DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA. Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA. Proceedings of the National Academy of Sciences of the United States of America 2012 imex curation Ma J., Edlich F., Bermejo GA., Norris KL., Youle RJ., Tjandra N. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Ma J., Edlich F., Bermejo GA., Norris KL., Youle RJ., Tjandra N. DIP original experiment: DIP-251861X Proceedings of the National Academy of Sciences of the United States of America 2012 IMEx Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA. Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA. Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA. Proceedings of the National Academy of Sciences of the United States of America 2012 imex curation Ma J., Edlich F., Bermejo GA., Norris KL., Youle RJ., Tjandra N. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Ma J., Edlich F., Bermejo GA., Norris KL., Youle RJ., Tjandra N. DIP original experiment: DIP-251860X Proceedings of the National Academy of Sciences of the United States of America 2012 IMEx Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA. vgli_hcmva UL37 immediate early glycoprotein UL37 protein protein hcmva Human cytomegalovirus (strain AD169) (HHV-5) Human herpesvirus 5 HHV-5 MSPVYVNLLGSVGLLAFWYFSYRWIQRKRLEDPLPPWLRKKKACALTRRSRHRLRRQHGVIDGENSETERSVDLVAALLAEAGEESVTEDTEREDTEEEREDEEEENEARTPEVNPIDAEGLSGLAREACEALKKALRRHRFLWQRRQRARMLQHNGPQQSHHAAVFCRVHGLRGFQVSVWLLLTLLWSTGHGVSVRCTYHGTDVNRTSNTTSMNCHLNCTRNHTQIYNGPCLGTEARLPLNVTFNQSRRKWHSVMLKFGFQYHLEGWFPLRVLNESREINVTEVHGEVACFRNDTNVTVGQLTLNFTGHSYVLRAIAHTSPFESYVRWEETNVTDNATSSENTTTVMSTLTKYAESDYIFLQDMCPRFLKRTVKLTRNKTKHNVTVTGNNMTTLPVWTPECKGWTYWTTLSVMWRNRRSALLRAKSRALGHWALLSICTVAAGSIALLSLFCILLIGLRRDLLEDFRYICRDEGSSSTKNDVHRIV DIP protein P16778 original sequence version: 55 bax_human Apoptosis regulator BAX BAX BCL2L4 Bcl-2-like protein 4 protein protein human Homo sapiens Human MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLSECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKLVLKALCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG DIP protein Q07812 original sequence version: 73 DIP protein Q07812 original sequence version: 156 DIP protein Q07812 original sequence version: 92 DIP protein Q07812 original sequence version: 94 DIP protein Q07812-1 original sequence version: 93 DIP protein Q07812 original sequence version: 95 DIP protein Q07812 original sequence version: 120 DIP protein Q07812 original sequence version: 126 DIP protein Q07812 original sequence version: 143 DIP protein Q07812 original sequence version: 172 DIP protein Q07812 original sequence version: 175 6C0CDB0A7DEE4994 bax-ul37-1 2 3 unspecified role unspecified role unspecified role unspecified role Region 130-150 Region 130-150 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 4 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction bax-ul37-2 1 3 unspecified role unspecified role unspecified role unspecified role Region 130-150 Region 130-150 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P16778:p.Leu143Ala L143A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain L A This feature has been corrected as a result of our quality control procedures. The original label was 'L143A'. Wed May 02 16:31:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu143ala' Tue Jun 30 16:30:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu143Ala' P16778:p.Arg139Glu R139E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut 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 'R139E'. Wed May 02 18:15:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg139glu' Tue Jun 30 19:03:06 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg139Glu' P16778:p.Arg146Glu R146E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut 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 'R146E'. Wed May 02 19:40:40 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg146glu' Tue Jun 30 17:05:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg146Glu' BODIPY-label BODIPY-label bodipy label bodipy label certain certain sequence position certain certain certain sequence position certain in vitro In vitro 4 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction