IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment. Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment. J. Neurochem. (0022-3042) 2009 imex curation Klein C.L., Rovelli G., Springer W., Schall C., Gasser T., Kahle P.J. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Parkinsons - Interactions investigated in the context of Parkinsons disease As far as the corresponding author is aware the LRRK1 and DAPK1 constructs are of Human origin. All construct/domain sequence info has been taken from Figure S1. The amino acid numbers for these domains in Figure S1 is similar, but not identical to those given in UniProt. Philipp.Kahle@uni-tuebingen.de 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Klein C.L., Rovelli G., Springer W., Schall C., Gasser T., Kahle P.J. Parkinsons - Interactions investigated in the context of Parkinsons disease As far as the corresponding author is aware the LRRK1 and DAPK1 constructs are of Human origin. All construct/domain sequence info has been taken from Figure S1. The amino acid numbers for these domains in Figure S1 is similar, but not identical to those given in UniProt. Philipp.Kahle@uni-tuebingen.de Accepted 2012-NOV-19 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Neurochem. (0022-3042) 2009 Only protein-protein interactions imex curation Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment. Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment. J. Neurochem. (0022-3042) 2009 imex curation Klein C.L., Rovelli G., Springer W., Schall C., Gasser T., Kahle P.J. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Parkinsons - Interactions investigated in the context of Parkinsons disease As far as the corresponding author is aware the LRRK1 and DAPK1 constructs are of Human origin. All construct/domain sequence info has been taken from Figure S1. The amino acid numbers for these domains in Figure S1 is similar, but not identical to those given in UniProt. Philipp.Kahle@uni-tuebingen.de 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions human-293t Homo sapiens 293 cells transformed with SV40 large T antigen 293t 293 cells expressing SV40 large T antigen. The original designation of this cell line was 293tsA1609neo. It is not in Cabri,ATCC or HyperCLDB. anti tag coip anti tag coimmunoprecipitation anti tag coip anti tag western anti tag western blot anti tag western Klein C.L., Rovelli G., Springer W., Schall C., Gasser T., Kahle P.J. Parkinsons - Interactions investigated in the context of Parkinsons disease I think the text implies Fig 1K is a positive interaction - but I can really see no band there, so have not entered it. EBI-6313673, EBI-6313660, EBI-6349193 -Figs 4C,S2 and 1D/E could maybe have been combined, but have kept separate for clarity. As far as the corresponding author is aware the LRRK1 and DAPK1 constructs are of Human origin. All construct/domain sequence info has been taken from Figure S1. The amino acid numbers for these domains in Figure S1 is similar, but not identical to those given in UniProt. Philipp.Kahle@uni-tuebingen.de Accepted 2012-NOV-19 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Neurochem. (0022-3042) 2009 Only protein-protein interactions imex curation Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment. Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment. J. Neurochem. (0022-3042) 2009 imex curation Klein C.L., Rovelli G., Springer W., Schall C., Gasser T., Kahle P.J. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Parkinsons - Interactions investigated in the context of Parkinsons disease As far as the corresponding author is aware the LRRK1 and DAPK1 constructs are of Human origin. All construct/domain sequence info has been taken from Figure S1. The amino acid numbers for these domains in Figure S1 is similar, but not identical to those given in UniProt. Philipp.Kahle@uni-tuebingen.de 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Klein C.L., Rovelli G., Springer W., Schall C., Gasser T., Kahle P.J. Parkinsons - Interactions investigated in the context of Parkinsons disease As far as the corresponding author is aware the LRRK1 and DAPK1 constructs are of Human origin. All construct/domain sequence info has been taken from Figure S1. The amino acid numbers for these domains in Figure S1 is similar, but not identical to those given in UniProt. Philipp.Kahle@uni-tuebingen.de Accepted 2012-NOV-19 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Neurochem. (0022-3042) 2009 Only protein-protein interactions imex curation Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment. Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment. J. Neurochem. (0022-3042) 2009 imex curation Klein C.L., Rovelli G., Springer W., Schall C., Gasser T., Kahle P.J. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Parkinsons - Interactions investigated in the context of Parkinsons disease As far as the corresponding author is aware the LRRK1 and DAPK1 constructs are of Human origin. All construct/domain sequence info has been taken from Figure S1. The amino acid numbers for these domains in Figure S1 is similar, but not identical to those given in UniProt. Philipp.Kahle@uni-tuebingen.de 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions human-293t Homo sapiens 293 cells transformed with SV40 large T antigen 293t 293 cells expressing SV40 large T antigen. The original designation of this cell line was 293tsA1609neo. It is not in Cabri,ATCC or HyperCLDB. molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column western blot western blot Immuno blot Immuno blot Klein C.L., Rovelli G., Springer W., Schall C., Gasser T., Kahle P.J. Parkinsons - Interactions investigated in the context of Parkinsons disease As far as the corresponding author is aware the LRRK1 and DAPK1 constructs are of Human origin. All construct/domain sequence info has been taken from Figure S1. The amino acid numbers for these domains in Figure S1 is similar, but not identical to those given in UniProt. Philipp.Kahle@uni-tuebingen.de Accepted 2012-NOV-19 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Neurochem. (0022-3042) 2009 Only protein-protein interactions imex curation Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment. Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment. J. Neurochem. (0022-3042) 2009 imex curation Klein C.L., Rovelli G., Springer W., Schall C., Gasser T., Kahle P.J. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Parkinsons - Interactions investigated in the context of Parkinsons disease As far as the corresponding author is aware the LRRK1 and DAPK1 constructs are of Human origin. All construct/domain sequence info has been taken from Figure S1. The amino acid numbers for these domains in Figure S1 is similar, but not identical to those given in UniProt. Philipp.Kahle@uni-tuebingen.de 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro affinity chrom affinity chromatography technology Affinity purification Affinity purification affinity chrom anti tag western anti tag western blot anti tag western Klein C.L., Rovelli G., Springer W., Schall C., Gasser T., Kahle P.J. Parkinsons - Interactions investigated in the context of Parkinsons disease As far as the corresponding author is aware the LRRK1 and DAPK1 constructs are of Human origin. All construct/domain sequence info has been taken from Figure S1. The amino acid numbers for these domains in Figure S1 is similar, but not identical to those given in UniProt. Philipp.Kahle@uni-tuebingen.de Accepted 2012-NOV-19 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Neurochem. (0022-3042) 2009 Only protein-protein interactions imex curation lrrk2_human Leucine-rich repeat serine/threonine-protein kinase 2 LRRK2 PARK8 Dardarin protein protein human Homo sapiens Human MASGSCQGCEEDEETLKKLIVRLNNVQEGKQIETLVQILEDLLVFTYSERASKLFQGKNIHVPLLIVLDSYMRVASVQQVGWSLLCKLIEVCPGTMQSLMGPQDVGNDWEVLGVHQLILKMLTVHNASVNLSVIGLKTLDLLLTSGKITLLILDEESDIFMLIFDAMHSFPANDEVQKLGCKALHVLFERVSEEQLTEFVENKDYMILLSALTNFKDEEEIVLHVLHCLHSLAIPCNNVEVLMSGNVRCYNIVVEAMKAFPMSERIQEVSCCLLHRLTLGNFFNILVLNEVHEFVVKAVQQYPENAALQISALSCLALLTETIFLNQDLEEKNENQENDDEGEEDKLFWLEACYKALTWHRKNKHVQEAACWALNNLLMYQNSLHEKIGDEDGHFPAHREVMLSMLMHSSSKEVFQASANALSTLLEQNVNFRKILLSKGIHLNVLELMQKHIHSPEVAESGCKMLNHLFEGSNTSLDIMAAVVPKILTVMKRHETSLPVQLEALRAILHFIVPGMPEESREDTEFHHKLNMVKKQCFKNDIHKLVLAALNRFIGNPGIQKCGLKVISSIVHFPDALEMLSLEGAMDSVLHTLQMYPDDQEIQCLGLSLIGYLITKKNVFIGTGHLLAKILVSSLYRFKDVAEIQTKGFQTILAILKLSASFSKLLVHHSFDLVIFHQMSSNIMEQKDQQFLNLCCKCFAKVAMDDYLKNVMLERACDQNNSIMVECLLLLGADANQAKEGSSLICQVCEKESSPKLVELLLNSGSREQDVRKALTISIGKGDSQIISLLLRRLALDVANNSICLGGFCIGKVEPSWLGPLFPDKTSNLRKQTNIASTLARMVIRYQMKSAVEEGTASGSDGNFSEDVLSKFDEWTFIPDSSMDSVFAQSDDLDSEGSEGSFLVKKKSNSISVGEFYRDAVLQRCSPNLQRHSNSLGPIFDHEDLLKRKRKILSSDDSLRSSKLQSHMRHSDSISSLASEREYITSLDLSANELRDIDALSQKCCISVHLEHLEKLELHQNALTSFPQQLCETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIGPSVVLDPTVKCPTLKQFNLSYNQLSFVPENLTDVVEKLEQLILEGNKISGICSPLRLKELKILNLSKNHISSLSENFLEACPKVESFSARMNFLAAMPFLPPSMTILKLSQNKFSCIPEAILNLPHLRSLDMSSNDIQYLPGPAHWKSLNLRELLFSHNQISILDLSEKAYLWSRVEKLHLSHNKLKEIPPEIGCLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPLDELHLNFDFKHIGCKAKDIIRFLQQRLKKAVPYNRMKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSATVGIDVKDWPIQIRDKRKRDLVLNVWDFAGREEFYSTHPHFMTQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFVNATEESDALAKLRKTIINESLNFKIRDQLVVGQLIPDCYVELEKIILSERKNVPIEFPVIDRKRLLQLVRENQLQLDENELPHAVHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKIMAQILTVKVEGCPKHPKGIISRRDVEKFLSKKRKFPKNYMSQYFKLLEKFQIALPIGEEYLLVPSSLSDHRPVIELPHCENSEIIIRLYEMPYFPMGFWSRLINRLLEISPYMLSGRERALRPNRMYWRQGIYLNWSPEAYCLVGSEVLDNHPESFLKITVPSCRKGCILLGQVVDHIDSLMEEWFPGLLEIDICGEGETLLKKWALYSFNDGEEHQKILLDDLMKKAEEGDLLVNPDQPRLTIPISQIAPDLILADLPRNIMLNNDELEFEQAPEFLLGDGSFGSVYRAAYEGEEVAVKIFNKHTSLRLLRQELVVLCHLHHPSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTTGGRIVEGLKFPNEFDELEIQGKLPDPVKEYGCAPWPMVEKLIKQCLKENPQERPTSAQVFDILNSAELVCLTRRILLPKNVIVECMVATHHNSRNASIWLGCGHTDRGQLSFLDLNTEGYTSEEVADSRILCLALVHLPVEKESWIVSGTQSGTLLVINTEDGKKRHTLEKMTDSVTCLYCNSFSKQSKQKNFLLVGTADGKLAIFEDKTVKLKGAAPLKILNIGNVSTPLMCLSESTNSTERNVMWGGCGTKIFSFSNDFTIQKLIETRTSQLFSYAAFSDSNIITVVVDTALYIAKQNSPVVEVWDKKTEKLCGLIDCVHFLREVMVKENKESKHKMSYSGRVKTLCLQKNTALWIGTGGGHILLLDLSTRRLIRVIYNFCNSVRVMMTAQLGSLKNVMLVLGYNRKNTEGTQKQKEIQSCLTVWDINLPHEVQNLEKHIEVRKELAEKMRRTSVE DIP protein Q5S007 original sequence version: 36 DIP protein Q5S007 original sequence version: 68 DIP protein Q5S007 original sequence version: 64 26142A0CECBBC3F4 lrrk1_human Leucine-rich repeat serine/threonine-protein kinase 1 LRRK1 KIAA1790 protein protein human Homo sapiens Human MAGMSQRPPSMYWCVGPEESAVCPERAMETLNGAGDTGGKPSTRGGDPAARSRRTEGIRAAYRRGDRGGARDLLEEACDQCASQLEKGQLLSIPAAYGDLEMVRYLLSKRLVELPTEPTDDNPAVVAAYFGHTAVVQELLESLPGPCSPQRLLNWMLALACQRGHLGVVKLLVLTHGADPESYAVRKNEFPVIVRLPLYAAIKSGNEDIAIFLLRHGAYFCSYILLDSPDPSKHLLRKYFIEASPLPSSYPGKTALRVKWSHLRLPWVDLDWLIDISCQITELDLSANCLATLPSVIPWGLINLRKLNLSDNHLGELPGVQSSDEIICSRLLEIDISSNKLSHLPPGFLHLSKLQKLTASKNCLEKLFEEENATNWIGLRKLQELDISDNKLTELPALFLHSFKSLNSLNVSRNNLKVFPDPWACPLKCCKASRNALECLPDKMAVFWKNHLKDVDFSENALKEVPLGLFQLDALMFLRLQGNQLAALPPQEKWTCRQLKTLDLSRNQLGKNEDGLKTKRIAFFTTRGRQRSGTEAASVLEFPAFLSESLEVLCLNDNHLDTVPPSVCLLKSLSELYLGNNPGLRELPPELGQLGNLWQLDTEDLTISNVPAEIQKEGPKAMLSYLRAQLRKAEKCKLMKMIIVGPPRQGKSTLLEILQTGRAPQVVHGEATIRTTKWELQRPAGSRAKVESVEFNVWDIGGPASMATVNQCFFTDKALYVVVWNLALGEEAVANLQFWLLNIEAKAPNAVVLVVGTHLDLIEAKFRVERIATLRAYVLALCRSPSGSRATGFPDITFKHLHEISCKSLEGQEGLRQLIFHVTCSMKDVGSTIGCQRLAGRLIPRSYLSLQEAVLAEQQRRSRDDDVQYLTDRQLEQLVEQTPDNDIKDYEDLQSAISFLIETGTLLHFPDTSHGLRNLYFLDPIWLSECLQRIFNIKGSRSVAKNGVIRAEDLRMLLVGTGFTQQTEEQYFQFLAKFEIALPVANDSYLLPHLLPSKPGLDTHGMRHPTANTIQRVFKMSFVPVGFWQRFIARMLISLAEMDLQLFENKKNTKSRNRKVTIYSFTGNQRNRCSTFRVKRNQTIYWQEGLLVTFDGGYLSVESSDVNWKKKKSGGMKIVCQSEVRDFSAMAFITDHVNSLIDQWFPALTATESDGTPLMEQYVPCPVCETAWAQHTDPSEKSEDVQYFDMEDCVLTAIERDFISCPRHPDLPVPLQELVPELFMTDFPARLFLENSKLEHSEDEGSVLGQGGSGTVIYRARYQGQPVAVKRFHIKKFKNFANVPADTMLRHLRATDAMKNFSEFRQEASMLHALQHPCIVALIGISIHPLCFALELAPLSSLNTVLSENARDSSFIPLGHMLTQKIAYQIASGLAYLHKKNIIFCDLKSDNILVWSLDVKEHINIKLSDYGISRQSFHEGALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPALGHHQLQIAKKLSKGIRPVLGQPEEVQFRRLQALMMECWDTKPEKRPLALSVVSQMKDPTFATFMYELCCGKQTAFFSSQGQEYTVVFWDGKEESRNYTVVNTEKGLMEVQRMCCPGMKVSCQLQVQRSLWTATEDQKIYIYTLKGMCPLNTPQQALDTPAVVTCFLAVPVIKKNSYLVLAGLADGLVAVFPVVRGTPKDSCSYLCSHTANRSKFSIADEDARQNPYPVKAMEVVNSGSEVWYSNGPGLLVIDCASLEICRRLEPYMAPSMVTSVVCSSEGRGEEVVWCLDDKANSLVMYHSTTYQLCARYFCGVPSPLRDMFPVRPLDTEPPAASHTANPKVPEGDSIADVSIMYSEELGTQILIHQESLTDYCSMSSYSSSPPRQAARSPSSLPSSPASSSSVPFSTDCEDSDMLHTPGAASDRSEHDLTPMDGETFSQHLQAVKILAVRDLIWVPRRGGDVIVIGLEKDSGAQRGRVIAVLKARELTPHGVLVDAAVVAKDTVVCTFENENTEWCLAVWRGWGAREFDIFYQSYEELGRLEACTRKRR DIP protein Q38SD2 original sequence version: 108 38E77EDC7C84583B dapk1_human Death-associated protein kinase 1 DAPK1 DAPK protein protein human Homo sapiens Human MTVFRQENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENKTDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAHKIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWIKPKDTQQALSRKASAVNMEKFKKFAARKKWKQSVRLISLCQRLSRSFLSRSNMSVARSDDTLDEEDSFVMKAIIHAINDDNVPGLQHLLGSLSNYDVNQPNKHGTPPLLIAAGCGNIQILQLLIKRGSRIDVQDKGGSNAVYWAARHGHVDTLKFLSENKCPLDVKDKSGEMALHVAARYGHADVAQLLCSFGSNPNIQDKEEETPLHCAAWHGYYSVAKALCEAGCNVNIKNREGETPLLTASARGYHDIVECLAEHGADLNACDKDGHIALHLAVRRCQMEVIKTLLSQGCFVDYQDRHGNTPLHVACKDGNMPIVVALCEANCNLDISNKYGRTPLHLAANNGILDVVRYLCLMGASVEALTTDGKTAEDLARSEQHEHVAGLLARLRKDTHRGLFIQQLRPTQNLQPRIKLKLFGHSGSGKTTLVESLKCGLLRSFFRRRRPRLSSTNSSRFPPSPLASKPTVSVSINNLYPGCENVSVRSRSMMFEPGLTKGMLEVFVAPTHHPHCSADDQSTKAIDIQNAYLNGVGDFSVWEFSGNPVYFCCYDYFAANDPTSIHVVVFSLEEPYEIQLNQVIFWLSFLKSLVPVEEPIAFGGKLKNPLQVVLVATHADIMNVPRPAGGEFGYDKDTSLLKEIRNRFGNDLHISNKLFVLDAGASGSKDMKVLRNHLQEIRSQIVSVCPPMTHLCEKIISTLPSWRKLNGPNQLMSLQQFVYDVQDQLNPLASEEDLRRIAQQLHSTGEINIMQSETVQDVLLLDPRWLCTNVLGKLLSVETPRALHHYRGRYTVEDIQRLVPDSDVEELLQILDAMDICARDLSSGTMVDVPALIKTDNLHRSWADEEDEVMVYGGVRIVPVEHLTPFPCGIFHKVQVNLCRWIHQQSTEGDADIRLWVNGCKLANRGAELLVLLVNHGQGIEVQVRGLETEKIKCCLLLDSVCSTIENVMATTLPGLLTVKHYLSPQQLREHHEPVMIYQPRDFFRAQTLKETSLTNTMGGYKESFSSIMCFGCHDVYSQASLGMDIHASDLNLLTRRKLSRLLDPPDPLGKDWCLLAMNLGLPDLVAKYNTSNGAPKDFLPSPLHALLREWTTYPESTVGTLMSKLRELGRRDAADFLLKASSVFKINLDGNGQEAYASSCNSGTSYNSISSVVSR E2C4246E7C78A6D2 gtp guanosine triphosphate - GTP 5'-GTP GTP Guanosine 5'-triphosphate guanosine 5'-triphosphoric acid guanosine triphosphate GUANOSINE-5'-TRIPHOSPHATE H4gtp guanosine 5'-(tetrahydrogen triphosphate) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) InChI=1/C10H16N5O14P3/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(27-9)1-26-31(22,23)29-32(24,25)28-30(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H,24,25)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1/f/h14,19-20,22,24H,11H2 InChI=1/C10H16N5O14P3/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(27-9)1-26-31(22,23)29-32(24,25)28-30(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H,24,25)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1/f/h14,19-20,22,24H,11H2 cor-roc 3 6 unspecified role unspecified role bait bait cor_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role prey prey roc_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 14 12 physical association physical association 1A roco-roco 3 6 unspecified role unspecified role prey prey roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role bait bait roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 17 19 physical association physical association 1B-1 roco-rck 3 6 unspecified role unspecified role prey prey rck_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role bait bait roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 22 24 physical association physical association 1B-2 weaker interaction than ROCO-ROCO roco-rckw 3 6 unspecified role unspecified role prey prey rckw_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role bait bait roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 29 27 physical association physical association 1B-3 weaker interaction than ROCO-ROCO rckw-roco 3 6 unspecified role unspecified role prey prey roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role bait bait rckw_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 34 32 physical association physical association 1B-4 rck-roco 3 6 unspecified role unspecified role bait bait rck_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role prey prey roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 39 37 physical association physical association 1B-5 fl_lrrk2-roco 2 6 unspecified role unspecified role bait bait c_terminus ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range 6 unspecified role unspecified role prey prey Q5S007:p.Tyr1699Cys mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain Y C Wed May 02 16:33:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr1699cys' Tue Jun 30 17:05:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr1699Cys' Q5S007:p.Arg1441Cys mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R C Wed May 02 19:14:06 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg1441cys' Tue Jun 30 19:50:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg1441Cys' n_terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain physical association physical association 1D/E, 5A-bottom, 5C-bottom, 5E bottom.S9. Full length MYC- LRRK2 and the MYC-ROCO-LRRK2 fragment were co-immunoprecipitated with full-length HA-LRRK2. GTP-binding deficient ROCO-LRRK2 mutants (K1347A and T1348N) showed reduced co-immunoprecipitation to a similar extent as their wt counterpart. rckw-rckw 2 6 unspecified role unspecified role bait bait rckw_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n_terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 6 unspecified role unspecified role prey prey rckw_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain c_terminus ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range 50 53 physical association physical association S2 lrrk2-1 4 6 unspecified role unspecified role neutral component neutral component delta_roco_construct sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain range range range range certain certain sequence position certain n_terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range physical association physical association 1L, 1F, 3F, 4D. Lysates from LRRK2 and DAPK1 co-expressing HEK293T cells showed predominantly homodimeric elution profiles for each ROCO kinase, but hinting at a possible existence of small amounts of heterodimers. The R1441C mutation in full length LRRK2 did not alter the LRRK2 elution profile. roco1-roco1 2 7 unspecified role unspecified role prey prey roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 7 unspecified role unspecified role bait bait roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 64 61 physical association physical association 2A/B dapk1-dapk1 2 8 unspecified role unspecified role prey prey roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 8 unspecified role unspecified role bait bait region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 72 68 physical association physical association 2C dapk1-1 4 8 unspecified role unspecified role neutral component neutral component region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association 2E, 3F Lysates from LRRK2 and DAPK1 co-expressing HEK293T cells showed predominantly homodimeric elution profiles for each ROCO kinase, but hinting at a possible existence of small amounts of heterodimers. lrrk1-lrrk1-1 4 7 unspecified role unspecified role neutral component neutral component region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association 2D roco-lrrk1 2 6 unspecified role unspecified role bait bait n_terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 7 unspecified role unspecified role prey prey roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 84 82 physical association physical association 3A lrrk2-lrrk1 2 6 unspecified role unspecified role bait bait roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n_terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 8 unspecified role unspecified role prey prey region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 92 88 physical association physical association 3B lrrk1-dapk1-1 2 8 unspecified role unspecified role prey prey roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 7 unspecified role unspecified role bait bait roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 98 95 physical association physical association 3B lrrk2-lrrk1-1 2 7 unspecified role unspecified role prey prey region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role bait bait c_terminus ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range physical association physical association 3C, S5A lrrk2-lrrk2-16 2 6 unspecified role unspecified role prey prey n_terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 8 unspecified role unspecified role bait bait region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association 3D dapk1-lrrk2 2 7 unspecified role unspecified role prey prey region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 8 unspecified role unspecified role bait bait region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association 3E gtp-lrrk2 5 6 unspecified role unspecified role prey prey Q5S007:p.Thr1348Asn mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain T N Wed May 02 15:31:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr1348asn' Tue Jun 30 18:18:52 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr1348Asn' roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q5S007:p.Lys1347Ala mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain K A Wed May 02 18:48:13 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys1347ala' Tue Jun 30 18:35:40 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys1347Ala' n_terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range human-293t Homo sapiens 293 cells transformed with SV40 large T antigen 293t 293 cells expressing SV40 large T antigen. The original designation of this cell line was 293tsA1609neo. It is not in Cabri,ATCC or HyperCLDB. 9 unspecified role unspecified role bait bait chemical synthesis Chemical synthesis (Chemical synthesis) physical association physical association S6A/B gtp-lrrk2-1 2 6 unspecified role unspecified role bait bait n_terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role prey prey c_terminus ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 126 129 physical association physical association 1C, S6C, S7 GTP binding deficient MYC-ROCO-LRRK2 mutants are co-immunoprecipitated along with their mutant GTP binding deficient HA-tagged counterpart identical to wt ROCO-LRRK2 homodimerization. Addition of excess GTP, or other nucleotides, had no significant impact on this co-precipitation. lrrk2-lrrk2-17 2 6 unspecified role unspecified role bait bait roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n_terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 6 unspecified role unspecified role prey prey Q5S007:p.Tyr1699Cys mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain Y C Wed May 02 19:01:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr1699cys' Tue Jun 30 16:44:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr1699Cys' Q5S007:p.Arg1441His mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R H Wed May 02 17:45:40 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg1441his' Tue Jun 30 19:21:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg1441His' roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q5S007:p.Arg1441Cys mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R C Wed May 02 17:02:08 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg1441cys' Tue Jun 30 19:59:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg1441Cys' Q5S007:p.Arg1441Gly mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R G Wed May 02 16:32:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg1441gly' Tue Jun 30 18:04:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg1441Gly' c_terminus ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range 132 137 physical association physical association 4A ROCO-LRRK2 homodimerization was weakened by all four tested substitutions. lrrk2-lrrk2-19 2 6 unspecified role unspecified role prey prey n_terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 6 unspecified role unspecified role bait bait c_terminus ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range physical association physical association 4C Contrary to co-IPs with ROCO-LRRK2 fragments, full length PD mutant LRRK2-R1441C and Y1699C proteins co-immunoprecipitated along with full length wt LRRK2 to a similar extent as full length wt LRRK2. lrrk2-lrrk2-20 1 6 putative self putative self putative self putative self c_terminus ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range Q5S007:p.Gly2019Ser mutation increasing rate mutation increasing interaction rate mutation increasing rate certain certain sequence position certain certain certain sequence position certain G S Wed May 02 15:00:25 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly2019ser' Tue Jun 30 18:29:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly2019Ser' Q5S007:p.Lys1906Met mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain K M Wed May 02 15:40:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys1906met' Tue Jun 30 18:19:49 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys1906Met' human-293t Homo sapiens 293 cells transformed with SV40 large T antigen 293t 293 cells expressing SV40 large T antigen. The original designation of this cell line was 293tsA1609neo. It is not in Cabri,ATCC or HyperCLDB. phosphorylation phosphorylation reaction phosphorylation true 5A-lanes 2-4/5C/5E lrrk1-dapk1-2 2 7 unspecified role unspecified role bait bait region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 6 unspecified role unspecified role prey prey c_terminus ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain physical association physical association S5B lrrk2-lrrk2-25 2 6 unspecified role unspecified role bait bait c_terminus ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range 6 unspecified role unspecified role prey prey n_terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range delta_roco_construct sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain range range range range certain certain sequence position certain physical association physical association 1K A very weak reaction. lrrk2-lrrk2-26 1 6 inhibitor inhibitor ancillary ancillary n_terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range roco_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q5S007:p.Arg1441Cys mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain R C Wed May 02 17:45:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg1441cys' Tue Jun 30 17:37:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg1441Cys' human-293t Homo sapiens 293 cells transformed with SV40 large T antigen 293t 293 cells expressing SV40 large T antigen. The original designation of this cell line was 293tsA1609neo. It is not in Cabri,ATCC or HyperCLDB. 6 putative self putative self putative self putative self c_terminus ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range Q5S007:p.Gly2019Ser mutation increasing rate mutation increasing interaction rate mutation increasing rate certain certain sequence position certain certain certain sequence position certain G S Wed May 02 15:30:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly2019ser' Tue Jun 30 17:00:06 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly2019Ser' human-293t Homo sapiens 293 cells transformed with SV40 large T antigen 293t 293 cells expressing SV40 large T antigen. The original designation of this cell line was 293tsA1609neo. It is not in Cabri,ATCC or HyperCLDB. phosphorylation phosphorylation reaction phosphorylation 5A lanes 5-6/5C/5E Co-expression of ROCO-LRRK2 led to decreased autophosphorylation of both wt and G2019S LRRK2. LRRK2 kinase inhibition was reduced in the presence of mutant ROCO-LRRK2 fragments compared with wt ROCO-LRRK2. GTP-binding deficient ROCO-LRRK2 mutants (K1347A and T1348N) inhibited LRRK2 autophosphorylation to a similar extent as their wt counterparts. "reduced kinase inhibition by ROCO-LRRK2 Y1699C did not reach statistical significance" - so not entered.