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/ Reduced H3K27me3 and DNA Hypomethylation Are Major Drivers of Gene Expression in K27M Mutant Pediatric High-Grade Gliomas. Reduced H3K27me3 and DNA Hypomethylation Are Major Drivers of Gene Expression in K27M Mutant Pediatric High-Grade Gliomas. Cancer Cell (1535-6108) 2013 imex curation Bender S., Tang Y., Lindroth A.M., Hovestadt V., Jones D.T., Kool M., Zapatka M., Northcott P.A., Sturm D., Wang W., Radlwimmer B., Højfeldt J.W., Truffaux N., Castel D., Schubert S., Ryzhova M., Seker-Cin H., Gronych J., Johann P.D., Stark S., Meyer J., Milde T., Schuhmann M., Ebinger M., Monoranu C.M., Ponnuswami A., Chen S., Jones C., Witt O., Collins V.P., von Deimling A., Jabado N., Puget S., Grill J., Helin K., Korshunov A., Lichter P., Monje M., Plass C., Cho Y.J., Pfister S.M. Cancer - Interactions investigated in the context of cancer The authors have confirmed that HA-tagged H3.3 (WT, K27M) constructs are Human in origin. c.plass@dkfz.de,yjcho1@stanford.edu,s.pfister@dkfz.de 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions human-hela_s3 Homo sapiens HeLa-S3 cervix carcinoma cell line hela_s3 HeLa-S3 cervix carcinoma cell line Human cervix carcinoma cell line is a subclone of its parent HELA (DSM ACC 57) derived in 1955 confirmed as human with IEF of AST, MDH anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Bender S., Tang Y., Lindroth A.M., Hovestadt V., Jones D.T., Kool M., Zapatka M., Northcott P.A., Sturm D., Wang W., Radlwimmer B., Højfeldt J.W., Truffaux N., Castel D., Schubert S., Ryzhova M., Seker-Cin H., Gronych J., Johann P.D., Stark S., Meyer J., Milde T., Schuhmann M., Ebinger M., Monoranu C.M., Ponnuswami A., Chen S., Jones C., Witt O., Collins V.P., von Deimling A., Jabado N., Puget S., Grill J., Helin K., Korshunov A., Lichter P., Monje M., Plass C., Cho Y.J., Pfister S.M. Cancer - Interactions investigated in the context of cancer The authors have confirmed that HA-tagged H3.3 (WT, K27M) constructs are Human in origin. c.plass@dkfz.de,yjcho1@stanford.edu,s.pfister@dkfz.de Accepted 2013-NOV-29 by PPORRAS Cancer Cell (1535-6108) 2013 Only protein-protein interactions imex curation Reduced H3K27me3 and DNA Hypomethylation Are Major Drivers of Gene Expression in K27M Mutant Pediatric High-Grade Gliomas. Reduced H3K27me3 and DNA Hypomethylation Are Major Drivers of Gene Expression in K27M Mutant Pediatric High-Grade Gliomas. Cancer Cell (1535-6108) 2013 imex curation Bender S., Tang Y., Lindroth A.M., Hovestadt V., Jones D.T., Kool M., Zapatka M., Northcott P.A., Sturm D., Wang W., Radlwimmer B., Højfeldt J.W., Truffaux N., Castel D., Schubert S., Ryzhova M., Seker-Cin H., Gronych J., Johann P.D., Stark S., Meyer J., Milde T., Schuhmann M., Ebinger M., Monoranu C.M., Ponnuswami A., Chen S., Jones C., Witt O., Collins V.P., von Deimling A., Jabado N., Puget S., Grill J., Helin K., Korshunov A., Lichter P., Monje M., Plass C., Cho Y.J., Pfister S.M. Cancer - Interactions investigated in the context of cancer The authors have confirmed that HA-tagged H3.3 (WT, K27M) constructs are Human in origin. c.plass@dkfz.de,yjcho1@stanford.edu,s.pfister@dkfz.de 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions human-sf188 Human SF-188 Glioma/Astrocytoma/glioblastoma multiforme Paediatric cell line sf188 SF-188 Glioma/Astrocytoma/glioblastoma multiforme Paediatric cell line anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Bender S., Tang Y., Lindroth A.M., Hovestadt V., Jones D.T., Kool M., Zapatka M., Northcott P.A., Sturm D., Wang W., Radlwimmer B., Højfeldt J.W., Truffaux N., Castel D., Schubert S., Ryzhova M., Seker-Cin H., Gronych J., Johann P.D., Stark S., Meyer J., Milde T., Schuhmann M., Ebinger M., Monoranu C.M., Ponnuswami A., Chen S., Jones C., Witt O., Collins V.P., von Deimling A., Jabado N., Puget S., Grill J., Helin K., Korshunov A., Lichter P., Monje M., Plass C., Cho Y.J., Pfister S.M. Cancer - Interactions investigated in the context of cancer The authors have confirmed that HA-tagged H3.3 (WT, K27M) constructs are Human in origin. c.plass@dkfz.de,yjcho1@stanford.edu,s.pfister@dkfz.de Accepted 2013-NOV-29 by PPORRAS Cancer Cell (1535-6108) 2013 Only protein-protein interactions imex curation Reduced H3K27me3 and DNA Hypomethylation Are Major Drivers of Gene Expression in K27M Mutant Pediatric High-Grade Gliomas. Reduced H3K27me3 and DNA Hypomethylation Are Major Drivers of Gene Expression in K27M Mutant Pediatric High-Grade Gliomas. Cancer Cell (1535-6108) 2013 imex curation Bender S., Tang Y., Lindroth A.M., Hovestadt V., Jones D.T., Kool M., Zapatka M., Northcott P.A., Sturm D., Wang W., Radlwimmer B., Højfeldt J.W., Truffaux N., Castel D., Schubert S., Ryzhova M., Seker-Cin H., Gronych J., Johann P.D., Stark S., Meyer J., Milde T., Schuhmann M., Ebinger M., Monoranu C.M., Ponnuswami A., Chen S., Jones C., Witt O., Collins V.P., von Deimling A., Jabado N., Puget S., Grill J., Helin K., Korshunov A., Lichter P., Monje M., Plass C., Cho Y.J., Pfister S.M. Cancer - Interactions investigated in the context of cancer The authors have confirmed that HA-tagged H3.3 (WT, K27M) constructs are Human in origin. c.plass@dkfz.de,yjcho1@stanford.edu,s.pfister@dkfz.de 13-Jan-2014: 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 western blot western blot Immuno blot Immuno blot Bender S., Tang Y., Lindroth A.M., Hovestadt V., Jones D.T., Kool M., Zapatka M., Northcott P.A., Sturm D., Wang W., Radlwimmer B., Højfeldt J.W., Truffaux N., Castel D., Schubert S., Ryzhova M., Seker-Cin H., Gronych J., Johann P.D., Stark S., Meyer J., Milde T., Schuhmann M., Ebinger M., Monoranu C.M., Ponnuswami A., Chen S., Jones C., Witt O., Collins V.P., von Deimling A., Jabado N., Puget S., Grill J., Helin K., Korshunov A., Lichter P., Monje M., Plass C., Cho Y.J., Pfister S.M. Cancer - Interactions investigated in the context of cancer The authors have confirmed that HA-tagged H3.3 (WT, K27M) constructs are Human in origin. c.plass@dkfz.de,yjcho1@stanford.edu,s.pfister@dkfz.de Accepted 2013-NOV-29 by PPORRAS Cancer Cell (1535-6108) 2013 Only protein-protein interactions imex curation Reduced H3K27me3 and DNA Hypomethylation Are Major Drivers of Gene Expression in K27M Mutant Pediatric High-Grade Gliomas. Reduced H3K27me3 and DNA Hypomethylation Are Major Drivers of Gene Expression in K27M Mutant Pediatric High-Grade Gliomas. Cancer Cell (1535-6108) 2013 imex curation Bender S., Tang Y., Lindroth A.M., Hovestadt V., Jones D.T., Kool M., Zapatka M., Northcott P.A., Sturm D., Wang W., Radlwimmer B., Højfeldt J.W., Truffaux N., Castel D., Schubert S., Ryzhova M., Seker-Cin H., Gronych J., Johann P.D., Stark S., Meyer J., Milde T., Schuhmann M., Ebinger M., Monoranu C.M., Ponnuswami A., Chen S., Jones C., Witt O., Collins V.P., von Deimling A., Jabado N., Puget S., Grill J., Helin K., Korshunov A., Lichter P., Monje M., Plass C., Cho Y.J., Pfister S.M. Cancer - Interactions investigated in the context of cancer The authors have confirmed that HA-tagged H3.3 (WT, K27M) constructs are Human in origin. c.plass@dkfz.de,yjcho1@stanford.edu,s.pfister@dkfz.de 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions human-sf188 Human SF-188 Glioma/Astrocytoma/glioblastoma multiforme Paediatric cell line sf188 SF-188 Glioma/Astrocytoma/glioblastoma multiforme Paediatric cell line anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Bender S., Tang Y., Lindroth A.M., Hovestadt V., Jones D.T., Kool M., Zapatka M., Northcott P.A., Sturm D., Wang W., Radlwimmer B., Højfeldt J.W., Truffaux N., Castel D., Schubert S., Ryzhova M., Seker-Cin H., Gronych J., Johann P.D., Stark S., Meyer J., Milde T., Schuhmann M., Ebinger M., Monoranu C.M., Ponnuswami A., Chen S., Jones C., Witt O., Collins V.P., von Deimling A., Jabado N., Puget S., Grill J., Helin K., Korshunov A., Lichter P., Monje M., Plass C., Cho Y.J., Pfister S.M. Cancer - Interactions investigated in the context of cancer The authors have confirmed that HA-tagged H3.3 (WT, K27M) constructs are Human in origin. c.plass@dkfz.de,yjcho1@stanford.edu,s.pfister@dkfz.de Accepted 2013-NOV-29 by PPORRAS Cancer Cell (1535-6108) 2013 Only protein-protein interactions imex curation Reduced H3K27me3 and DNA Hypomethylation Are Major Drivers of Gene Expression in K27M Mutant Pediatric High-Grade Gliomas. Reduced H3K27me3 and DNA Hypomethylation Are Major Drivers of Gene Expression in K27M Mutant Pediatric High-Grade Gliomas. Cancer Cell (1535-6108) 2013 imex curation Bender S., Tang Y., Lindroth A.M., Hovestadt V., Jones D.T., Kool M., Zapatka M., Northcott P.A., Sturm D., Wang W., Radlwimmer B., Højfeldt J.W., Truffaux N., Castel D., Schubert S., Ryzhova M., Seker-Cin H., Gronych J., Johann P.D., Stark S., Meyer J., Milde T., Schuhmann M., Ebinger M., Monoranu C.M., Ponnuswami A., Chen S., Jones C., Witt O., Collins V.P., von Deimling A., Jabado N., Puget S., Grill J., Helin K., Korshunov A., Lichter P., Monje M., Plass C., Cho Y.J., Pfister S.M. Cancer - Interactions investigated in the context of cancer The authors have confirmed that HA-tagged H3.3 (WT, K27M) constructs are Human in origin. c.plass@dkfz.de,yjcho1@stanford.edu,s.pfister@dkfz.de 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions human-hela_s3 Homo sapiens HeLa-S3 cervix carcinoma cell line hela_s3 HeLa-S3 cervix carcinoma cell line Human cervix carcinoma cell line is a subclone of its parent HELA (DSM ACC 57) derived in 1955 confirmed as human with IEF of AST, MDH anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Bender S., Tang Y., Lindroth A.M., Hovestadt V., Jones D.T., Kool M., Zapatka M., Northcott P.A., Sturm D., Wang W., Radlwimmer B., Højfeldt J.W., Truffaux N., Castel D., Schubert S., Ryzhova M., Seker-Cin H., Gronych J., Johann P.D., Stark S., Meyer J., Milde T., Schuhmann M., Ebinger M., Monoranu C.M., Ponnuswami A., Chen S., Jones C., Witt O., Collins V.P., von Deimling A., Jabado N., Puget S., Grill J., Helin K., Korshunov A., Lichter P., Monje M., Plass C., Cho Y.J., Pfister S.M. Cancer - Interactions investigated in the context of cancer The authors have confirmed that HA-tagged H3.3 (WT, K27M) constructs are Human in origin. c.plass@dkfz.de,yjcho1@stanford.edu,s.pfister@dkfz.de Accepted 2013-NOV-29 by PPORRAS Cancer Cell (1535-6108) 2013 Only protein-protein interactions imex curation Reduced H3K27me3 and DNA Hypomethylation Are Major Drivers of Gene Expression in K27M Mutant Pediatric High-Grade Gliomas. Reduced H3K27me3 and DNA Hypomethylation Are Major Drivers of Gene Expression in K27M Mutant Pediatric High-Grade Gliomas. Cancer Cell (1535-6108) 2013 imex curation Bender S., Tang Y., Lindroth A.M., Hovestadt V., Jones D.T., Kool M., Zapatka M., Northcott P.A., Sturm D., Wang W., Radlwimmer B., Højfeldt J.W., Truffaux N., Castel D., Schubert S., Ryzhova M., Seker-Cin H., Gronych J., Johann P.D., Stark S., Meyer J., Milde T., Schuhmann M., Ebinger M., Monoranu C.M., Ponnuswami A., Chen S., Jones C., Witt O., Collins V.P., von Deimling A., Jabado N., Puget S., Grill J., Helin K., Korshunov A., Lichter P., Monje M., Plass C., Cho Y.J., Pfister S.M. Cancer - Interactions investigated in the context of cancer The authors have confirmed that HA-tagged H3.3 (WT, K27M) constructs are Human in origin. c.plass@dkfz.de,yjcho1@stanford.edu,s.pfister@dkfz.de 13-Jan-2014: 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 bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Bender S., Tang Y., Lindroth A.M., Hovestadt V., Jones D.T., Kool M., Zapatka M., Northcott P.A., Sturm D., Wang W., Radlwimmer B., Højfeldt J.W., Truffaux N., Castel D., Schubert S., Ryzhova M., Seker-Cin H., Gronych J., Johann P.D., Stark S., Meyer J., Milde T., Schuhmann M., Ebinger M., Monoranu C.M., Ponnuswami A., Chen S., Jones C., Witt O., Collins V.P., von Deimling A., Jabado N., Puget S., Grill J., Helin K., Korshunov A., Lichter P., Monje M., Plass C., Cho Y.J., Pfister S.M. Cancer - Interactions investigated in the context of cancer The authors have confirmed that HA-tagged H3.3 (WT, K27M) constructs are Human in origin. c.plass@dkfz.de,yjcho1@stanford.edu,s.pfister@dkfz.de Accepted 2013-NOV-29 by PPORRAS Cancer Cell (1535-6108) 2013 Only protein-protein interactions imex curation ezh2_human Histone-lysine N-methyltransferase EZH2 KMT6 Enhancer of zeste homolog 2 ENX-1 Lysine N-methyltransferase 6 EZH2 protein protein human Homo sapiens Human MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP DIP protein Q15910 original sequence version: 97 DIP protein Q15910 original sequence version: 94 DIP protein Q15910 original sequence version: 92 DIP protein Q15910 original sequence version: 96 DIP protein Q15910 original sequence version: 122 DIP protein Q15910 original sequence version: 100 1B5029EB9D509BE5 h4_human Histone H4 H4-16 H4C1 H4C11 H4C12 H4C13 H4C14 H4C15 H4C2 H4C3 H4C4 H4C5 H4C6 H4C8 H4C9 H4/A H4/B H4/C H4/D H4/E H4/G H4/H H4/I H4/J H4/K H4/M H4/N H4/O H4F2 H4FA H4FB H4FC H4FD H4FE H4FG H4FH H4FI H4FJ H4FK H4FM H4FN H4FO HIST1H4A HIST1H4B HIST1H4C HIST1H4D HIST1H4E HIST1H4F HIST1H4H HIST1H4I HIST1H4J HIST1H4K HIST1H4L HIST2H4 HIST2H4A HIST2H4B HIST4H4 protein protein human Homo sapiens Human MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG DIP protein P62805 original sequence version: 68 DIP protein P62805 original sequence version: 111 DIP protein P62805 original sequence version: 94 DIP protein P62805 original sequence version: 97 DIP protein P62805 original sequence version: 116 DIP protein P62805 original sequence version: 105 DIP protein P62805 original sequence version: 120 DIP protein P62805 original sequence version: 144 DIP protein P62805 original sequence version: 150 DIP protein P62805 original sequence version: 154 DIP protein P62805 original sequence version: 156 DIP protein P62805 original sequence version: 112 DIP protein P62805 original sequence version: 121 DIP protein P62805 original sequence version: 123 DIP protein P62805 original sequence version: 126 DIP protein P62805 original sequence version: 132 DIP protein P62805 original sequence version: 136 DIP protein P62805 original sequence version: 119 A9E5DFD3F8B97598 h33_human Histone H3.3 H3-3A H3-3B H3.3A H3.3B H3F3 H3F3A H3F3B PP781 protein protein human Homo sapiens Human MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA DIP protein P84243 original sequence version: 72 DIP protein P84243 original sequence version: 73 DIP protein P84243 original sequence version: 97 DIP protein P84243 original sequence version: 125 DIP protein P84243 original sequence version: 110 DIP protein P84243 original sequence version: 96 5158ED279E6F9E1C suz12_human Polycomb protein SUZ12 CHET9 JJAZ1 KIAA0160 SUZ12 Suppressor of zeste 12 protein homolog Joined to JAZF1 protein Chromatin precipitated E2F target 9 protein protein protein human Homo sapiens Human MAPQKHGGGGGGGSGPSAGSGGGGFGGSAAVAAATASGGKSGGGSCGGGGSYSASSSSSAAAAAGAAVLPVKKPKMEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLESEDGEVEQQRTYSSGHNRLYFHSDTCLPLRPQEMEVDSEDEKDPEWLREKTITQIEEFSDVNEGEKEVMKLWNLHVMKHGFIADNQMNHACMLFVENYGQKIIKKNLCRNFMLHLVSMHDFNLISIMSIDKAVTKLREMQQKLEKGESASPANEEITEEQNGTANGFSEINSKEKALETDSVSGVSKQSKKQKL DIP protein Q15022 original sequence version: 92 DIP protein Q15022 original sequence version: 88 DIP protein Q15022 original sequence version: 91 DIP protein Q15022 original sequence version: 106 A8830EBC3FD38D56 ezh2-h3f3a 4 10 unspecified role unspecified role prey prey 9 unspecified role unspecified role prey prey P84243:p.Lys28Met mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain K M Wed May 02 17:44:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys28met' Tue Jun 30 18:09:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys28Met' 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 association association 2D The exogenous K27M mutant H3.3 was enriched compared with the exogenous wild-type H3.3 protein. h3f3a-ezh2 2 9 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 P84243:p.Lys28Met mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain K M Wed May 02 17:55:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys28met' Tue Jun 30 18:55:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys28Met' 10 unspecified role unspecified role prey prey 7 unspecified role unspecified role prey prey association association 2C, Supp 1B. EZH2 as well as SUZ12 was dramatically enriched in immunoprecipitated K27M-containing mono-nucleosomes relative to wild-type H3.3 protein. h3f3a-ezh2-1 3 7 unspecified role unspecified role prey prey 10 unspecified role unspecified role prey prey 9 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 P84243:p.Lys28Met mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain K M Wed May 02 17:28:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys28met' Tue Jun 30 19:51:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys28Met' association association 2C, Supp1B. EZH2 as well as SUZ12 was dramatically enriched in immunoprecipitated K27M-containing mono-nucleosomes relative to wild-type H3.3 protein. h3f3a-ezh2-2 5 9 unspecified role unspecified role bait bait P84243:p.Lys28Met mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain K M Wed May 02 15:30:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys28met' Tue Jun 30 17:34:52 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys28Met' region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 10 unspecified role unspecified role prey prey 7 unspecified role unspecified role prey prey association association 2C, Supp 1B. EZH2 as well as SUZ12 was dramatically enriched in immunoprecipitated K27M-containing mono-nucleosomes relative to wild-type H3.3 protein. ezh2-h3f3a-1 1 7 unspecified role unspecified role bait bait 9 unspecified role unspecified role prey prey P84243:p.Lys28Met mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain K M Wed May 02 16:41:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys28met' Tue Jun 30 16:15:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys28Met' region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 10 unspecified role unspecified role prey prey association association 2D The exogenous K27M mutant H3.3 was enriched compared with the exogenous wild-type H3.3 protein. ezh2-h3f3a-2 6 9 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 P84243:p.Lys28Met mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain K M Wed May 02 20:19:38 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys28met' Tue Jun 30 19:30:59 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys28Met' 10 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait association association 2D The exogenous K27M mutant H3.3 was enriched compared with the exogenous wild-type H3.3 protein. h3f3a-ezh2-3 2 9 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 8 unspecified role unspecified role prey prey physical association physical association 2B h3f3a-hist1h4a 5 9 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 8 unspecified role unspecified role prey prey physical association physical association 2B h3f3a-hist1h4a-1 3 8 unspecified role unspecified role prey prey 9 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 2B