DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. Structure (London, England : 1993) 2012 imex curation Zanier K., ould M'hamed ould Sidi A., Boulade-Ladame C., Rybin V., Chappelle A., Atkinson A., Kieffer B., Travé G. Only protein-protein interactions in vitro In vitro pull down pull down autoradiography autoradiography Zanier K., ould M'hamed ould Sidi A., Boulade-Ladame C., Rybin V., Chappelle A., Atkinson A., Kieffer B., Travé G. DIP original experiment: DIP-249309X Structure (London, England : 1993) 2012 IMEx Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. Structure (London, England : 1993) 2012 imex curation Zanier K., ould M'hamed ould Sidi A., Boulade-Ladame C., Rybin V., Chappelle A., Atkinson A., Kieffer B., Travé G. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Zanier K., ould M'hamed ould Sidi A., Boulade-Ladame C., Rybin V., Chappelle A., Atkinson A., Kieffer B., Travé G. DIP original experiment: DIP-249307X Structure (London, England : 1993) 2012 IMEx Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. Structure (London, England : 1993) 2012 imex curation Zanier K., ould M'hamed ould Sidi A., Boulade-Ladame C., Rybin V., Chappelle A., Atkinson A., Kieffer B., Travé G. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Zanier K., ould M'hamed ould Sidi A., Boulade-Ladame C., Rybin V., Chappelle A., Atkinson A., Kieffer B., Travé G. DIP original experiment: DIP-249308X Structure (London, England : 1993) 2012 IMEx Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. Structure (London, England : 1993) 2012 imex curation Zanier K., ould M'hamed ould Sidi A., Boulade-Ladame C., Rybin V., Chappelle A., Atkinson A., Kieffer B., Travé G. Only protein-protein interactions ecolx Escherichia coli nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Zanier K., ould M'hamed ould Sidi A., Boulade-Ladame C., Rybin V., Chappelle A., Atkinson A., Kieffer B., Travé G. DIP original experiment: DIP-249306X Structure (London, England : 1993) 2012 IMEx Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. Structure (London, England : 1993) 2012 imex curation Zanier K., ould M'hamed ould Sidi A., Boulade-Ladame C., Rybin V., Chappelle A., Atkinson A., Kieffer B., Travé G. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Zanier K., ould M'hamed ould Sidi A., Boulade-Ladame C., Rybin V., Chappelle A., Atkinson A., Kieffer B., Travé G. DIP original experiment: DIP-249305X Structure (London, England : 1993) 2012 IMEx Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. ube3a_human Ubiquitin-protein ligase E3A E6AP ubiquitin-protein ligase Oncogenic protein-associated protein E6-AP Human papillomavirus E6-associated protein Renal carcinoma antigen NY-REN-54 UBE3A E6AP EPVE6AP HPVE6A HECT-type ubiquitin transferase E3A protein protein human Homo sapiens Human MEKLHQCYWKSGEPQSDDIEASRMKRAAAKHLIERYYHQLTEGCGNEACTNEFCASCPTFLRMDNNAAAIKALELYKINAKLCDPHPSKKGASSAYLENSKGAPNNSCSEIKMNKKGARIDFKDVTYLTEEKVYEILELCREREDYSPLIRVIGRVFSSAEALVQSFRKVKQHTKEELKSLQAKDEDKDEDEKEKAACSAAAMEEDSEASSSRIGDSSQGDNNLQKLGPDDVSVDIDAIRRVYTRLLSNEKIETAFLNALVYLSPNVECDLTYHNVYSRDPNYLNLFIIVMENRNLHSPEYLEMALPLFCKAMSKLPLAAQGKLIRLWSKYNADQIRRMMETFQQLITYKVISNEFNSRNLVNDDDAIVAASKCLKMVYYANVVGGEVDTNHNEEDDEEPIPESSELTLQELLGEERRNKKGPRVDPLETELGVKTLDCRKPLIPFEEFINEPLNEVLEMDKDYTFFKVETENKFSFMTCPFILNAVTKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALVRLEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKLFWFNPSSFETEGQFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNVEDDMMITFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKLKMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGML DIP protein Q05086 original sequence version: 159 DIP protein Q05086-1 original sequence version: 165 DIP protein Q05086-1 original sequence version: 127 F80F0502B3B3838A ve6_hpv18 Protein E6 E6 protein protein hpv18 Human papillomavirus type 18 MARFEDPTRRPYKLPDLCTELNTSLQDIEITCVYCKTVLELTEVFEFAFKDLFVVYRDSIPHAACHKCIDFYSRIRELRHYSDSVYGDTLEKLTNTGLYNLLIRCLRCQKPLNPAEKLRHLNEKRRFHNIAGHYRGQCHSCCNRARQERLQRRRETQV DIP protein P06463 original sequence version: 80 5BCF13CF43D157FA ve6_hpv16 Protein E6 E6 protein protein hpv16 Human papillomavirus type 16 MHQKRTAMFQDPQERPRKLPQLCTELQTTIHDIILECVYCKQQLLRREVYDFAFRDLCIVYRDGNPYAVCDKCLKFYSKISEYRHYCYSLYGTTLEQQYNKPLCDLLIRCINCQKPLCPEEKQRHLDKKQRFHNIRGRWTGRCMSCCRSSRTRRETQL DIP protein P03126 original sequence version: 77 DIP protein P03126 original sequence version: 112 DIP protein P03126 original sequence version: 116 DIP protein P03126 original sequence version: 89 01FEF5ADCFDB37EB b9upe7_hpv11 Protein E6 E6 protein protein hpv11 Human papillomavirus type 11 MESKDASTSATSIDQLCKTFNLSLHTLQIQCVFCRNALTTAEIYAYAYKNLKVVWRDNFPFAACACCLELQGKINQYRHFNYAAYAPTVEEETNEDILKVLIRCYLCHKPLCEIEKLKHILGKARFIKLNNQWKGRCLHCWTTCMEDLLP DIP protein B9UPE7 original sequence version: 14 e6-11 2 7 unspecified role unspecified role unspecified role unspecified role Region 1-82 Region 1-82 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 e6-5 5 8 unspecified role unspecified role unspecified role unspecified role Region 8-87 Region 8-87 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P03126:p.Phe54Arg F54R 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 F R This feature has been corrected as a result of our quality control procedures. The original label was 'F54R'. Wed May 02 17:07:54 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe54arg' Tue Jun 30 17:45:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe54Arg' P03126:p.Tyr50Arg Y50R/E 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 Y R Wed May 02 17:06:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr50arg' Tue Jun 30 19:01:49 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr50Arg' P03126:p.His31Ala H31A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain H A This feature has been corrected as a result of our quality control procedures. The original label was 'H31A'. Wed May 02 17:59:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his31ala' Tue Jun 30 19:30:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.His31Ala' P03126:p.Asp51Arg D51R 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 D R This feature has been corrected as a result of our quality control procedures. The original label was 'D51R'. Wed May 02 14:25:30 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp51arg' Tue Jun 30 17:44:26 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp51Arg' P03126:p.Asp51Ala D51A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain D A This feature has been corrected as a result of our quality control procedures. The original label was 'D51A'. Wed May 02 15:56:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp51ala' Tue Jun 30 20:24:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp51Ala' P03126:p.Tyr50Glu mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain Y E Wed May 02 17:44:25 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr50glu' Tue Jun 30 16:50:17 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr50Glu' ecolx Escherichia coli direct interaction direct interaction e6-6 3 9 unspecified role unspecified role unspecified role unspecified role Region 1-81 Region 1-81 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 ube3a-e6-7 1 8 unspecified role unspecified role prey prey 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 6 unspecified role unspecified role bait bait Region 401-418 Region 401-418 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain 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 e6-7 4 8 unspecified role unspecified role unspecified role unspecified role Region 8-87 Region 8-87 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P03126:p.Phe54Arg F54R 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 F R This feature has been corrected as a result of our quality control procedures. The original label was 'F54R'. Wed May 02 19:56:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe54arg' Tue Jun 30 15:35:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe54Arg' ecolx Escherichia coli direct interaction direct interaction