DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: regulation of fatty acid ethanolamide biosynthesis by bile acids. Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: regulation of fatty acid ethanolamide biosynthesis by bile acids. Structure (London, England : 1993) 2015 imex curation Magotti P., Bauer I., Igarashi M., Babagoli M., Marotta R., Piomelli D., Garau G. Only protein-protein interactions ecolx Escherichia coli comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel weight by comassie molecular weight estimation by coomasie staining weight by comassie Magotti P., Bauer I., Igarashi M., Babagoli M., Marotta R., Piomelli D., Garau G. DIP original experiment: DIP-264806X Structure (London, England : 1993) 2015 IMEx Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: regulation of fatty acid ethanolamide biosynthesis by bile acids. Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: regulation of fatty acid ethanolamide biosynthesis by bile acids. Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: regulation of fatty acid ethanolamide biosynthesis by bile acids. Structure (London, England : 1993) 2015 imex curation Magotti P., Bauer I., Igarashi M., Babagoli M., Marotta R., Piomelli D., Garau G. 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 Magotti P., Bauer I., Igarashi M., Babagoli M., Marotta R., Piomelli D., Garau G. DIP original experiment: DIP-264805X Structure (London, England : 1993) 2015 IMEx Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: regulation of fatty acid ethanolamide biosynthesis by bile acids. Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: regulation of fatty acid ethanolamide biosynthesis by bile acids. Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: regulation of fatty acid ethanolamide biosynthesis by bile acids. Structure (London, England : 1993) 2015 imex curation Magotti P., Bauer I., Igarashi M., Babagoli M., Marotta R., Piomelli D., Garau G. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Magotti P., Bauer I., Igarashi M., Babagoli M., Marotta R., Piomelli D., Garau G. DIP original experiment: DIP-264807X Structure (London, England : 1993) 2015 IMEx Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: regulation of fatty acid ethanolamide biosynthesis by bile acids. napep_human N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D NAPEPLD C7orf18 protein protein human Homo sapiens Human MDENESNQSLMTSSQYPKEAVRKRQNSARNSGASDSSRFSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNPSIPNVLRWLIMEKDHSSVPSSKEELDKELPVLKPYFITNPEEAGVREAGLRVTWLGHATVMVEMDELIFLTDPIFSSRASPSQYMGPKRFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNERFGNELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHTDVQTKKSMAIHWGTFALANEHYLEPPVKLNEALERYGLNAEDFFVLKHGESRYLNNDDENF DIP protein Q6IQ20 original sequence version: 93 napepld-1 2 4 unspecified role unspecified role unspecified role unspecified role Q6IQ20:p.[Gln158Ser;Tyr159Ser] Q158S/Y159S 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 S certain certain sequence position certain certain certain sequence position certain Q S This feature has been corrected as a result of our quality control procedures. The original label was 'Q158S/Y159S'. Wed May 02 15:06:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln158ser,tyr159ser' Tue Jun 30 20:13:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Gln158Ser;Tyr159Ser]' Region 47-393 Region 47-393 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 napepld-2 1 4 unspecified role unspecified role unspecified role unspecified role Q6IQ20:p.[Gln158Ser;Tyr159Ser] Q158S/Y159S 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 S certain certain sequence position certain certain certain sequence position certain Q S This feature has been corrected as a result of our quality control procedures. The original label was 'Q158S/Y159S'. Wed May 02 16:59:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln158ser,tyr159ser' Tue Jun 30 17:43:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Gln158Ser;Tyr159Ser]' Region 47-393 Region 47-393 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 napepld-3 3 4 unspecified role unspecified role unspecified role unspecified role Region 47-393 Region 47-393 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