DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Kim S., Sun H., Ball HL., Wassmann K., Luo X., Yu H. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Kim S., Sun H., Ball HL., Wassmann K., Luo X., Yu H. DIP original experiment: DIP-220586X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Kim S., Sun H., Ball HL., Wassmann K., Luo X., Yu H. Only protein-protein interactions in vitro In vitro pull down pull down autoradiography autoradiography Kim S., Sun H., Ball HL., Wassmann K., Luo X., Yu H. DIP original experiment: DIP-220583X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Kim S., Sun H., Ball HL., Wassmann K., Luo X., Yu H. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Kim S., Sun H., Ball HL., Wassmann K., Luo X., Yu H. DIP original experiment: DIP-220584X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Kim S., Sun H., Ball HL., Wassmann K., Luo X., Yu H. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Kim S., Sun H., Ball HL., Wassmann K., Luo X., Yu H. DIP original experiment: DIP-220585X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Kim S., Sun H., Ball HL., Wassmann K., Luo X., Yu H. Only protein-protein interactions in vitro In vitro pull down pull down autoradiography autoradiography Kim S., Sun H., Ball HL., Wassmann K., Luo X., Yu H. DIP original experiment: DIP-220582X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Kim S., Sun H., Ball HL., Wassmann K., Luo X., Yu H. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Kim S., Sun H., Ball HL., Wassmann K., Luo X., Yu H. DIP original experiment: DIP-220580X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Kim S., Sun H., Ball HL., Wassmann K., Luo X., Yu H. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Kim S., Sun H., Ball HL., Wassmann K., Luo X., Yu H. DIP original experiment: DIP-220581X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Phosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition. cdc20_human Cell division cycle protein 20 homolog CDC20 p55CDC protein protein human Homo sapiens Human MAQFAFESDLHSLLQLDAPIPNAPPARWQRKAKEAAGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRYIPHRSAAQMEVASFLLSKENQPENSQTPTKKEHQKAWALNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGSSRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQMEQPGEYISSVAWIKEGNYLAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLSWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPDGRHLASGGNDNLVNVWPSAPGEGGWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAHSQVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTSRVLSLTMSPDGATVASAAADETLRLWRCFELDPARRREREKASAAKSSLIHQGIR DIP protein Q12834 original sequence version: 132 DIP protein Q12834 original sequence version: 74 DIP protein Q12834 original sequence version: 100 DIP protein Q12834 original sequence version: 118 DIP protein Q12834 original sequence version: 125 DIP protein Q12834 original sequence version: 114 DIP protein Q12834 original sequence version: 147 DIP protein Q12834 original sequence version: 162 FD5C967AF84089E8 md2l1_human Mitotic spindle assembly checkpoint protein MAD2A MAD2L1 MAD2 Mitotic arrest deficient 2-like protein 1 protein protein human Homo sapiens Human MALQLSREQGITLRGSAEIVAEFFSFGINSILYQRGIYPSETFTRVQKYGLTLLVTTDLELIKYLNNVVEQLKDWLYKCSVQKLVVVISNIESGEVLERWQFDIECDKTAKDDSAPREKSQKAIQDEIRSVIRQITATVTFLPLLEVSCSFDLLIYTDKDLVVPEKWEESGPQFITNSEEVRLRSFTTTIHKVNSMVAYKIPVND DIP protein Q13257 original sequence version: 133 DIP protein Q13257 original sequence version: 78 DIP protein Q13257 original sequence version: 105 DIP protein Q13257 original sequence version: 120 DIP protein Q13257 original sequence version: 127 DIP protein Q13257 original sequence version: 116 DIP protein Q13257 original sequence version: 150 DIP protein Q13257 original sequence version: 156 DIP protein Q13257 original sequence version: 134 B8DCBF0043836764 md1l1_human Mitotic spindle assembly checkpoint protein MAD1 Mitotic arrest deficient 1-like protein 1 Mitotic checkpoint MAD1 protein homolog Tax-binding protein 181 MAD1L1 MAD1 TXBP181 protein protein human Homo sapiens Human MEDLGENTMVLSTLRSLNNFISQRVEGGSGLDISTSAPGSLQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITTENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRRQDSIPAFLSSLTLELFSRQTVA DIP protein Q9Y6D9 original sequence version: 56 DIP protein Q9Y6D9 original sequence version: 99 DIP protein Q9Y6D9-1 original sequence version: 135 DIP protein Q9Y6D9 original sequence version: 135 DIP protein Q9Y6D9 original sequence version: 113 DA65529856A37EE3 cdc20-mad2l1-13 6 8 unspecified role unspecified role unspecified role unspecified role Region 124-137 Region 124-137 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction mad2l1-cdc20-3 3 9 unspecified role unspecified role prey prey human Homo sapiens Human 8 unspecified role unspecified role prey prey human Homo sapiens Human 10 unspecified role unspecified role prey prey human Homo sapiens Human 9 unspecified role unspecified role bait bait Myc-tag Myc-tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human association association mad2l1-cdc20-4 2 8 unspecified role unspecified role prey prey Region 124-137 Region 124-137 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 35S-label 35S-label 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro 9 unspecified role unspecified role bait bait His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Region 196-205 Region 196-205 required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q13257:p.Ser195Asp S195D mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain S D This feature has been corrected as a result of our quality control procedures. The original label was 'S195D'. Wed May 02 20:15:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser195asp' Tue Jun 30 19:50:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser195Asp' ecolx Escherichia coli direct interaction direct interaction mad1l1-mad2l1-9 7 10 unspecified role unspecified role unspecified role unspecified role Region 495-718 Region 495-718 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction mad2l1-cdc20-5 1 8 unspecified role unspecified role prey prey human Homo sapiens Human 9 unspecified role unspecified role bait bait Myc-tag Myc-tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Q13257:p.Ser195Asp S195D mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain S D This feature has been corrected as a result of our quality control procedures. The original label was 'S195D'. Wed May 02 19:54:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser195asp' Tue Jun 30 16:01:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser195Asp' human Homo sapiens Human physical association physical association mad2l1-mad1l1-3 4 9 unspecified role unspecified role prey prey human Homo sapiens Human 10 unspecified role unspecified role prey prey human Homo sapiens Human 9 unspecified role unspecified role bait bait Myc-tag Myc-tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Q13257:p.Ser195Asp S195D mutation mutation certain certain sequence position certain certain certain sequence position certain S D This feature has been corrected as a result of our quality control procedures. The original label was 'S195D'. Wed May 02 19:14:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser195asp' Tue Jun 30 20:24:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser195Asp' human Homo sapiens Human association association mad2l1-mad1l1-4 5 10 unspecified role unspecified role prey prey Region 495-718 Region 495-718 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 35S-label 35S-label 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro 9 unspecified role unspecified role bait bait His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Region 196-205 Region 196-205 required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction