTRERKHANDQTVIFSDENQMDLTSSHTVMITKGLLDNPISEKSTKIDTTSFLANLKLHTEDSRMKKEVNFSVDQNTSSENKIDFNDFIKRLKTGKCSAFPDVPDKENFEIPIYSKEPNSASSTHQMHVSLKEDENNSNITRLFREKDDGMNFTQCHTANIQTLIPTSSETNSRESKGNDITIYGNDFMDLTFNHTLQILPATGNFSEIENQTQNAMDVTTGYGTKASGNKTVFKSKQNTAFQDLSINSADKIHITRSHIMGAETHIVSQTCNQDARILAMTPESIYSNPSIQGCKTVFYSSCNDAMEMTKCLSNMREEKNLLKHDSNYAKMYCNPDAMSSLTEKTIYSGEENMDITKSHTVAIDNQIFKQDQSNVQIAAAPTPEKEMMLQNLMTTSEDGKMNVNCNSVPHVSKERIQQSLSNPLSISLTDRKTELLSGENMDLTESHTSNLGSQVPLAAYNLAPESTSESHSQSKSSSDECEEITKSRNEPFQRSDIIAKNSLTDTWNKDKDWVLKILPYLDKDSPQSADCNQEIATSHNIVYCGGVLDKQITNRNTVSWEQSLFSTTKPLFSSGQFSMKNHDTAISSHTVKSVLGQNSKLAEPLRKSLSNPTPDYCHDKMIICSEEEQNMDLTKSHTVVIGFGPSELQELGKTNLEHTTGQLTTMNRQIAVKVEKCGKSPIEKSGVLKSNCIMDVLEDESVQKPKFPKEKQNVKIWGRKSVGGPKIDKTIVFSEDDKNDMDITKSYTIEINHRPLLEKRDCHLVPLAGTSETILYTCRQDDMEITRSHTTALECKTVSPDEITTRPMDKTVVFVDNHVELEMTESHTVFIDYQEKERTDRPNFELSQRKSLGTPTVICTPTEESVFFPGNGESDRLVANDSQLTPLEEWSNNRGPVEVADNMELSKSATCKNIKDVQSPGFLNEPLSSKSQRRKSLKLKNDKTIVFSENHKNDMDITQSCMVEIDNESALEDKEDFHLAGASKTILYSCGQDDMEITRSHTTALECKTLLPNEIAIRPMDKTVLFTDNYSDLEVTDSHTVFIDCQATEKILEENPKFGIGKGKNLGVSFPKDNSCVQEIAEKQALAVGNKIVLHTEQKQQLFAATNRTTNEIIKFHSAAMDEKVIGKVVDQACTLEKAQVESCQLNNRDRRNVDFTSSHATAVCGSSDNYSCLPNVISCTDNLEGSAMLLCDKDEEKANYCPVQNDLAYANDFASEYYLESEGQPLSAPCPLLEKEEVIQTSTKGQLDCVITLHKDQDLIKDPRNLLANQTLVYSQDLGEMTKLNSKRVSFKLPKDQMKVYVDDIYVIPQPHFSTDQPPLPKKGQSSINKEEVILSKAGNKSLNIIENSSAPICENKPKILNSEEWFAAACKKELKENIQTTNYNTALDFHSNSDVTKQVIQTHVNAGEAPDPVITSNVPCFHSIKPNLNNLNGKTGEFLAFQTVHLPPLPEQLLELGNKAHNDMHIVQATEIHNINIISSNAKDSRDEENKKSHNGAETTSLPPKTVFKDKVRRCSLGIFLPRLPNKRNCSVTGIDDLEQIPADTTDINHLETQPVSSKDSGIGSVAGKLNLSPSQYINEENLPVYPDEINSSDSINIETEEKALIETYQKEISPYENKMGKTCNSQKRTWVQEEEDIHKEKKIRKNEIKFSDTTQDREIFDHHTEEDIDKSANSVLIKNLSRTPSSCSSSLDSIKADGTSLDFSTYRSSQMESQFLRDTICEESLREKLQDGRITIREFFILLQVHILIQKPRQSNLPGNFTVNTPPTPEDLMLSQYVYRPKIQIYREDCEARRQKIEELKLSASNQDKLLVDINKNLWEKMRHCSDKELKAFGIYLNKIKSCFTKMTKVFTHQGKVALYGKLVQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLEDEEKNNPVEEWDSEMRAAEKELEQLKTEEEELQRNLLELEVQKEQTLAQIDFMQKQRNRTEELLDQLSLSEWDVVEWSDDQAVFTFVYDTIQLTITFEESVVGFPFLDKRYRKIVDVNFQSLLDEDQAPPSSLLVHKLIFQYVEEKESWKKTCTTQHQLPKMLEEFSLVVHHCRLLGEEIEYLKRWGPNYNLMNIDINNNELRLLFSSSAAFAKFEITLFLSAYYPSVPLPSTIQNHVGNTSQDDIATILSKVPLENNYLKNVVKQIYQDLFQDCHFYH DIP protein Q8NG31-2 original sequence version: 59 DIP protein Q8NG31-2 original sequence version: 72 DIP protein Q8NG31-2 original sequence version: 115 A04548DF87BCA275 bub1_human Mitotic checkpoint serine/threonine-protein kinase BUB1 BUB1A BUB1 BUB1L protein protein human Homo sapiens Human MDTPENVLQMLEAHMQSYKGNDPLGEWERYIQWVEENFPENKEYLITLLEHLMKEFLDKKKYHNDPRFISYCLKFAEYNSDLHQFFEFLYNHGIGTLSSPLYIAWAGHLEAQGELQHASAVLQRGIQNQAEPREFLQQQYRLFQTRLTETHLPAQARTSEPLHNVQVLNQMITSKSNPGNNMACISKNQGSELSGVISSACDKESNMERRVITISKSEYSVHSSLASKVDVEQVVMYCKEKLIRGESEFSFEELRAQKYNQRRKHEQWVNEDRHYMKRKEANAFEEQLLKQKMDELHKKLHQVVETSHEDLPASQERSEVNPARMGPSVGSQQELRAPCLPVTYQQTPVNMEKNPREAPPVVPPLANAISAALVSPATSQSIAPPVPLKAQTVTDSMFAVASKDAGCVNKSTHEFKPQSGAEIKEGCETHKVANTSSFHTTPNTSLGMVQATPSKVQPSPTVHTKEALGFIMNMFQAPTLPDISDDKDEWQSLDQNEDAFEAQFQKNVRSSGAWGVNKIISSLSSAFHVFEDGNKENYGLPQPKNKPTGARTFGERSVSRLPSKPKEEVPHAEEFLDDSTVWGIRCNKTLAPSPKSPGDFTSAAQLASTPFHKLPVESVHILEDKENVVAKQCTQATLDSCEENMVVPSRDGKFSPIQEKSPKQALSSHMYSASLLRLSQPAAGGVLTCEAELGVEACRLTDTDAAIAEDPPDAIAGLQAEWMQMSSLGTVDAPNFIVGNPWDDKLIFKLLSGLSKPVSSYPNTFEWQCKLPAIKPKTEFQLGSKLVYVHHLLGEGAFAQVYEATQGDLNDAKNKQKFVLKVQKPANPWEFYIGTQLMERLKPSMQHMFMKFYSAHLFQNGSVLVGELYSYGTLLNAINLYKNTPEKVMPQGLVISFAMRMLYMIEQVHDCEIIHGDIKPDNFILGNGFLEQDDEDDLSAGLALIDLGQSIDMKLFPKGTIFTAKCETSGFQCVEMLSNKPWNYQIDYFGVAATVYCMLFGTYMKVKNEGGECKPEGLFRRLPHLDMWNEFFHVMLNIPDCHHLPSLDLLRQKLKKVFQQHYTNKIRALRNRLIVLLLECKRSRK DIP protein O43683 original sequence version: 94 DIP protein O43683 original sequence version: 154 38AE5E1F88C53BDC scbub1-1 3 7 unspecified role unspecified role unspecified role unspecified role Region 29-230 Region 29-230 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction scbub1-2 2 7 unspecified role unspecified role unspecified role unspecified role Region 29-230 Region 29-230 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction scbub1-3 4 7 unspecified role unspecified role unspecified role unspecified role Region 29-230 Region 29-230 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction scbub1-4 1 7 unspecified role unspecified role unspecified role unspecified role Region 29-230 Region 29-230 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction scbub1-5 5 7 unspecified role unspecified role unspecified role unspecified role Region 29-230 Region 29-230 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction bub1-knl1-1 6 8 unspecified role unspecified role prey prey Region 1-728 Region 1-728 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 9 unspecified role unspecified role bait bait Region 1-189 Region 1-189 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain O43683:p.[Gly20Ser;Asn21Gln;Asp22Ala] G20S/N21Q/D22A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain D A certain certain sequence position certain certain certain sequence position certain N Q certain certain sequence position certain certain certain sequence position certain G S This feature has been corrected as a result of our quality control procedures. The original label was 'G20S/N21Q/D22A'. Wed May 02 16:19:02 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly20ser,asn21gln,asp22ala' Tue Jun 30 17:11:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Gly20Ser;Asn21Gln;Asp22Ala]' O43683:p.[Leu45Gly;Leu49Gly] L45G/L49G mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain L G certain certain sequence position certain certain certain sequence position certain L G This feature has been corrected as a result of our quality control procedures. The original label was 'L45G/L49G'. Wed May 02 17:09:39 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu45gly,leu49gly' Tue Jun 30 19:12:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu45Gly;Leu49Gly]' O43683:p.Asp65Gly D65G mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain D G This feature has been corrected as a result of our quality control procedures. The original label was 'D65G'. Wed May 02 19:27:30 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp65gly' Tue Jun 30 16:10:52 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp65Gly' O43683:p.[Gly93Ala;Gly95Ala] G93A/G95A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain G A certain certain sequence position certain certain certain sequence position certain G A This feature has been corrected as a result of our quality control procedures. The original label was 'G93A/G95A'. Wed May 02 15:15:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly93ala,gly95ala' Tue Jun 30 19:55:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Gly93Ala;Gly95Ala]' O43683:p.[Gly93Ala;Ile94Gly;Gly95Leu] G93A/I94G/G95L mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain G L certain certain sequence position certain certain certain sequence position certain I G certain certain sequence position certain certain certain sequence position certain G A This feature has been corrected as a result of our quality control procedures. The original label was 'G93A/I94G/G95L'. Wed May 02 17:53:57 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly93ala,ile94gly,gly95leu' Tue Jun 30 17:58:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Gly93Ala;Ile94Gly;Gly95Leu]' yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast direct interaction direct interaction