DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing. ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing. Nature structural & molecular biology 2009 imex curation Jacob Y., Feng S., LeBlanc CA., Bernatavichute YV., Stroud H., Cokus S., Johnson LM., Pellegrini M., Jacobsen SE., Michaels SD. Only protein-protein interactions in vitro In vitro methyltransferase as methyltransferase assay methyltransferase as predetermined predetermined participant predetermined Jacob Y., Feng S., LeBlanc CA., Bernatavichute YV., Stroud H., Cokus S., Johnson LM., Pellegrini M., Jacobsen SE., Michaels SD. DIP original experiment: DIP-133073X Nature structural & molecular biology 2009 IMEx ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing. ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing. ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing. Nature structural & molecular biology 2009 imex curation Jacob Y., Feng S., LeBlanc CA., Bernatavichute YV., Stroud H., Cokus S., Johnson LM., Pellegrini M., Jacobsen SE., Michaels SD. Only protein-protein interactions in vitro In vitro methyltransferase as methyltransferase assay methyltransferase as weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Jacob Y., Feng S., LeBlanc CA., Bernatavichute YV., Stroud H., Cokus S., Johnson LM., Pellegrini M., Jacobsen SE., Michaels SD. DIP original experiment: DIP-133074X Nature structural & molecular biology 2009 IMEx ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing. ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing. ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing. Nature structural & molecular biology 2009 imex curation Jacob Y., Feng S., LeBlanc CA., Bernatavichute YV., Stroud H., Cokus S., Johnson LM., Pellegrini M., Jacobsen SE., Michaels SD. Only protein-protein interactions in vitro In vitro methyltransferase as methyltransferase assay methyltransferase as predetermined predetermined participant predetermined Jacob Y., Feng S., LeBlanc CA., Bernatavichute YV., Stroud H., Cokus S., Johnson LM., Pellegrini M., Jacobsen SE., Michaels SD. DIP original experiment: DIP-133075X Nature structural & molecular biology 2009 IMEx ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing. ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing. ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing. Nature structural & molecular biology 2009 imex curation Jacob Y., Feng S., LeBlanc CA., Bernatavichute YV., Stroud H., Cokus S., Johnson LM., Pellegrini M., Jacobsen SE., Michaels SD. Only protein-protein interactions in vitro In vitro methyltransferase as methyltransferase assay methyltransferase as weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Jacob Y., Feng S., LeBlanc CA., Bernatavichute YV., Stroud H., Cokus S., Johnson LM., Pellegrini M., Jacobsen SE., Michaels SD. DIP original experiment: DIP-133072X Nature structural & molecular biology 2009 IMEx ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing. h32_arath Histone H3.2 HTR2 HTR3 HTR13 HTR9 HTR1 Histone H3.1 F12B17_250 F12B17_260 K1G2.8 MNA5.9 T12M4.9 At1g09200 At3g27360 At5g10390 At5g10400 At5g65360 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRFRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVAALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA DIP protein P59226 original sequence version: 82 atxr5_arath Histone-lysine N-methyltransferase ATXR5 ATXR5 SDG15 SET15 Protein SET DOMAIN GROUP 15 Trithorax-related protein 5 17I14.20 MTH16.26 At5g09790 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MATWNASSPAASPCSSRRRTKAPARRPSSESPPPRKMKSMAEIMAKSVPVVEQEEEEDEDSYSNVTCEKCGSGEGDDELLLCDKCDRGFHMKCLRPIVVRVPIGTWLCVDCSDQRPVRRLSQKKILHFFRIEKHTHQTDKLELSQEETRKRRRSCSLTVKKRRRKLLPLVPSEDPDQRLAQMGTLASALTALGIKYSDGLNYVPGMAPRSANQSKLEKGGMQVLCKEDLETLEQCQSMYRRGECPPLVVVFDPLEGYTVEADGPIKDLTFIAEYTGDVDYLKNREKDDCDSIMTLLLSEDPSKTLVICPDKFGNISRFINGINNHNPVAKKKQNCKCVRYSINGECRVLLVATRDISKGERLYYDYNGYEHEYPTHHFL This sequence has been withdrawn from Uniprot. F5A792C7E491BB48 F5A792C7E491BB48 h31_human Histone H3.1 H3FA H3FL H3FD H3FI H3FH H3FK H3FF H3FJ H3FB Histone H3/a Histone H3/b Histone H3/c Histone H3/d Histone H3/f Histone H3/h Histone H3/i Histone H3/j Histone H3/k Histone H3/l H3C1 HIST1H3A H3C2 HIST1H3B H3C3 H3FC HIST1H3C H3C4 HIST1H3D H3C6 HIST1H3E H3C7 HIST1H3F H3C8 HIST1H3G H3C10 HIST1H3H H3C11 HIST1H3I H3C12 HIST1H3J protein protein human Homo sapiens Human MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA DIP protein P68431 original sequence version: 78 DIP protein P68431 original sequence version: 79 DIP protein P68431 original sequence version: 76 DIP protein P68431 original sequence version: 92 DIP protein P68431 original sequence version: 87 DIP protein P68431 original sequence version: 101 DIP protein P68431 original sequence version: 130 DIP protein P68431 original sequence version: 115 9B89008EA50A0EF6 atxr6_arath Histone-lysine N-methyltransferase ATXR6 ATXR6 SDG34 SET34 Protein SET DOMAIN GROUP 34 Trithorax-related protein 6 MOP9.18 At5g24330 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MVAVRRRRTQASNPRSEPPQHMSDHDSDSDWDTVCEECSSGKQPAKLLLCDKCDKGFHLFCLRPILVSVPKGSWFCPSCSKHQIPKSFPLIQTKIIDFFRIKRSPDSSQISSSSDSIGKKRKKTSLVMSKKKRRLLPYNPSNDPQRRLEQMASLATALRASNTKFSNELTYVSGKAPRSANQAAFEKGGMQVLSKEGVETLALCKKMMDLGECPPLMVVFDPYEGFTVEADRFIKDWTIITEYVGDVDYLSNREDDYDGDSMMTLLHASDPSQCLVICPDRRSNIARFISGINNHSPEGRKKQNLKCVRFNINGEARVLLVANRDISKGERLYYDYNGYEHEYPTEHFV DIP protein Q9FNE9 original sequence version: 62 atxr5-hist1h3a-1 4 7 enzyme target enzyme target substrate substrate unspecified role unspecified role ecolx Escherichia coli 6 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli methylation methylation reaction methylation atxr6-htr2-1 3 8 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli 5 enzyme target enzyme target substrate substrate unspecified role unspecified role P59226:p.Lys28Ala K28A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K A This feature has been corrected as a result of our quality control procedures. The original label was 'K28A'. Wed May 02 17:06:20 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys28ala' Tue Jun 30 19:54:20 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys28Ala' ecolx Escherichia coli methylation methylation reaction methylation atxr6-hist1h3a-1 1 8 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli 7 enzyme target enzyme target substrate substrate unspecified role unspecified role ecolx Escherichia coli methylation methylation reaction methylation atxr5-htr2-1 2 5 enzyme target enzyme target substrate substrate unspecified role unspecified role P59226:p.Lys28Ala K28A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K A This feature has been corrected as a result of our quality control procedures. The original label was 'K28A'. Wed May 02 16:29:18 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys28ala' Tue Jun 30 18:35:20 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys28Ala' ecolx Escherichia coli 6 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli methylation methylation reaction methylation