DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids. Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids. Structure (London, England : 1993) 2010 imex curation Lee CJ., De Biasio A., Beglova N. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Lee CJ., De Biasio A., Beglova N. DIP original experiment: DIP-216846X Structure (London, England : 1993) 2010 IMEx Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids. Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids. Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids. Structure (London, England : 1993) 2010 imex curation Lee CJ., De Biasio A., Beglova N. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Lee CJ., De Biasio A., Beglova N. DIP original experiment: DIP-216850X Structure (London, England : 1993) 2010 IMEx Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids. Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids. Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids. Structure (London, England : 1993) 2010 imex curation Lee CJ., De Biasio A., Beglova N. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Lee CJ., De Biasio A., Beglova N. DIP original experiment: DIP-216847X Structure (London, England : 1993) 2010 IMEx Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids. Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids. Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids. Structure (London, England : 1993) 2010 imex curation Lee CJ., De Biasio A., Beglova N. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Lee CJ., De Biasio A., Beglova N. DIP original experiment: DIP-216849X Structure (London, England : 1993) 2010 IMEx Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids. Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids. Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids. Structure (London, England : 1993) 2010 imex curation Lee CJ., De Biasio A., Beglova N. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Lee CJ., De Biasio A., Beglova N. DIP original experiment: DIP-216848X Structure (London, England : 1993) 2010 IMEx Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids. lrp8_mouse Low-density lipoprotein receptor-related protein 8 Apolipoprotein E receptor 2 Lrp8 Apoer2 protein protein mouse Mus musculus Mouse MGRPELGALRPLALLLLLLLQLQHLSAADPLPGGQGPVKECEEDQFRCRNERCIPLVWRCDEDNDCSDNSDEDDCPKRTCADSDFTCDNGHCIPERWKCDGEEECPDGSDESKATCSSEECPAEKLSCGPTSHKCVPASWRCDGEKDCEGGADEAGCPTLCAPHEFQCSNRSCLASVFVCDGDDDCGDGSDERGCSDPACPPREFRCGGGGTCIPERWVCDRQFDCEDRSDEAAELCGRAGQGTTATPAACAPTAQFTCRSGECIHLGWRCDGDRDCKDKSDEADCSPGPCRENEFQCGDGTCVLAIKRCNQERDCPDGSDEAGCLQESTCEGPRRFQCKSGECVDGGKVCDDQRDCRDWSDEPQKVCGLNECLHNNGGCSHICTDLKIGFECTCPAGFQLLDQKTCGDIDECQDPDACSQICVNYKGYFKCECHPGYEMDTLTKNCKAVAGKSPSLIFTNRHEVRRIDLVKRDYSRLIPMLKNVVALDVEVATNRIYWCDLSYRKIYSAHMDKASIPDEQVVLIDEQLHSPEGLAVDWVHKHIYWTDSGNKTISVATTDGRRRCTLFSRELSEPRAIAVDPLRGFMYWSDWGFQAKIEKAGLNGADRQTLVSDNIEWPNGITLDLLSQRLYWVDSKLHQLSSIDFNGGNRKMLIFSTDFLSHPFGVAVFEDKVFWTDLENEAIFSANRLNGLEIAILAENLNNPHDIVIFHELKQPKAADACDLSAQPNGGCEYLCLPAPQISSHSPKYTCACPDTMWLGPDMKRCYRAPQSTSTTTLASAMTRTVPATTRAPGTTIHDPTYQNHSTETPSQTAAAPHSVNVPRAPSTSPSTPSPATSNHSQHYGNEGSQMGSTVTAAVIGVIVPIVVIALLCMSGYLIWRNWKRKNTKSMNFDNPVYRKTTEEEEEDELHIGRTAQIGHVYPAAISNYDRPLWAEPCLGETRDLEDPAPALKELFVLPGEPRSQLHQLPKNPLSELPVVKCKRVALSLEDDGLP DIP protein Q924X6 original sequence version: 83 DIP protein Q924X6 original sequence version: 93 BA1AF0132A964EBA ldlr_human Low-density lipoprotein receptor LDLR protein protein human Homo sapiens Human MGPWGWKLRWTVALLLAAAGTAVGDRCERNEFQCQDGKCISYKWVCDGSAECQDGSDESQETCLSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGCPPKTCSQDEFRCHDGKCISRQFVCDSDRDCLDGSDEASCPVLTCGPASFQCNSSTCIPQLWACDNDPDCEDGSDEWPQRCRGLYVFQGDSSPCSAFEFHCLSGECIHSSWRCDGGPDCKDKSDEENCAVATCRPDEFQCSDGNCIHGSRQCDREYDCKDMSDEVGCVNVTLCEGPNKFKCHSGECITLDKVCNMARDCRDWSDEPIKECGTNECLDNNGGCSHVCNDLKIGYECLCPDGFQLVAQRRCEDIDECQDPDTCSQLCVNLEGGYKCQCEEGFQLDPHTKACKAVGSIAYLFFTNRHEVRKMTLDRSEYTSLIPNLRNVVALDTEVASNRIYWSDLSQRMICSTQLDRAHGVSSYDTVISRDIQAPDGLAVDWIHSNIYWTDSVLGTVSVADTKGVKRKTLFRENGSKPRAIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDIYSLVTENIQWPNGITLDLLSGRLYWVDSKLHSISSIDVNGGNRKTILEDEKRLAHPFSLAVFEDKVFWTDIINEAIFSANRLTGSDVNLLAENLLSPEDMVLFHNLTQPRGVNWCERTTLSNGGCQYLCLPAPQINPHSPKFTCACPDGMLLARDMRSCLTEAEAAVATQETSTVRLKVSSTAVRTQHTTTRPVPDTSRLPGATPGLTTVEIVTMSHQALGDVAGRGNEKKPSSVRALSIVLPIVLLVFLCLGVFLLWKNWRLKNINSINFDNPVYQKTTEDEVHICHNQDGYSYPSRQMVSLEDDVA DIP protein P01130 original sequence version: 115 DIP protein P01130 original sequence version: 122 DIP protein P01130 original sequence version: 140 DIP protein P01130 original sequence version: 173 A4C28E9B8BADAD5E apoh_human Beta-2-glycoprotein 1 APOH B2G1 Beta-2-glycoprotein I Apolipoprotein H Activated protein C-binding protein APC inhibitor Anticardiolipin cofactor protein protein human Homo sapiens Human MISPVLILFSSFLCHVAIAGRTCPKPDDLPFSTVVPLKTFYEPGEEITYSCKPGYVSRGGMRKFICPLTGLWPINTLKCTPRVCPFAGILENGAVRYTTFEYPNTISFSCNTGFYLNGADSAKCTEEGKWSPELPVCAPIICPPPSIPTFATLRVYKPSAGNNSLYRDTAVFECLPQHAMFGNDTITCTTHGNWTKLPECREVKCPFPSRPDNGFVNYPAKPTLYYKDKATFGCHDGYSLDGPEEIECTKLGNWSAMPSCKASCKVPVKKATVVYQGERVKIQEKFKNGMLHGDKVSFFCKNKEKKCSYTEDAQCIDGTIEVPKCFKEHSSLAFWKTDASDVKPC DIP protein P02749 original sequence version: 131 63101704F8EDFE3F apoh-ldlr-1 1 8 unspecified role unspecified role unspecified role unspecified role Domain V Region 263-345 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P02749:p.[Lys301Asp;Lys327Asp;Lys336Asp] K301D/K327D/K336D mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K D certain certain sequence position certain certain certain sequence position certain K D 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 'K301D/K327D/K336D'. Wed May 02 18:56:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys301asp,lys327asp,lys336asp' Tue Jun 30 16:09:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys301Asp;Lys327Asp;Lys336Asp]' P02749:p.[Lys301Asp;Lys327Asp] K301D/K327D mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K D 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 'K301D/K327D'. Wed May 02 16:34:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys301asp,lys327asp' Tue Jun 30 16:02:26 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys301Asp;Lys327Asp]' ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role LA3 domain Region 86-122 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain LA4 domain Region 126-165 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction apoh-ldlr-2 5 8 unspecified role unspecified role unspecified role unspecified role Domain V Region 263-345 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role LA3 domain Region 86-122 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction apoh-lrp8-1 2 6 unspecified role unspecified role unspecified role unspecified role LA1 domain Region 12-47 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Atto488-label Atto488-label fluorescent dye fluorescent dye label fluorescent dye undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role Domain V Region 263-345 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction apoh-lrp8-2 3 6 unspecified role unspecified role unspecified role unspecified role LA1 domain Region 12-47 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role Domain V Region 263-345 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction apoh-ldlr-3 4 8 unspecified role unspecified role unspecified role unspecified role Domain V Region 263-345 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role LA4 domain Region 126-165 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Atto488-label Atto488-label fluorescent dye fluorescent dye label fluorescent dye undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecolx Escherichia coli direct interaction direct interaction