DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Crystal structure of the dynamin tetramer. Crystal structure of the dynamin tetramer. Nature 2015 imex curation Reubold TF., Faelber K., Plattner N., Posor Y., Ketel K., Curth U., Schlegel J., Anand R., Manstein DJ., Noé F., Haucke V., Daumke O., Eschenburg S. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Reubold TF., Faelber K., Plattner N., Posor Y., Ketel K., Curth U., Schlegel J., Anand R., Manstein DJ., Noé F., Haucke V., Daumke O., Eschenburg S. DIP original experiment: DIP-267145X Nature 2015 IMEx Crystal structure of the dynamin tetramer. Crystal structure of the dynamin tetramer. Crystal structure of the dynamin tetramer. Nature 2015 imex curation Reubold TF., Faelber K., Plattner N., Posor Y., Ketel K., Curth U., Schlegel J., Anand R., Manstein DJ., Noé F., Haucke V., Daumke O., Eschenburg S. Only protein-protein interactions ecolx Escherichia coli tem transmission electron microscopy tem predetermined predetermined participant predetermined Reubold TF., Faelber K., Plattner N., Posor Y., Ketel K., Curth U., Schlegel J., Anand R., Manstein DJ., Noé F., Haucke V., Daumke O., Eschenburg S. DIP original experiment: DIP-267148X Nature 2015 IMEx Crystal structure of the dynamin tetramer. Crystal structure of the dynamin tetramer. Crystal structure of the dynamin tetramer. Nature 2015 imex curation Reubold TF., Faelber K., Plattner N., Posor Y., Ketel K., Curth U., Schlegel J., Anand R., Manstein DJ., Noé F., Haucke V., Daumke O., Eschenburg S. 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 Reubold TF., Faelber K., Plattner N., Posor Y., Ketel K., Curth U., Schlegel J., Anand R., Manstein DJ., Noé F., Haucke V., Daumke O., Eschenburg S. DIP original experiment: DIP-267149X Nature 2015 IMEx Crystal structure of the dynamin tetramer. Crystal structure of the dynamin tetramer. Crystal structure of the dynamin tetramer. Nature 2015 imex curation Reubold TF., Faelber K., Plattner N., Posor Y., Ketel K., Curth U., Schlegel J., Anand R., Manstein DJ., Noé F., Haucke V., Daumke O., Eschenburg S. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Reubold TF., Faelber K., Plattner N., Posor Y., Ketel K., Curth U., Schlegel J., Anand R., Manstein DJ., Noé F., Haucke V., Daumke O., Eschenburg S. DIP original experiment: DIP-267147X Nature 2015 IMEx Crystal structure of the dynamin tetramer. Crystal structure of the dynamin tetramer. Crystal structure of the dynamin tetramer. Nature 2015 imex curation Reubold TF., Faelber K., Plattner N., Posor Y., Ketel K., Curth U., Schlegel J., Anand R., Manstein DJ., Noé F., Haucke V., Daumke O., Eschenburg S. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Reubold TF., Faelber K., Plattner N., Posor Y., Ketel K., Curth U., Schlegel J., Anand R., Manstein DJ., Noé F., Haucke V., Daumke O., Eschenburg S. DIP original experiment: DIP-267146X Nature 2015 IMEx Crystal structure of the dynamin tetramer. dyn1_human Dynamin-1 DNM1 DNM protein protein human Homo sapiens Human MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNATTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKVAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKLQSQLLSIEKEVEEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRSGQASPSRPESPRPPFDL DIP protein Q05193 original sequence version: 142 DIP protein Q05193 original sequence version: 113 DIP protein Q05193 original sequence version: 100 DIP protein Q05193 original sequence version: 115 DIP protein Q05193-1 original sequence version: 111 DIP protein Q05193 original sequence version: 153 7FCD8CB572FFEAEF q9uq16-2 Dynamin-3 KIAA0820 Dynamin, testicular T-dynamin DNM3 protein protein human Homo sapiens Human MGNREMEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLHCKGKKFTDFDEVRLEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFITRENCLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLPNFRNKLQGQLLSIEHEVEAYKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSGDQVDTLELSGGAKINRIFHERFPFEIVKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVIQELINTVKKCTKKLANFPRLCEETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQRSSQVHKKTTVGNQVIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVYKDYRFLELACDSQEDVDSWKASLLRAGVYPDKSVAENDENGQAENFSMDPQLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQALKEALGIIGDISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPSRPTRAPPSVPSRRPPPSPTRPTIIRPLESSLLD DIP protein Q9UQ16-2 original sequence version: 140 922D192B91B47957 dnm3-1 1 7 unspecified role unspecified role unspecified role unspecified role Region 1-754 Region 1-754 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 dnm3-2 2 7 unspecified role unspecified role unspecified role unspecified role Region 1-754 Region 1-754 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 dnm3-3 5 7 unspecified role unspecified role unspecified role unspecified role Region 1-754 Region 1-754 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9UQ16-2:p.[Ile481Asp;His677Asp;Leu678Ser] I481D/H677D/L678S 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 L S certain certain sequence position certain certain certain sequence position certain H D certain certain sequence position certain certain certain sequence position certain I D This feature has been corrected as a result of our quality control procedures. The original label was 'I481D/H677D/L678S'. Wed May 02 18:14:51 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile481asp,his677asp,leu678ser' Tue Jun 30 18:29:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Ile481Asp;His677Asp;Leu678Ser]' ecolx Escherichia coli direct interaction direct interaction dnm3-4 3 7 unspecified role unspecified role unspecified role unspecified role Region 1-754 Region 1-754 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 dnm1-18 4 6 unspecified role unspecified role unspecified role unspecified role Q05193:p.[Ile481Asp;His687_Leu688delinsAspSer] I481D/H687D/L688S 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 HL DS certain certain sequence position certain certain certain sequence position certain I D Wed May 02 15:50:56 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile481asp,his_leu687-688asp_ser' Tue Jun 30 18:29:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Ile481Asp;His687_Leu688delinsAspSer]' Region 6-746 Region 6-746 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