DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ jacob-2014-1 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Jacob Y., Bergamin E., Donoghue MT., Mongeon V., LeBlanc C., Voigt P., Underwood CJ., Brunzelle JS., Michaels SD., Reinberg D., Couture JF., Martienssen RA. DIP original experiment: DIP-266316X Science (New York, N.Y.) 2014 IMEx Selective methylation of histone H3 variant H3.1 regulates heterochromatin replication. Jacob Y., Bergamin E., Donoghue MT., Mongeon V., LeBlanc C., Voigt P., Underwood CJ., Brunzelle JS., Michaels SD., Reinberg D., Couture JF., Martienssen RA. Only protein-protein interactions imex curation jacob-2014-2 in vitro In vitro methyltransferase as methyltransferase assay methyltransferase as weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Jacob Y., Bergamin E., Donoghue MT., Mongeon V., LeBlanc C., Voigt P., Underwood CJ., Brunzelle JS., Michaels SD., Reinberg D., Couture JF., Martienssen RA. DIP original experiment: DIP-266317X Science (New York, N.Y.) 2014 IMEx Selective methylation of histone H3 variant H3.1 regulates heterochromatin replication. Jacob Y., Bergamin E., Donoghue MT., Mongeon V., LeBlanc C., Voigt P., Underwood CJ., Brunzelle JS., Michaels SD., Reinberg D., Couture JF., Martienssen RA. Only protein-protein interactions imex curation h3.1 Histone 3.1 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) KQLATKAARKSAPATGGVKY atxr5_ricco Probable Histone-lysine N-methyltransferase ATXR5 ATXR5 RCOM_1460410 protein protein castor bean Ricinus communis Castor bean MAPASITTTTTVARRIVGSRRRTKATSPPDSPPPKKLKPISEILAKAQYAVVERADYGDVSCMQCGSGERAEELLLCDKCDKGFHMKCVRPIVVRVPIGSWLCPKCSGQRRVRRLSQRKIIDFFRIQKCNHKTDKCSSPQDIRKHRRRSGSLVYQKRRRRLLPFVSSEDPAQRLKQMGTLASALTELQMEFSDDLTYSSGMAPRSANQARFEEGGMQVLTKEDIETLEQCRAMCKRGDCPPLLVVFDSREGFTVEADGQIKDMTFIAEYTGDVDYIRNREHDDCDSMMTLLLAKDPSKSLVICPDKRGNIARFISGINNHTLDGKKKQNCKCVRYSVNGECRVFLVATRDIAKGERLYYDYNGYEHEYPTQHFV atxr5-h3.1-1 3263609 N/A 3263611 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3263612 unspecified role unspecified role unspecified role unspecified role Region 158-374 Region 158-374 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false atxr5-h3.1-2 3263610 N/A 3263611 enzyme target enzyme target substrate substrate unspecified role unspecified role in vitro In vitro N/A 3263612 enzyme enzyme unspecified role unspecified role Region 158-374 Region 158-374 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli methylation methylation reaction methylation false false false