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 structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. Structure (London, England : 1993) 2007 imex curation Derewenda U., Tarricone C., Choi WC., Cooper DR., Lukasik S., Perrina F., Tripathy A., Kim MH., Cafiso DS., Musacchio A., Derewenda ZS. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Derewenda U., Tarricone C., Choi WC., Cooper DR., Lukasik S., Perrina F., Tripathy A., Kim MH., Cafiso DS., Musacchio A., Derewenda ZS. DIP original experiment: DIP-67897X Structure (London, England : 1993) 2007 IMEx The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. Structure (London, England : 1993) 2007 imex curation Derewenda U., Tarricone C., Choi WC., Cooper DR., Lukasik S., Perrina F., Tripathy A., Kim MH., Cafiso DS., Musacchio A., Derewenda ZS. Only protein-protein interactions ecolx Escherichia coli cd circular dichroism CD CD cd predetermined predetermined participant predetermined Derewenda U., Tarricone C., Choi WC., Cooper DR., Lukasik S., Perrina F., Tripathy A., Kim MH., Cafiso DS., Musacchio A., Derewenda ZS. DIP original experiment: DIP-67894X Structure (London, England : 1993) 2007 IMEx The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. Structure (London, England : 1993) 2007 imex curation Derewenda U., Tarricone C., Choi WC., Cooper DR., Lukasik S., Perrina F., Tripathy A., Kim MH., Cafiso DS., Musacchio A., Derewenda ZS. Only protein-protein interactions in vitro In vitro epr electron paramagnetic resonance ESR EPR EPR ESR epr predetermined predetermined participant predetermined Derewenda U., Tarricone C., Choi WC., Cooper DR., Lukasik S., Perrina F., Tripathy A., Kim MH., Cafiso DS., Musacchio A., Derewenda ZS. DIP original experiment: DIP-67896X Structure (London, England : 1993) 2007 IMEx The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. Structure (London, England : 1993) 2007 imex curation Derewenda U., Tarricone C., Choi WC., Cooper DR., Lukasik S., Perrina F., Tripathy A., Kim MH., Cafiso DS., Musacchio A., Derewenda ZS. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Derewenda U., Tarricone C., Choi WC., Cooper DR., Lukasik S., Perrina F., Tripathy A., Kim MH., Cafiso DS., Musacchio A., Derewenda ZS. DIP original experiment: DIP-67898X Structure (London, England : 1993) 2007 IMEx The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. Structure (London, England : 1993) 2007 imex curation Derewenda U., Tarricone C., Choi WC., Cooper DR., Lukasik S., Perrina F., Tripathy A., Kim MH., Cafiso DS., Musacchio A., Derewenda ZS. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Derewenda U., Tarricone C., Choi WC., Cooper DR., Lukasik S., Perrina F., Tripathy A., Kim MH., Cafiso DS., Musacchio A., Derewenda ZS. DIP original experiment: DIP-67895X Structure (London, England : 1993) 2007 IMEx The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. Structure (London, England : 1993) 2007 imex curation Derewenda U., Tarricone C., Choi WC., Cooper DR., Lukasik S., Perrina F., Tripathy A., Kim MH., Cafiso DS., Musacchio A., Derewenda ZS. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Derewenda U., Tarricone C., Choi WC., Cooper DR., Lukasik S., Perrina F., Tripathy A., Kim MH., Cafiso DS., Musacchio A., Derewenda ZS. DIP original experiment: DIP-67892X Structure (London, England : 1993) 2007 IMEx The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. Structure (London, England : 1993) 2007 imex curation Derewenda U., Tarricone C., Choi WC., Cooper DR., Lukasik S., Perrina F., Tripathy A., Kim MH., Cafiso DS., Musacchio A., Derewenda ZS. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Derewenda U., Tarricone C., Choi WC., Cooper DR., Lukasik S., Perrina F., Tripathy A., Kim MH., Cafiso DS., Musacchio A., Derewenda ZS. DIP original experiment: DIP-67893X Structure (London, England : 1993) 2007 IMEx The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. lis1_mouse Platelet-activating factor acetylhydrolase IB subunit beta PAF acetylhydrolase 45 kDa subunit PAF-AH alpha Lissencephaly-1 protein Pafah1b1 Lis1 Lis-1 Pafaha protein protein mouse Mus musculus Mouse MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR DIP protein P63005 original sequence version: 47 4DBF6A24A6B131CD ndel1_mouse Nuclear distribution protein nudE-like 1 Protein mNudE-like Ndel1 Nudel protein protein mouse Mus musculus Mouse MDGEDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENSFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYVPGSVNCGVMNSNGPECPRSGRATFFHKGAVNGFDPAPPPPGLGSSRPSSAPGMLPLSV DIP protein Q9ERR1 original sequence version: 37 CB3059DFD998E9EC ndel1_human Nuclear distribution protein nudE-like 1 NDEL1 Mitosin-associated protein 1 EOPA MITAP1 NUDEL protein protein human Homo sapiens Human MDGEDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENTFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYISGNVNCGVLNGNGTKFSRSGHTSFFDKGAVNGFDPAPPPPGLGSSRPSSAPGMLPLSV DIP protein Q9GZM8 original sequence version: 36 DIP protein Q9GZM8 original sequence version: 65 DIP protein Q9GZM8 original sequence version: 78 E91EA053FCA315D7 ndel1-pafah1b1-5 3 8 unspecified role unspecified role unspecified role unspecified role spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm 9 unspecified role unspecified role unspecified role unspecified role Region 8-192 Region 8-192 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 ndel1-pafah1b1-6 1 8 unspecified role unspecified role prey prey spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm 9 unspecified role unspecified role bait bait Region 8-192 Region 8-192 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag tag tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli direct interaction direct interaction ndel1-9 5 9 unspecified role unspecified role unspecified role unspecified role Region 8-99 Region 8-99 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 ndel1-pafah1b1-7 4 10 unspecified role unspecified role bait bait Region 58-169 Region 58-169 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9GZM8:p.Glu119Ala E119A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain E A This feature has been corrected as a result of our quality control procedures. The original label was 'E119A'. Wed May 02 18:13:07 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu119ala' Tue Jun 30 15:55:34 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu119Ala' Q9GZM8:p.Arg130Ala R130A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R130A'. Wed May 02 15:26:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg130ala' Tue Jun 30 17:35:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg130Ala' GST-tag GST-tag tag tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 8 unspecified role unspecified role prey prey spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction ndel1-2 2 9 unspecified role unspecified role unspecified role unspecified role Region 8-99 Region 8-99 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 ndel1-3 6 9 unspecified role unspecified role unspecified role unspecified role Region 8-192 Region 8-192 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 ndel1-4 7 10 unspecified role unspecified role unspecified role unspecified role Region 58-169 Region 58-169 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