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/ Structural Basis for Cooperative Function of Mettl3 and Mettl14 Methyltransferases. Structural Basis for Cooperative Function of Mettl3 and Mettl14 Methyltransferases. Molecular cell 2016 imex curation Wang P., Doxtader KA., Nam Y. Cancer - Interactions investigated in the context of cancer yunsun.nam@utsouthwestern.edu 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Wang P., Doxtader KA., Nam Y. Cancer - Interactions investigated in the context of cancer yunsun.nam@utsouthwestern.edu Accepted 2018-JUN-20 AT 11:17 BST AT 11:17 BST by PPORRAS Molecular cell 2016 Only protein-protein interactions imex curation imex curation As discussed, the "whole molecule" feature is used to make the link is to show that there is an "obligate" complex:Mettl3 (mta70) is the active subunit, but does not function in the absence of met14 - the link shows the 2 mols are complexed, in effect. Text states: "While Mettl14 active site is not required, it has a critical role to structurally support Mettl3, and to interact with substrate RNA. " I suppose I could have entered the met 14 as an "ancillary" as well, but the 2 proteins are co-expressed (certainly in E.coli + probably the other expression systems)? Structural Basis for Cooperative Function of Mettl3 and Mettl14 Methyltransferases. Structural Basis for Cooperative Function of Mettl3 and Mettl14 Methyltransferases. Molecular cell 2016 imex curation Wang P., Doxtader KA., Nam Y. Cancer - Interactions investigated in the context of cancer yunsun.nam@utsouthwestern.edu 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Wang P., Doxtader KA., Nam Y. Cancer - Interactions investigated in the context of cancer SEC-MALS -Size Exclusion Chromatography with Multi-Angle Light Scattering or SEC followed by SDS-PAGE and protein visualisation with Stain-Free dye (Biorad). yunsun.nam@utsouthwestern.edu Accepted 2018-JUN-20 AT 11:17 BST AT 11:17 BST by PPORRAS Molecular cell 2016 Only protein-protein interactions imex curation imex curation As discussed, the "whole molecule" feature is used to make the link is to show that there is an "obligate" complex:Mettl3 (mta70) is the active subunit, but does not function in the absence of met14 - the link shows the 2 mols are complexed, in effect. Text states: "While Mettl14 active site is not required, it has a critical role to structurally support Mettl3, and to interact with substrate RNA. " I suppose I could have entered the met 14 as an "ancillary" as well, but the 2 proteins are co-expressed (certainly in E.coli + probably the other expression systems)? Structural Basis for Cooperative Function of Mettl3 and Mettl14 Methyltransferases. Structural Basis for Cooperative Function of Mettl3 and Mettl14 Methyltransferases. Molecular cell 2016 imex curation Wang P., Doxtader KA., Nam Y. Cancer - Interactions investigated in the context of cancer yunsun.nam@utsouthwestern.edu 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro radiolabeled methyl methyltransferase radiometric assay radiolabeled methyl predetermined predetermined participant predetermined Wang P., Doxtader KA., Nam Y. Cancer - Interactions investigated in the context of cancer dear checker;in some figures they do not use the mutant RNA -e.g. Fig 5A. So as to avoid extra (not very informative) interactions I have not added extra interactions MINUS the Rna mutation decreasing. If you really think I ought to, I am not arguing.. yunsun.nam@utsouthwestern.edu Accepted 2018-JUN-20 AT 11:17 BST AT 11:17 BST by PPORRAS Molecular cell 2016 Only protein-protein interactions imex curation imex curation As discussed, the "whole molecule" feature is used to make the link is to show that there is an "obligate" complex:Mettl3 (mta70) is the active subunit, but does not function in the absence of met14 - the link shows the 2 mols are complexed, in effect. Text states: "While Mettl14 active site is not required, it has a critical role to structurally support Mettl3, and to interact with substrate RNA. " I suppose I could have entered the met 14 as an "ancillary" as well, but the 2 proteins are co-expressed (certainly in E.coli + probably the other expression systems)? met14_human N6-adenosine-methyltransferase non-catalytic subunit Methyltransferase-like protein 14 METTL14 KIAA1627 protein protein human Homo sapiens Human MDSRLQEIRERQKLRRQLLAQQLGAESADSIGAVLNSKDEQREIAETRETCRASYDTSAPNAKRKYLDEGETDEDKMEEYKDELEMQQDEENLPYEEEIYKDSSTFLKGTQSLNPHNDYCQHFVDTGHRPQNFIRDVGLADRFEEYPKLRELIRLKDELIAKSNTPPMYLQADIEAFDIRELTPKFDVILLEPPLEEYYRETGITANEKCWTWDDIMKLEIDEIAAPRSFIFLWCGSGEGLDLGRVCLRKWGYRRCEDICWIKTNKNNPGKTKTLDPKAVFQRTKEHCLMGIKGTVKRSTDGDFIHANVDIDLIITEEPEIGNIEKPVEIFHIIEHFCLGRRRLHLFGRDSTIRPGWLTVGPTLTNSNYNAETYASYFSAPNSYLTGCTEEIERLRPKSPPPKSKSDRGGGAPRGGGRGGTSAGRGRERNRSNFRGERGGFRGGRGGAHRGGFPPR DIP protein Q9HCE5 original sequence version: 72 DIP protein Q9HCE5 original sequence version: 73 DIP protein Q9HCE5 original sequence version: 95 73A45B66BB76E241 s-adenosyl-l-methionine S adenosyl Methionine small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) s-adenosyl-l-homocysteine S-adenosyl-l-homocysteine small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) “ggacu” “GGACU” rna ribonucleic acid RNA rna synthetic construct synthetic construct UACACUCGAUCUGGACUAAAGCUGCUC mta70_human N6-adenosine-methyltransferase catalytic subunit N6-adenosine-methyltransferase 70 kDa subunit METTL3 MTA70 Methyltransferase-like protein 3 protein protein human Homo sapiens Human MSDTWSSIQAHKKQLDSLRERLQRRRKQDSGHLDLRNPEAALSPTFRSDSPVPTAPTSGGPKPSTASAVPELATDPELEKKLLHHLSDLALTLPTDAVSICLAISTPDAPATQDGVESLLQKFAAQELIEVKRGLLQDDAHPTLVTYADHSKLSAMMGAVAEKKGPGEVAGTVTGQKRRAEQDSTTVAAFASSLVSGLNSSASEPAKEPAKKSRKHAASDVDLEIESLLNQQSTKEQQSKKVSQEILELLNTTTAKEQSIVEKFRSRGRAQVQEFCDYGTKEECMKASDADRPCRKLHFRRIINKHTDESLGDCSFLNTCFHMDTCKYVHYEIDACMDSEAPGSKDHTPSQELALTQSVGGDSSADRLFPPQWICCDIRYLDVSILGKFAVVMADPPWDIHMELPYGTLTDDEMRRLNIPVLQDDGFLFLWVTGRAMELGRECLNLWGYERVDEIIWVKTNQLQRIIRTGRTGHWLNHGKEHCLVGVKGNPQGFNQGLDCDVIVAEVRSTSHKPDEIYGMIERLSPGTRKIELFGRPHNVQPNWITLGNQLDGIHLLDPDVVARFKQRYPDGIISKPKNL DIP protein Q86U44 original sequence version: 95 DIP protein Q86U44 original sequence version: 96 63A7F10195A3C6AC mettl14-mettl3-14 2 8 unspecified role unspecified role neutral component neutral component purified purified methyltransferase_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component purified purified region_including_methyltransferase_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Figure 1B/C, Supp. figure 1A/C mettl14-mettl3-15 1 6 cofactor cofactor coenzyme neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) 4 unspecified role unspecified role neutral component neutral component purified purified region_including_methyltransferase_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component purified purified methyltransferase_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Table 1 1.65A R Work= 0.16 R Free= 0.179 mettl14-mettl3-16 1 5 cofactor cofactor coenzyme neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) 4 unspecified role unspecified role neutral component neutral component purified purified region_including_methyltransferase_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component purified purified methyltransferase_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Table 1i 1.7A R Work= 0.163 R Free= 0.187 mettl14-mettl3-17 1 4 unspecified role unspecified role neutral component neutral component purified purified region_including_methyltransferase_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component purified purified methyltransferase_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Table 1ii 1.65A R Work= 0.16 R Free= 0.184 mettl14-mettl3-18 3 7 enzyme target enzyme target substrate substrate neutral component neutral component purified purified c16u mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain C U synthetic construct synthetic construct 4 unspecified role unspecified role neutral component neutral component purified purified whole_molecule sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 enzyme enzyme neutral component neutral component purified purified Q86U44:p.Asp395Ala mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain D A Wed May 02 14:48:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp395ala' Tue Jun 30 20:19:59 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp395Ala' Q86U44:p.Trp475Ala mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain W A Wed May 02 19:13:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp475ala' Tue Jun 30 17:07:09 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp475Ala' Q86U44:p.Cys294Ala mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain C A Wed May 02 16:14:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys294ala' Tue Jun 30 17:35:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys294Ala' Q86U44:p.Tyr406Cys mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain Y C Wed May 02 18:57:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr406cys' Tue Jun 30 16:03:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr406Cys' whole_molecule sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q86U44:p.Asn477Ala mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain N A Wed May 02 14:47:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn477ala' Tue Jun 30 16:57:20 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asn477Ala' Q86U44:p.Cys326Ala mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain C A Wed May 02 16:46:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys326ala' Tue Jun 30 18:36:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys326Ala' ecoli Escherichia coli (strain K12) 41 35 methylation methylation reaction methylation Figure 2D, 4H, 5A/D mettl14-mettl3-19 3 7 enzyme target enzyme target substrate substrate neutral component neutral component purified purified synthetic construct synthetic construct 4 unspecified role unspecified role neutral component neutral component purified purified Q9HCE5:p.Asp312Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain D A Wed May 02 16:16:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp312ala' Tue Jun 30 16:07:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp312Ala' Q9HCE5:p.Glu192Ala mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain E A Wed May 02 18:35:51 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu192ala' Tue Jun 30 20:22:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu192Ala' whole_molecule sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 8 enzyme enzyme neutral component neutral component purified purified whole_molecule sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 49 51 methylation methylation reaction methylation Figure 2E, 4G/I Mettl3 is the catalytically active subunit, its activity is negligible without forming stoichiometric complexes with Mettl14. mettl14-mettl3-20 3 7 enzyme target enzyme target substrate substrate neutral component neutral component purified purified c16u mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain C U synthetic construct synthetic construct 4 unspecified role unspecified role neutral component neutral component purified purified Q9HCE5:p.Asp312Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain D A Wed May 02 15:15:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp312ala' Tue Jun 30 18:44:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp312Ala' Q9HCE5:p.Glu192Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain E A Wed May 02 14:24:08 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu192ala' Tue Jun 30 18:19:47 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu192Ala' whole_molecule sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 enzyme enzyme neutral component neutral component purified purified whole_molecule sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 58 60 methylation methylation reaction methylation Figure 2D-2, 4H, 5A mettl14-mettl3-21 3 7 enzyme target enzyme target substrate substrate neutral component neutral component purified purified c16u mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain C U synthetic construct synthetic construct 4 unspecified role unspecified role neutral component neutral component purified purified region_including_methyltransferase_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 enzyme enzyme neutral component neutral component purified purified whole_molecule sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 65 67 methylation methylation reaction methylation Figure 4H mettl14-mettl3-22 3 7 enzyme target enzyme target substrate substrate neutral component neutral component purified purified synthetic construct synthetic construct 4 unspecified role unspecified role neutral component neutral component purified purified whole_molecule sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 8 enzyme enzyme neutral component neutral component purified purified Q86U44:p.Tyr406Cys mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain Y C Wed May 02 16:42:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr406cys' Tue Jun 30 19:15:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr406Cys' Q86U44:p.Asp395Ala mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain D A Wed May 02 18:13:20 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp395ala' Tue Jun 30 17:01:34 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp395Ala' whole_molecule sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q86U44:p.Trp475Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain W A Wed May 02 17:18:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp475ala' Tue Jun 30 15:53:41 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp475Ala' Q86U44:p.Cys294Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain C A Wed May 02 18:04:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys294ala' Tue Jun 30 19:50:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys294Ala' Q86U44:p.Cys326Ala mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain C A Wed May 02 18:27:08 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys326ala' Tue Jun 30 16:51:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys326Ala' Q86U44:p.Asn477Ala mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain N A Wed May 02 16:05:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn477ala' Tue Jun 30 16:53:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asn477Ala' human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 75 71 methylation methylation reaction methylation Figure 2E-2, 4G/I,5B/E Mettl3 is the catalytically active subunit, its activity is negligible without forming stoichiometric complexes with Mettl14. mettl14-mettl3-23 3 7 enzyme target enzyme target substrate substrate neutral component neutral component purified purified synthetic construct synthetic construct 4 unspecified role unspecified role neutral component neutral component purified purified region_including_methyltransferase_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 enzyme enzyme neutral component neutral component purified purified (ccch)x2_motifs required to bind necessary binding region required to bind range range range range (ccch)x2_motifs+methyltransferase domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 83 86 methylation methylation reaction methylation Figure 5A (Supp fig 6A) mettl14-mettl3-24 3 7 enzyme target enzyme target substrate substrate neutral component neutral component purified purified c16u mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain C U synthetic construct synthetic construct 4 unspecified role unspecified role neutral component neutral component purified purified Q9HCE5:p.Arg298Pro mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain R P Wed May 02 18:28:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg298pro' Tue Jun 30 18:31:56 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg298Pro' whole_molecule sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 enzyme enzyme neutral component neutral component purified purified whole_molecule sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 94 92 methylation methylation reaction methylation Figure 5D, (Supp 3A) I have added Supp fig 3A to figs 5 D/E as the mutation on substrate has no effect - Supp 3A does not use mutated substrate - most other figs do. mettl14-mettl3-25 3 7 enzyme target enzyme target substrate substrate neutral component neutral component purified purified c16u mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain C U synthetic construct synthetic construct 4 unspecified role unspecified role neutral component neutral component purified purified Q9HCE5:p.Arg298Pro mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain R P Wed May 02 16:42:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg298pro' Tue Jun 30 16:25:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg298Pro' whole_molecule sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 8 enzyme enzyme neutral component neutral component purified purified whole_molecule sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 100 102 methylation methylation reaction methylation Figure 5E, Supp 3A mettl14-mettl3-26 3 7 enzyme target enzyme target substrate substrate neutral component neutral component purified purified synthetic construct synthetic construct 4 unspecified role unspecified role neutral component neutral component purified purified whole_molecule sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain trini-high_5 Trichoplusia ni cell line from eggs high_5 Insect cell line from Trichoplusia ni egg cells Invitrogen supplies this cell line. Invitrogen supply this cell line. 8 enzyme enzyme neutral component neutral component purified purified whole_molecule sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain trini-high_5 Trichoplusia ni cell line from eggs high_5 Insect cell line from Trichoplusia ni egg cells Invitrogen supplies this cell line. Invitrogen supply this cell line. 108 106 methylation methylation reaction methylation Supp 3A/C