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 Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature structural & molecular biology 2010 imex curation Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. Only protein-protein interactions ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. DIP original experiment: DIP-217679X Nature structural & molecular biology 2010 IMEx The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature structural & molecular biology 2010 imex curation Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. Only protein-protein interactions human Homo sapiens Human fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. DIP original experiment: DIP-217683X Nature structural & molecular biology 2010 IMEx The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature structural & molecular biology 2010 imex curation Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. Only protein-protein interactions human Homo sapiens Human fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. DIP original experiment: DIP-217682X Nature structural & molecular biology 2010 IMEx The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature structural & molecular biology 2010 imex curation Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. Only protein-protein interactions ecolx Escherichia coli tem transmission electron microscopy tem predetermined predetermined participant predetermined Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. DIP original experiment: DIP-217674X Nature structural & molecular biology 2010 IMEx The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature structural & molecular biology 2010 imex curation Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. 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 Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. DIP original experiment: DIP-217677X Nature structural & molecular biology 2010 IMEx The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature structural & molecular biology 2010 imex curation Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. Only protein-protein interactions ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. DIP original experiment: DIP-217672X Nature structural & molecular biology 2010 IMEx The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature structural & molecular biology 2010 imex curation Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. Only protein-protein interactions ecolx Escherichia coli ms of complexes mass spectrometry studies of complexes ms of complexes predetermined predetermined participant predetermined Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. DIP original experiment: DIP-217673X Nature structural & molecular biology 2010 IMEx The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature structural & molecular biology 2010 imex curation Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. DIP original experiment: DIP-217684X Nature structural & molecular biology 2010 IMEx The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature structural & molecular biology 2010 imex curation Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. Only protein-protein interactions ecolx Escherichia coli tem transmission electron microscopy tem predetermined predetermined participant predetermined Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. DIP original experiment: DIP-217681X Nature structural & molecular biology 2010 IMEx The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature structural & molecular biology 2010 imex curation Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. DIP original experiment: DIP-217678X Nature structural & molecular biology 2010 IMEx The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature structural & molecular biology 2010 imex curation Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. Only protein-protein interactions ecolx Escherichia coli ms of complexes mass spectrometry studies of complexes ms of complexes predetermined predetermined participant predetermined Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. DIP original experiment: DIP-217680X Nature structural & molecular biology 2010 IMEx The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature structural & molecular biology 2010 imex curation Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. 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 Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. DIP original experiment: DIP-217671X Nature structural & molecular biology 2010 IMEx The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature structural & molecular biology 2010 imex curation Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. Only protein-protein interactions ecolx Escherichia coli pull down pull down weight by staining molecular weight estimation by staining weight by staining Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. DIP original experiment: DIP-217676X Nature structural & molecular biology 2010 IMEx The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature structural & molecular biology 2010 imex curation Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. Only protein-protein interactions ecolx Escherichia coli pull down pull down weight by staining molecular weight estimation by staining weight by staining Wang L., Yang JK., Kabaleeswaran V., Rice AJ., Cruz AC., Park AY., Yin Q., Damko E., Jang SB., Raunser S., Robinson CV., Siegel RM., Walz T., Wu H. DIP original experiment: DIP-217675X Nature structural & molecular biology 2010 IMEx The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. fadd_human FAS-associated death domain protein FAS-associating death domain-containing protein Mediator of receptor induced toxicity FADD MORT1 GIG3 Growth-inhibiting gene 3 protein protein protein human Homo sapiens Human MDPFLVLLHSVSSSLSSSELTELKFLCLGRVGKRKLERVQSGLDLFSMLLEQNDLEPGHTELLRELLASLRRHDLLRRVDDFEAGAAAGAAPGEEDLCAAFNVICDNVGKDWRRLARQLKVSDTKIDSIEDRYPRNLTERVRESLRIWKNTEKENATVAHLVGALRSCQMNLVADLVQEVQQARDLQNRSGAMSPMSWNSDASTSEAS DIP protein Q13158 original sequence version: 155 DIP protein Q13158 original sequence version: 130 DIP protein Q13158 original sequence version: 110 DIP protein Q13158 original sequence version: 118 DIP protein Q13158 original sequence version: 141 DIP protein Q13158 original sequence version: 166 0E65E2F852E83507 tnr6_mouse Tumor necrosis factor receptor superfamily member 6 Fas Apt1 Tnfrsf6 FASLG receptor Apoptosis-mediating surface antigen FAS Apo-1 antigen protein protein mouse Mus musculus Mouse MLWIWAVLPLVLAGSQLRVHTQGTNSISESLKLRRRVRETDKNCSEGLYQGGPFCCQPCQPGKKKVEDCKMNGGTPTCAPCTEGKEYMDKNHYADKCRRCTLCDEEHGLEVETNCTLTQNTKCKCKPDFYCDSPGCEHCVRCASCEHGTLEPCTATSNTNCRKQSPRNRLWLLTILVLLIPLVFIYRKYRKRKCWKRRQDDPESRTSSRETIPMNASNLSLSKYIPRIAEDMTIQEAKKFARENNIKEGKIDEIMHDSIQDTAEQKVQLLLCWYQSHGKSDAYQDLIKGLKKAECRRTLDKFQDMVQKDLGKSTPDTGNENEGQCLE DIP protein P25446 original sequence version: 112 D8DA95CA525CED56 p25445-1 Tumor necrosis factor receptor superfamily member 6 FAS APT1 FAS1 TNFRSF6 Apo-1 antigen Apoptosis-mediating surface antigen FAS FASLG receptor protein protein human Homo sapiens Human MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLEGLHHDGQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSNLGWLCLLLLPIPLIVWVKRKEVQKTCRKHRKENQGSHESPTLNPETVAINLSDVDLSKYITTIAGVMTLSQVKGFVRKNGVNEAKIDEIKNDNVQDTAEQKVQLLRNWHQLHGKKEAYDTLIKDLKKANLCTLAEKIQTIILKDITSDSENSNFRNEIQSLV DIP protein P25445-1 original sequence version: 126 DIP protein P25445 original sequence version: 149 DIP protein P25445-1 original sequence version: 145 DIP protein P25445 original sequence version: 153 DIP protein P25445-1 original sequence version: 153 DIP protein P25445 original sequence version: 152 DIP protein P25445-1 original sequence version: 204 DIP protein P25445 original sequence version: 176 fadd-fas-8 8 16 unspecified role unspecified role unspecified role unspecified role Death domain Region 210-310 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role Death domain Region 93-184 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fadd-fas-9 12 15 unspecified role unspecified role unspecified role unspecified role Death domain Region 93-191 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Death domain Region 218-318 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fadd-fas-10 14 15 unspecified role unspecified role bait bait Death domain Region 93-191 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecolx Escherichia coli 17 unspecified role unspecified role prey prey Death domain Region 218-318 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P25445-1:p.Glu261Lys E261K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain E K This feature has been corrected as a result of our quality control procedures. The original label was 'E261K'. Wed May 02 16:46:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu261lys' Tue Jun 30 15:43:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu261Lys' P25445-1:p.Glu272Lys E272K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain E K This feature has been corrected as a result of our quality control procedures. The original label was 'E272K'. Wed May 02 15:22:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu272lys' Tue Jun 30 16:35:34 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu272Lys' P25445-1:p.Thr270Lys T270K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain T K This feature has been corrected as a result of our quality control procedures. The original label was 'T270K'. Wed May 02 18:43:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr270lys' Tue Jun 30 18:19:20 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr270Lys' P25445-1:p.Arg250Glu R250E/Q mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R E Wed May 02 17:52:56 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg250glu' Tue Jun 30 18:12:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg250Glu' P25445-1:p.Gln283Lys Q283K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Q K This feature has been corrected as a result of our quality control procedures. The original label was 'Q283K'. Wed May 02 19:51:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln283lys' Tue Jun 30 18:41:09 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln283Lys' P25445-1:p.Lys287Asp K287D mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K D This feature has been corrected as a result of our quality control procedures. The original label was 'K287D'. Wed May 02 16:52:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys287asp' Tue Jun 30 17:13:20 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys287Asp' P25445-1:p.Asp260Tyr D260Y mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain D Y This feature has been corrected as a result of our quality control procedures. The original label was 'D260Y'. Wed May 02 18:32:34 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp260tyr' Tue Jun 30 17:28:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp260Tyr' P25445-1:p.Ala257Asp A257D mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain A D This feature has been corrected as a result of our quality control procedures. The original label was 'A257D'. Wed May 02 20:14:46 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala257asp' Tue Jun 30 18:15:16 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala257Asp' P25445-1:p.Arg250Gln mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain R Q Wed May 02 19:45:47 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg250gln' Tue Jun 30 17:43:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg250Gln' P25445-1:p.Arg250Glu mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain R E Wed May 02 19:50:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg250glu' Tue Jun 30 20:20:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg250Glu' ecolx Escherichia coli physical association physical association fadd-fas-11 9 16 unspecified role unspecified role unspecified role unspecified role Death domain Region 210-310 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role Death domain Region 93-184 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fadd-fas-12 5 16 unspecified role unspecified role unspecified role unspecified role Death domain Region 210-310 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role Death domain Region 93-184 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fadd-fas-13 6 15 unspecified role unspecified role unspecified role unspecified role Death domain Region 93-191 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Death domain Region 218-318 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fadd-fas-14 3 15 unspecified role unspecified role fluorescence donor fluorescence donor CFP-tag CFP-tag cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range Death domain Region 93-208 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 17 unspecified role unspecified role fluorescence accept fluorescence acceptor fluorescence accept YFP-tag YFP-tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range P25445-1:p.Asp260Tyr D260Y/V mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain D Y Wed May 02 15:02:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp260tyr' Tue Jun 30 19:18:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp260Tyr' P25445-1:p.Ala257Asp A257D mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain A D This feature has been corrected as a result of our quality control procedures. The original label was 'A257D'. Wed May 02 19:22:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala257asp' Tue Jun 30 19:45:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala257Asp' P25445-1:p.Glu261Lys E261K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain E K This feature has been corrected as a result of our quality control procedures. The original label was 'E261K'. Wed May 02 17:29:07 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu261lys' Tue Jun 30 15:56:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu261Lys' P25445-1:p.Arg250Glu R250E mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R250E'. Wed May 02 18:44:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg250glu' Tue Jun 30 19:17:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg250Glu' P25445-1:p.Thr270Lys T270K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain T K This feature has been corrected as a result of our quality control procedures. The original label was 'T270K'. Wed May 02 18:27:57 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr270lys' Tue Jun 30 18:11:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr270Lys' P25445-1:p.Glu272Lys E272K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain E K This feature has been corrected as a result of our quality control procedures. The original label was 'E272K'. Wed May 02 19:11:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu272lys' Tue Jun 30 19:28:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu272Lys' P25445-1:p.Gln283Lys Q283K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Q K This feature has been corrected as a result of our quality control procedures. The original label was 'Q283K'. Wed May 02 14:54:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln283lys' Tue Jun 30 18:01:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln283Lys' P25445-1:p.Asp260Val mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain D V Wed May 02 18:56:54 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp260val' Tue Jun 30 16:41:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp260Val' human Homo sapiens Human direct interaction direct interaction fas-fadd-3 10 16 unspecified role unspecified role bait bait Death domain Region 210-310 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 unspecified role unspecified role prey prey Death domain Region 93-184 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecolx Escherichia coli physical association physical association fadd-fas-15 7 15 unspecified role unspecified role unspecified role unspecified role Death domain Region 93-191 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Death domain Region 218-318 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fadd-fas-16 13 15 unspecified role unspecified role bait bait Death domain Region 93-191 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range Q13158:p.Arg117Glu R117E mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R117E'. Wed May 02 20:28:38 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg117glu' Tue Jun 30 19:11:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg117Glu' Q13158:p.Asp123Arg D123R mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation 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 'D123R'. Wed May 02 16:04:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp123arg' Tue Jun 30 16:49:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp123Arg' Q13158:p.Arg135Glu R135E mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R135E'. Wed May 02 15:20:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg135glu' Tue Jun 30 15:47:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg135Glu' Q13158:p.Arg142Glu R142E mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R142E'. Wed May 02 17:46:18 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg142glu' Tue Jun 30 19:39:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg142Glu' Q13158:p.Leu172Lys L172K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain L K This feature has been corrected as a result of our quality control procedures. The original label was 'L172K'. Wed May 02 18:48:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu172lys' Tue Jun 30 20:04:06 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu172Lys' Q13158:p.Asp175Lys D175K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain D K This feature has been corrected as a result of our quality control procedures. The original label was 'D175K'. Wed May 02 16:58:26 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp175lys' Tue Jun 30 19:49:30 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp175Lys' ecolx Escherichia coli 17 unspecified role unspecified role prey prey Death domain Region 218-318 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association fadd-fas-17 1 16 unspecified role unspecified role unspecified role unspecified role Death domain Region 210-310 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role Death domain Region 93-184 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fadd-fas-18 4 15 unspecified role unspecified role unspecified role unspecified role Death domain Region 93-191 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Death domain Region 218-318 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fadd-fas-19 2 15 unspecified role unspecified role fluorescence donor fluorescence donor CFP-tag CFP-tag cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range Death domain Region 93-208 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q13158:p.Arg117Glu R117E mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R117E'. Wed May 02 20:15:42 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg117glu' Tue Jun 30 19:11:16 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg117Glu' Q13158:p.Leu172Glu L172E mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain L E This feature has been corrected as a result of our quality control procedures. The original label was 'L172E'. Wed May 02 20:05:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu172glu' Tue Jun 30 16:59:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu172Glu' Q13158:p.Asp123Arg D123R mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation 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 'D123R'. Wed May 02 17:50:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp123arg' Tue Jun 30 17:26:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp123Arg' Q13158:p.Arg135Glu R135E mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R135E'. Wed May 02 14:33:39 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg135glu' Tue Jun 30 17:54:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg135Glu' Q13158:p.Arg142Glu R142E mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R142E'. Wed May 02 15:33:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg142glu' Tue Jun 30 19:21:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg142Glu' Q13158:p.Lys153Glu K153E mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K153E'. Wed May 02 17:45:34 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys153glu' Tue Jun 30 18:24:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys153Glu' human Homo sapiens Human 17 unspecified role unspecified role fluorescence accept fluorescence acceptor fluorescence accept YFP-tag YFP-tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range human Homo sapiens Human direct interaction direct interaction fadd-fas-20 11 16 unspecified role unspecified role unspecified role unspecified role Death domain Region 210-310 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role Death domain Region 93-184 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction