DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Selective methylation of histone H3 variant H3.1 regulates heterochromatin replication. Selective methylation of histone H3 variant H3.1 regulates heterochromatin replication. Science (New York, N.Y.) 2014 imex curation 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 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. Selective methylation of histone H3 variant H3.1 regulates heterochromatin replication. Selective methylation of histone H3 variant H3.1 regulates heterochromatin replication. Science (New York, N.Y.) 2014 imex curation 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 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. atxr5_ricco Probable Histone-lysine N-methyltransferase ATXR5 ATXR5 RCOM_1460410 protein protein castor bean Ricinus communis Castor bean MAPASITTTTTVARRIVGSRRRTKATSPPDSPPPKKLKPISEILAKAQYAVVERADYGDVSCMQCGSGERAEELLLCDKCDKGFHMKCVRPIVVRVPIGSWLCPKCSGQRRVRRLSQRKIIDFFRIQKCNHKTDKCSSPQDIRKHRRRSGSLVYQKRRRRLLPFVSSEDPAQRLKQMGTLASALTELQMEFSDDLTYSSGMAPRSANQARFEEGGMQVLTKEDIETLEQCRAMCKRGDCPPLLVVFDSREGFTVEADGQIKDMTFIAEYTGDVDYIRNREHDDCDSMMTLLLAKDPSKSLVICPDKRGNIARFISGINNHTLDGKKKQNCKCVRYSVNGECRVFLVATRDIAKGERLYYDYNGYEHEYPTQHFV DIP protein B9RU15 original sequence version: 37 h3.1 Histone 3.1 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) KQLATKAARKSAPATGGVKY atxr5-h3.1-1 1 4 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 3 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 ecolx Escherichia coli direct interaction direct interaction atxr5-h3.1-2 2 4 enzyme target enzyme target substrate substrate unspecified role unspecified role in vitro In vitro 3 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 ecolx Escherichia coli methylation methylation reaction methylation