DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 2011 imex curation Wenzel DM., Lissounov A., Brzovic PS., Klevit RE. Only protein-protein interactions in vitro In vitro comigration in sds comigration in sds page comigration in sds predetermined predetermined participant predetermined Wenzel DM., Lissounov A., Brzovic PS., Klevit RE. DIP original experiment: DIP-219045X Nature 2011 IMEx UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 2011 imex curation Wenzel DM., Lissounov A., Brzovic PS., Klevit RE. Only protein-protein interactions in vitro In vitro comigration in sds comigration in sds page comigration in sds predetermined predetermined participant predetermined Wenzel DM., Lissounov A., Brzovic PS., Klevit RE. DIP original experiment: DIP-219046X Nature 2011 IMEx UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 2011 imex curation Wenzel DM., Lissounov A., Brzovic PS., Klevit RE. Only protein-protein interactions in vitro In vitro comigration in sds comigration in sds page comigration in sds predetermined predetermined participant predetermined Wenzel DM., Lissounov A., Brzovic PS., Klevit RE. DIP original experiment: DIP-219043X Nature 2011 IMEx UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 2011 imex curation Wenzel DM., Lissounov A., Brzovic PS., Klevit RE. Only protein-protein interactions in vitro In vitro pull down pull down anti tag western anti tag western blot anti tag western Wenzel DM., Lissounov A., Brzovic PS., Klevit RE. DIP original experiment: DIP-219042X Nature 2011 IMEx UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 2011 imex curation Wenzel DM., Lissounov A., Brzovic PS., Klevit RE. Only protein-protein interactions in vitro In vitro comigration in sds comigration in sds page comigration in sds predetermined predetermined participant predetermined Wenzel DM., Lissounov A., Brzovic PS., Klevit RE. DIP original experiment: DIP-219044X Nature 2011 IMEx UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. ubiq_human UBIQ_HUMAN protein protein human Homo sapiens Human MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG p68036-1 Ubiquitin-conjugating enzyme E2 L3 E2 ubiquitin-conjugating enzyme L3 L-UBC UbcH7 Ubiquitin carrier protein L3 Ubiquitin-conjugating enzyme E2-F1 Ubiquitin-protein ligase L3 UBE2L3 UBCE7 UBCH7 protein protein human Homo sapiens Human MAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINFPAEYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAENWKPATKTDQVIQSLIALVNDPQPEHPLRADLAEEYSKDRKKFCKNAEEFTKKYGEKRPVD DIP protein P68036-1 original sequence version: 102 DIP protein P68036 original sequence version: 98 DIP protein P68036 original sequence version: 48 DIP protein P68036 original sequence version: 103 DIP protein P68036 original sequence version: 77 DIP protein P68036-1 original sequence version: 109 ari1_human E3 ubiquitin-protein ligase ARIH1 Protein ariadne-1 homolog ARIH1 ARI MOP6 UBCH7BP Ubiquitin-conjugating enzyme E2-binding protein 1 UbcH7-binding protein UbcM4-interacting protein HHARI H7-AP2 Monocyte protein 6 HUSSY-27 protein protein human Homo sapiens Human MDSDEGYNYEFDEDEECSEEDSGAEEEEDEDDDEPDDDTLDLGEVELVEPGLGVGGERDGLLCGETGGGGGSALGPGGGGGGGGGGGGGGPGHEQEEDYRYEVLTAEQILQHMVECIREVNEVIQNPATITRILLSHFNWDKEKLMERYFDGNLEKLFAECHVINPSKKSRTRQMNTRSSAQDMPCQICYLNYPNSYFTGLECGHKFCMQCWSEYLTTKIMEEGMGQTISCPAHGCDILVDDNTVMRLITDSKVKLKYQHLITNSFVECNRLLKWCPAPDCHHVVKVQYPDAKPVRCKCGRQFCFNCGENWHDPVKCKWLKKWIKKCDDDSETSNWIAANTKECPKCHVTIEKDGGCNHMVCRNQNCKAEFCWVCLGPWEPHGSAWYNCNRYNEDDAKAARDAQERSRAALQRYLFYCNRYMNHMQSLRFEHKLYAQVKQKMEEMQQHNMSWIEVQFLKKAVDVLCQCRATLMYTYVFAFYLKKNNQSIIFENNQADLENATEVLSGYLERDISQDSLQDIKQKVQDKYRYCESRRRVLLQHVHEGYEKDLWEYIED DIP protein Q9Y4X5 original sequence version: 122 DIP protein Q9Y4X5 original sequence version: 103 DFFF8965DAB41DC8 q9jk66-1 E3 ubiquitin-protein ligase parkin Prkn Park2 Parkin RBR E3 ubiquitin-protein ligase protein protein rat Rattus norvegicus (Rat) Rat MIVFVRFNSSYGFPVEVDSDTSIFQLKEVVAKRQGVPADQLRVIFAGKELQNHLTVQNCDLEQQSIVHIVQRPQRKSHETNASGGDKPQSTPEGSIWEPRSLTRVDLSSHILPADSVGLAVILDTDSKSDSEAARGPEAKPTYHSFFVYCKGPCHKVQPGKLRVQCGTCRQATLTLAQGPSCWDDVLIPNRMSGECQSPDCPGTRAEFFFKCGAHPTSDKDTSVALNLITNNSRSIPCIACTDVRNPVLVFQCNHRHVICLDCFHLYCVTRLNDRQFVHDAQLGYSLPCVAGCPNSLIKELHHFRILGEEQYNRYQQYGAEECVLQMGGVLCPRPGCGAGLLPEQGQKKVTCEGGNGLGCGFVFCRDCKEAYHEGECDSMFEASGATSQAYRVDQRAAEQARWEEASKETIKKTTKPCPRCNVPIEKNGGCMHMKCPQPQCKLEWCWNCGCEWNRACMGDHWFDV DIP protein Q9JK66-1 original sequence version: 79 q05086-2 Ubiquitin-protein ligase E3A E6AP E6AP ubiquitin-protein ligase EPVE6AP HPVE6A Human papillomavirus E6-associated protein Oncogenic protein-associated protein E6-AP Renal carcinoma antigen NY-REN-54 UBE3A HECT-type ubiquitin transferase E3A protein protein human Homo sapiens Human MKRAAAKHLIERYYHQLTEGCGNEACTNEFCASCPTFLRMDNNAAAIKALELYKINAKLCDPHPSKKGASSAYLENSKGAPNNSCSEIKMNKKGARIDFKDVTYLTEEKVYEILELCREREDYSPLIRVIGRVFSSAEALVQSFRKVKQHTKEELKSLQAKDEDKDEDEKEKAACSAAAMEEDSEASSSRIGDSSQGDNNLQKLGPDDVSVDIDAIRRVYTRLLSNEKIETAFLNALVYLSPNVECDLTYHNVYSRDPNYLNLFIIVMENRNLHSPEYLEMALPLFCKAMSKLPLAAQGKLIRLWSKYNADQIRRMMETFQQLITYKVISNEFNSRNLVNDDDAIVAASKCLKMVYYANVVGGEVDTNHNEEDDEEPIPESSELTLQELLGEERRNKKGPRVDPLETELGVKTLDCRKPLIPFEEFINEPLNEVLEMDKDYTFFKVETENKFSFMTCPFILNAVTKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALVRLEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKLFWFNPSSFETEGQFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNVEDDMMITFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKLKMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGML Variant in position: 212:D->V (in AS, unknown pathological significance). Variant in position: 237:L->Q (in AS, unknown pathological significance). Variant in position: 263:L->W (in AS, unknown pathological significance). Variant in position: 458:P->L (in AS, unknown pathological significance). Variant in position: 545:G->R (in AS, unknown pathological significance). Variant in position: 584:E->Q (in AS, unknown pathological significance). Variant in position: 656:T->I (in AS, unknown pathological significance). Variant in position: 690:F->C (in AS, unknown pathological significance). Variant in position: 827:P->L (in AS, unknown pathological significance). Variant in position: 106:T->K (in AS, unknown pathological significance). Variant in position: 237:L->H (in AS, unknown pathological significance). Variant in position: 435:L->P (in AS, unknown pathological significance). Variant in position: 477:R->P (in AS, unknown pathological significance). Variant in position: 566:M->K (in AS, unknown pathological significance). Variant in position: 117:C->R (common polymorphism, may be associated with AS). Variant in position: 270:N->T (common polymorphism, may be associated with AS). Variant in position: 762:V->I (common polymorphism, may be associated with AS). Variant in position: 133:V->G (common polymorphism, may be associated with AS). Variant in position: 335:S->T (common polymorphism, may be associated with AS). Variant in position: 478:M->I (common polymorphism, may be associated with AS). Variant in position: 588:Q->E (common polymorphism, may be associated with AS). Variant in position: 588:Q->P (common polymorphism, may be associated with AS). Variant in position: 673:L->R (common polymorphism, may be associated with AS). DIP protein Q05086-2 original sequence version: 140 DIP protein Q05086-2 original sequence version: 118 3C061DA8D216055A ub-ube3a-1 2 10 unspecified role unspecified role unspecified role unspecified role Hect domain Region 495-852 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction arih1-ube2l3-3 4 7 unspecified role unspecified role prey prey T7-tag T7-tag t7 tag t7 tag MASMTGGQQMG epitope tag MASMTGGQQMG epitope 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 bait bait Ring1-IBR domain Region 177-316 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q9Y4X5:p.Ile188Ala I188A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain I A This feature has been corrected as a result of our quality control procedures. The original label was 'I188A'. Wed May 02 16:26:47 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile188ala' Tue Jun 30 19:12:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile188Ala' GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst 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 park2-ub-1 5 9 unspecified role unspecified role unspecified role unspecified role Ring1/2-IBR domain region 217-465 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q9JK66-1:p.Cys431Ser C431S mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain C S This feature has been corrected as a result of our quality control procedures. The original label was 'C431S'. Wed May 02 19:14:01 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys431ser' Tue Jun 30 19:16:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys431Ser' ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction arih1-ub-1 3 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role Ring1/2-IBR domain Region 177-393 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q9Y4X5:p.Cys367Ser C367S mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain C S This feature has been corrected as a result of our quality control procedures. The original label was 'C367S'. Wed May 02 17:27:47 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys367ser' Tue Jun 30 18:15:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys367Ser' Q9Y4X5:p.Cys372Ser C372S mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain C S This feature has been corrected as a result of our quality control procedures. The original label was 'C372S'. Wed May 02 16:29:13 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys372ser' Tue Jun 30 17:25:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys372Ser' ecolx Escherichia coli direct interaction direct interaction ub-ube2l3-2 1 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction