DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. Nature structural & molecular biology 2011 imex curation Calabrese MF., Scott DC., Duda DM., Grace CR., Kurinov I., Kriwacki RW., Schulman BA. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Calabrese MF., Scott DC., Duda DM., Grace CR., Kurinov I., Kriwacki RW., Schulman BA. DIP original experiment: DIP-218653X Nature structural & molecular biology 2011 IMEx A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. Nature structural & molecular biology 2011 imex curation Calabrese MF., Scott DC., Duda DM., Grace CR., Kurinov I., Kriwacki RW., Schulman BA. Only protein-protein interactions in vitro In vitro comigration in sds comigration in sds page comigration in sds predetermined predetermined participant predetermined Calabrese MF., Scott DC., Duda DM., Grace CR., Kurinov I., Kriwacki RW., Schulman BA. DIP original experiment: DIP-218655X Nature structural & molecular biology 2011 IMEx A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. Nature structural & molecular biology 2011 imex curation Calabrese MF., Scott DC., Duda DM., Grace CR., Kurinov I., Kriwacki RW., Schulman BA. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Calabrese MF., Scott DC., Duda DM., Grace CR., Kurinov I., Kriwacki RW., Schulman BA. DIP original experiment: DIP-218652X Nature structural & molecular biology 2011 IMEx A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. Nature structural & molecular biology 2011 imex curation Calabrese MF., Scott DC., Duda DM., Grace CR., Kurinov I., Kriwacki RW., Schulman BA. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Calabrese MF., Scott DC., Duda DM., Grace CR., Kurinov I., Kriwacki RW., Schulman BA. DIP original experiment: DIP-218654X Nature structural & molecular biology 2011 IMEx A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. Nature structural & molecular biology 2011 imex curation Calabrese MF., Scott DC., Duda DM., Grace CR., Kurinov I., Kriwacki RW., Schulman BA. Only protein-protein interactions in vitro In vitro comigration in sds comigration in sds page comigration in sds predetermined predetermined participant predetermined Calabrese MF., Scott DC., Duda DM., Grace CR., Kurinov I., Kriwacki RW., Schulman BA. DIP original experiment: DIP-218656X Nature structural & molecular biology 2011 IMEx A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. Nature structural & molecular biology 2011 imex curation Calabrese MF., Scott DC., Duda DM., Grace CR., Kurinov I., Kriwacki RW., Schulman BA. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Calabrese MF., Scott DC., Duda DM., Grace CR., Kurinov I., Kriwacki RW., Schulman BA. DIP original experiment: DIP-218650X Nature structural & molecular biology 2011 IMEx A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. Nature structural & molecular biology 2011 imex curation Calabrese MF., Scott DC., Duda DM., Grace CR., Kurinov I., Kriwacki RW., Schulman BA. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Calabrese MF., Scott DC., Duda DM., Grace CR., Kurinov I., Kriwacki RW., Schulman BA. DIP original experiment: DIP-218651X Nature structural & molecular biology 2011 IMEx A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. ubc12_yeast NEDD8-conjugating enzyme UBC12 UBC12 YLR306W L2142.3 RUB1-conjugating enzyme Ubiquitin carrier protein 12 protein protein yeast Saccharomyces cerevisiae Baker's yeast MLKLRQLQKKKQKENENSSSIQPNLSAARIRLKRDLDSLDLPPTVTLNVITSPDSADRSQSPKLEVIVRPDEGYYNYGSINFNLDFNEVYPIEPPKVVCLKKIFHPNIDLKGNVCLNILREDWSPALDLQSIITGLLFLFLEPNPNDPLNKDAAKLLCEGEKEFAEAVRLTMSGGSIEHVKYDNIVSP BEEECF40B82C4BAB BEEECF40B82C4BAB cul1_human Cullin-1 CUL1 protein protein human Homo sapiens Human MSSTRSQNPHGLKQIGLDQIWDDLRAGIQQVYTRQSMAKSRYMELYTHVYNYCTSVHQSNQARGAGVPPSKSKKGQTPGGAQFVGLELYKRLKEFLKNYLTNLLKDGEDLMDESVLKFYTQQWEDYRFSSKVLNGICAYLNRHWVRRECDEGRKGIYEIYSLALVTWRDCLFRPLNKQVTNAVLKLIEKERNGETINTRLISGVVQSYVELGLNEDDAFAKGPTLTVYKESFESQFLADTERFYTRESTEFLQQNPVTEYMKKAEARLLEEQRRVQVYLHESTQDELARKCEQVLIEKHLEIFHTEFQNLLDADKNEDLGRMYNLVSRIQDGLGELKKLLETHIHNQGLAAIEKCGEAALNDPKMYVQTVLDVHKKYNALVMSAFNNDAGFVAALDKACGRFINNNAVTKMAQSSSKSPELLARYCDSLLKKSSKNPEEAELEDTLNQVMVVFKYIEDKDVFQKFYAKMLAKRLVHQNSASDDAEASMISKLKQACGFEYTSKLQRMFQDIGVSKDLNEQFKKHLTNSEPLDLDFSIQVLSSGSWPFQQSCTFALPSELERSYQRFTAFYASRHSGRKLTWLYQLSKGELVTNCFKNRYTLQASTFQMAILLQYNTEDAYTVQQLTDSTQIKMDILAQVLQILLKSKLLVLEDENANVDEVELKPDTLIKLYLGYKNKKLRVNINVPMKTEQKQEQETTHKNIEEDRKLLIQAAIVRIMKMRKVLKHQQLLGEVLTQLSSRFKPRVPVIKKCIDILIEKEYLERVDGEKDTYSYLA DIP protein Q13616 original sequence version: 144 DIP protein Q13616 original sequence version: 133 DIP protein Q13616 original sequence version: null DIP protein Q13616 original sequence version: 135 DIP protein Q13616 original sequence version: 98 DIP protein Q13616 original sequence version: 110 DIP protein Q13616 original sequence version: 146 DIP protein Q13616 original sequence version: 148 DIP protein Q13616 original sequence version: 100 DIP protein Q13616 original sequence version: 85 DIP protein Q13616 original sequence version: 114 DIP protein Q13616 original sequence version: 119 DIP protein Q13616 original sequence version: 136 DIP protein Q13616 original sequence version: 117 DIP protein Q13616 original sequence version: 99 DIP protein Q13616 original sequence version: 108 6625A1FFA7799BBA ubc12_human NEDD8-conjugating enzyme Ubc12 UBE2M UBC12 Ubiquitin-conjugating enzyme E2 M NEDD8 carrier protein protein protein human Homo sapiens Human MIKLFSLKQQKKEEESAGGTKGSSKKASAAQLRIQKDINELNLPKTCDISFSDPDDLLNFKLVICPDEGFYKSGKFVFSFKVGQGYPHDPPKVKCETMVYHPNIDLEGNVCLNILREDWKPVLTINSIIYGLQYLFLEPNPEDPLNKEAAEVLQNNRRLFEQNVQRSMRGGYIGSTYFERCLK DIP protein P61081 original sequence version: 108 DIP protein P61081 original sequence version: 84 DIP protein P61081 original sequence version: 106 E3C288CA6A98BC5C rbx1_human E3 ubiquitin-protein ligase RBX1 RBX1 RNF75 ROC1 Regulator of cullins 1 RING finger protein 75 Protein ZYP RING-box protein 1 E3 ubiquitin-protein transferase RBX1 protein protein human Homo sapiens Human MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH DIP protein P62877 original sequence version: 120 DIP protein P62877 original sequence version: 115 DIP protein P62877 original sequence version: 78 DIP protein P62877 original sequence version: 113 DIP protein P62877 original sequence version: 75 DIP protein P62877 original sequence version: 86 DIP protein P62877 original sequence version: 136 DIP protein P62877 original sequence version: 126 DIP protein P62877 original sequence version: 90 DIP protein P62877 original sequence version: 114 30FC5ADF66096C0E nedd8_human NEDD8 Ubiquitin-like protein Nedd8 Neddylin Neural precursor cell expressed developmentally down-regulated protein 8 NEDD8 protein protein human Homo sapiens Human MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIYSGKQMNDEKTAADYKILGGSVLHLVLALRGGGGLRQ DIP protein Q15843 original sequence version: 103 DIP protein Q15843 original sequence version: 149 DIP protein Q15843 original sequence version: 58 DIP protein Q15843 original sequence version: 124 DIP protein Q15843 original sequence version: 95 DIP protein Q15843 original sequence version: 111 DC2FE102BE4725D2 cul1-rbx1-17 6 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 411-776 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction cul1-ubc12-1 4 8 unspecified role unspecified role unspecified role unspecified role P52491:p.Asn146Cys N146C mutation mutation certain certain sequence position certain certain certain sequence position certain N C This feature has been corrected as a result of our quality control procedures. The original label was 'N146C'. Wed May 02 18:23:13 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn146cys' Tue Jun 30 18:33:03 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asn146Cys' ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role Q13616:p.Arg717Cys R717C mutation mutation certain certain sequence position certain certain certain sequence position certain R C This feature has been corrected as a result of our quality control procedures. The original label was 'R717C'. Wed May 02 20:25:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg717cys' Tue Jun 30 19:02:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg717Cys' C-terminal domain Region 411-776 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction nedd8-ube2m-1 5 10 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction cul1-ubc12-2 1 8 unspecified role unspecified role unspecified role unspecified role P52491:p.Glu121Cys E121C mutation mutation certain certain sequence position certain certain certain sequence position certain E C This feature has been corrected as a result of our quality control procedures. The original label was 'E121C'. Wed May 02 17:10:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu121cys' Tue Jun 30 17:01:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu121Cys' ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role Q13616:p.Arg717Cys R717C mutation mutation certain certain sequence position certain certain certain sequence position certain R C This feature has been corrected as a result of our quality control procedures. The original label was 'R717C'. Wed May 02 17:56:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg717cys' Tue Jun 30 17:34:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg717Cys' C-terminal domain Region 411-776 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction cul1-rbx1-18 7 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 411-776 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction cul1-nedd8-5 2 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 411-776 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction rbx1-ube2m-3 3 10 unspecified role unspecified role unspecified role unspecified role Core domain Region 27-183 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role RING domain Region 36-108 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction