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/ LRRK2 phosphorylates novel tau epitopes and promotes tauopathy. LRRK2 phosphorylates novel tau epitopes and promotes tauopathy. Acta Neuropathologica 2013 imex curation Bailey R.M, Jason P. Covy, Heather L. Melrose, Linda Rousseau, Ruth Watkinson, Joshua Knight, Sarah Miles, Matthew J. Farrer, Dennis W. Dickson, Benoit I. Giasson, Jada Lewis Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Parkinsons - Interactions investigated in the context of Parkinsons disease Alzheimers - Interactions investigated in the context of Alzheimers disease The authors have not confirmed that the LRRK2 Kinase Dead mutant "D1994K" was used. This construct might be "D1994A" - which is a well known KD mutant. jada.lewis@ufl.edu 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay western blot western blot Immuno blot Immuno blot Bailey R.M, Jason P. Covy, Heather L. Melrose, Linda Rousseau, Ruth Watkinson, Joshua Knight, Sarah Miles, Matthew J. Farrer, Dennis W. Dickson, Benoit I. Giasson, Jada Lewis Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. The authors have not confirmed that the LRRK2 Kinase Dead mutant "D1994K" was used. This construct might be "D1994A" - which is a well known KD mutant. jada.lewis@ufl.edu Accepted 2013-DEC-04 by ORCHARD Acta Neuropathologica 2013 Only protein-protein interactions imex curation LRRK2 phosphorylates novel tau epitopes and promotes tauopathy. LRRK2 phosphorylates novel tau epitopes and promotes tauopathy. Acta Neuropathologica 2013 imex curation Bailey R.M, Jason P. Covy, Heather L. Melrose, Linda Rousseau, Ruth Watkinson, Joshua Knight, Sarah Miles, Matthew J. Farrer, Dennis W. Dickson, Benoit I. Giasson, Jada Lewis Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Parkinsons - Interactions investigated in the context of Parkinsons disease Alzheimers - Interactions investigated in the context of Alzheimers disease The authors have not confirmed that the LRRK2 Kinase Dead mutant "D1994K" was used. This construct might be "D1994A" - which is a well known KD mutant. jada.lewis@ufl.edu 13-Jan-2014: 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 Bailey R.M, Jason P. Covy, Heather L. Melrose, Linda Rousseau, Ruth Watkinson, Joshua Knight, Sarah Miles, Matthew J. Farrer, Dennis W. Dickson, Benoit I. Giasson, Jada Lewis Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. The authors have not confirmed that the LRRK2 Kinase Dead mutant "D1994K" was used. This construct might be "D1994A" - which is a well known KD mutant. jada.lewis@ufl.edu Accepted 2013-DEC-04 by ORCHARD Acta Neuropathologica 2013 Only protein-protein interactions imex curation LRRK2 phosphorylates novel tau epitopes and promotes tauopathy. LRRK2 phosphorylates novel tau epitopes and promotes tauopathy. Acta Neuropathologica 2013 imex curation Bailey R.M, Jason P. Covy, Heather L. Melrose, Linda Rousseau, Ruth Watkinson, Joshua Knight, Sarah Miles, Matthew J. Farrer, Dennis W. Dickson, Benoit I. Giasson, Jada Lewis Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Parkinsons - Interactions investigated in the context of Parkinsons disease Alzheimers - Interactions investigated in the context of Alzheimers disease The authors have not confirmed that the LRRK2 Kinase Dead mutant "D1994K" was used. This construct might be "D1994A" - which is a well known KD mutant. jada.lewis@ufl.edu 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay sequence tag sequence tag identification sequence tag Bailey R.M, Jason P. Covy, Heather L. Melrose, Linda Rousseau, Ruth Watkinson, Joshua Knight, Sarah Miles, Matthew J. Farrer, Dennis W. Dickson, Benoit I. Giasson, Jada Lewis Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. The authors have not confirmed that the LRRK2 Kinase Dead mutant "D1994K" was used. This construct might be "D1994A" - which is a well known KD mutant. jada.lewis@ufl.edu Accepted 2013-DEC-04 by ORCHARD Acta Neuropathologica 2013 Only protein-protein interactions imex curation p10636-8 Microtubule-associated protein tau Tau-4 MAPT MAPTL MTBT1 TAU Neurofibrillary tangle protein Paired helical filament-tau 2N4R protein protein human Homo sapiens Human MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL DIP protein P10636-8 original sequence version: 206 DIP protein P10636-8 original sequence version: 203 DIP protein P10636-8 original sequence version: 166 DIP protein P10636-8 original sequence version: 218 835A8706D847A8CC p10636-7 Microtubule-associated protein tau MAPT MAPTL MTBT1 TAU Neurofibrillary tangle protein Paired helical filament-tau 1N4R protein protein human Homo sapiens Human MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL 0D4EABCA15179E7D 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 p10636-4 Microtubule-associated protein tau MAPT MAPTL MTBT1 TAU Neurofibrillary tangle protein Paired helical filament-tau 1N3R protein protein human Homo sapiens Human MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL EA206819FE73B67A p10636-2 Microtubule-associated protein tau MAPT MAPTL MTBT1 Neurofibrillary tangle protein Paired helical filament-tau TAU 0N3R protein protein human Homo sapiens Human MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL mint 9B26AEDFF4D2677C lrrk2-mapt-9 2 4 enzyme target enzyme target substrate substrate neutral component neutral component ecoli Escherichia coli (strain K12) 6 enzyme enzyme neutral component neutral component region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q5S007:p.Asp1994Lys mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain D K Wed May 02 18:44:46 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp1994lys' Tue Jun 30 18:59:26 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp1994Lys' 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 19:54:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly2019ser' Tue Jun 30 16:54:56 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly2019Ser' phosphorylation phosphorylation reaction phosphorylation Fig 1A/B, Supp fig 1. Tau = 2N4R lrrk2-27 2 6 putative self putative self putative self putative self region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q5S007:p.Asp1994Lys mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain D K Wed May 02 15:11:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp1994lys' Tue Jun 30 17:33:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp1994Lys' 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 20:03:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly2019ser' Tue Jun 30 18:07:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly2019Ser' phosphorylation phosphorylation reaction phosphorylation true Fig 1A/B lrrk2-mapt-10 2 8 enzyme target enzyme target substrate substrate neutral component neutral component ecoli Escherichia coli (strain K12) 6 enzyme enzyme neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q5S007:p.Gly2019Ser mutation mutation certain certain sequence position certain certain certain sequence position certain G S Wed May 02 14:45:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly2019ser' Tue Jun 30 18:19:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly2019Ser' phosphorylation phosphorylation reaction phosphorylation Fig 1B, Supp Fig 1. Tau = 0N3R lrrk2-mapt-11 2 6 enzyme enzyme neutral component neutral component region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q5S007:p.Gly2019Ser mutation mutation certain certain sequence position certain certain certain sequence position certain G S Wed May 02 19:26:46 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly2019ser' Tue Jun 30 17:59:46 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly2019Ser' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 7 enzyme target enzyme target substrate substrate neutral component neutral component ecoli Escherichia coli (strain K12) phosphorylation phosphorylation reaction phosphorylation Fig 1B-2, Supp fig 1. Tau = 1N3R lrrk2-mapt-12 2 6 enzyme enzyme neutral component neutral component region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q5S007:p.Gly2019Ser mutation mutation certain certain sequence position certain certain certain sequence position certain G S Wed May 02 17:12:08 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly2019ser' Tue Jun 30 17:03:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly2019Ser' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 5 enzyme target enzyme target substrate substrate neutral component neutral component ecoli Escherichia coli (strain K12) phosphorylation phosphorylation reaction phosphorylation Fig 1B-3, Supp Fig 1. Tau = 1N4R lrrk2-mapt-13 3 8 enzyme target enzyme target substrate substrate neutral component neutral component ecoli Escherichia coli (strain K12) 6 enzyme enzyme neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q5S007:p.Gly2019Ser mutation mutation certain certain sequence position certain certain certain sequence position certain G S Wed May 02 16:58:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly2019ser' Tue Jun 30 19:54:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly2019Ser' Q5S007:p.Asp1994Lys mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain D K Wed May 02 20:04:51 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp1994lys' Tue Jun 30 16:52:34 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp1994Lys' phosphorylation phosphorylation reaction phosphorylation Fig 2A, Supp. Table 1 and 2. Tau = 0N3R T149, T153, T169, T205, T263 and T231 were identified as the major phosphorylation sites. P10636-2 thr-149 O-phospho-L-threonine; P10636-2 thr-153 O-phospho-L-threonine; P10636-2 thr-169 O-phospho-L-threonine; P10636-2 thr-205 O-phospho-L-threonine; P10636-2 thr-263 O-phospho-L-threonine; P10636-2 thr-231 O-phospho-L-threonine; lrrk2-mapt-14 2 4 enzyme target enzyme target substrate substrate neutral component neutral component P10636-8:p.Thr149Ala mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain T A Wed May 02 20:32:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr149ala' Tue Jun 30 19:19:10 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr149Ala' peptide_a sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P10636-8:p.Thr153Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain T A Wed May 02 16:16:02 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr153ala' Tue Jun 30 16:01:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr153Ala' chemical synthesis Chemical synthesis (Chemical synthesis) 6 enzyme enzyme neutral component neutral component region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q5S007:p.Gly2019Ser mutation mutation certain certain sequence position certain certain certain sequence position certain G S Wed May 02 18:01:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly2019ser' Tue Jun 30 16:58:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly2019Ser' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain phosphorylation phosphorylation reaction phosphorylation Fig 2Bi Tau = 2N4R this one uses mutant only - not WT so cannot amalgamate with Fig 2C. lrrk2-mapt-15 2 4 enzyme target enzyme target substrate substrate neutral component neutral component peptide_b sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P10636-8:p.Thr231Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain T A Wed May 02 19:32:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr231ala' Tue Jun 30 19:35:34 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr231Ala' chemical synthesis Chemical synthesis (Chemical synthesis) 6 enzyme enzyme neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q5S007:p.Gly2019Ser mutation mutation certain certain sequence position certain certain certain sequence position certain G S Wed May 02 20:13:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly2019ser' Tue Jun 30 20:16:20 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly2019Ser' region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 58 61 phosphorylation phosphorylation reaction phosphorylation Fig 2Bii. Tau = 2N4R lrrk2-mapt-16 2 6 enzyme enzyme neutral component neutral component region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 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 17:41:45 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly2019ser' Tue Jun 30 18:57:17 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly2019Ser' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 4 enzyme target enzyme target substrate substrate neutral component neutral component P10636-8:p.Thr149Ala mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain T A Wed May 02 14:36:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr149ala' Tue Jun 30 16:47:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr149Ala' P10636-8:p.Thr153Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain T A Wed May 02 19:23:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr153ala' Tue Jun 30 18:14:55 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr153Ala' peptide_a sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 68 72 phosphorylation phosphorylation reaction phosphorylation Fig 2C Tau = 2N4R The Km of WT and G2019S LRRK2 for the Tau-A peptide was determined to be ~170 μM. The V max of tau phosphorylation by G2019S LRRK2 was ~threefold greater than that of WT LRRK2 (10738 and 3739 relative values). lrrk2-mapt-17 1 8 enzyme target enzyme target substrate substrate neutral component neutral component ecoli Escherichia coli (strain K12) 6 enzyme enzyme neutral component neutral component region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q5S007:p.Gly2019Ser mutation mutation certain certain sequence position certain certain certain sequence position certain G S Wed May 02 15:15:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly2019ser' Tue Jun 30 20:14:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly2019Ser' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q5S007:p.Asp1994Lys mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain D K Wed May 02 16:35:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp1994lys' Tue Jun 30 18:53:20 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp1994Lys' phosphorylation phosphorylation reaction phosphorylation Fig 3B Tau = 0N3R Tau was phosphorylated by LRRK2 at T149 and T153 by G2019S LRRK2 but not by the KD form. P10636-2 thr149 O-phospho-L-threonine: P10636-2 thr153 O-phospho-L-threonine: