DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Nature 2014 imex curation Chowdhury R., Sekirnik R., Brissett NC., Krojer T., Ho CH., Ng SS., Clifton IJ., Ge W., Kershaw NJ., Fox GC., Muniz JR., Vollmar M., Phillips C., Pilka ES., Kavanagh KL., von Delft F., Oppermann U., McDonough MA., Doherty AJ., Schofield CJ. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Chowdhury R., Sekirnik R., Brissett NC., Krojer T., Ho CH., Ng SS., Clifton IJ., Ge W., Kershaw NJ., Fox GC., Muniz JR., Vollmar M., Phillips C., Pilka ES., Kavanagh KL., von Delft F., Oppermann U., McDonough MA., Doherty AJ., Schofield CJ. DIP original experiment: DIP-260823X Nature 2014 IMEx Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Nature 2014 imex curation Chowdhury R., Sekirnik R., Brissett NC., Krojer T., Ho CH., Ng SS., Clifton IJ., Ge W., Kershaw NJ., Fox GC., Muniz JR., Vollmar M., Phillips C., Pilka ES., Kavanagh KL., von Delft F., Oppermann U., McDonough MA., Doherty AJ., Schofield CJ. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Chowdhury R., Sekirnik R., Brissett NC., Krojer T., Ho CH., Ng SS., Clifton IJ., Ge W., Kershaw NJ., Fox GC., Muniz JR., Vollmar M., Phillips C., Pilka ES., Kavanagh KL., von Delft F., Oppermann U., McDonough MA., Doherty AJ., Schofield CJ. DIP original experiment: DIP-260824X Nature 2014 IMEx Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Nature 2014 imex curation Chowdhury R., Sekirnik R., Brissett NC., Krojer T., Ho CH., Ng SS., Clifton IJ., Ge W., Kershaw NJ., Fox GC., Muniz JR., Vollmar M., Phillips C., Pilka ES., Kavanagh KL., von Delft F., Oppermann U., McDonough MA., Doherty AJ., Schofield CJ. 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 Chowdhury R., Sekirnik R., Brissett NC., Krojer T., Ho CH., Ng SS., Clifton IJ., Ge W., Kershaw NJ., Fox GC., Muniz JR., Vollmar M., Phillips C., Pilka ES., Kavanagh KL., von Delft F., Oppermann U., McDonough MA., Doherty AJ., Schofield CJ. DIP original experiment: DIP-260827X Nature 2014 IMEx Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Nature 2014 imex curation Chowdhury R., Sekirnik R., Brissett NC., Krojer T., Ho CH., Ng SS., Clifton IJ., Ge W., Kershaw NJ., Fox GC., Muniz JR., Vollmar M., Phillips C., Pilka ES., Kavanagh KL., von Delft F., Oppermann U., McDonough MA., Doherty AJ., Schofield CJ. 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 Chowdhury R., Sekirnik R., Brissett NC., Krojer T., Ho CH., Ng SS., Clifton IJ., Ge W., Kershaw NJ., Fox GC., Muniz JR., Vollmar M., Phillips C., Pilka ES., Kavanagh KL., von Delft F., Oppermann U., McDonough MA., Doherty AJ., Schofield CJ. DIP original experiment: DIP-260822X Nature 2014 IMEx Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Nature 2014 imex curation Chowdhury R., Sekirnik R., Brissett NC., Krojer T., Ho CH., Ng SS., Clifton IJ., Ge W., Kershaw NJ., Fox GC., Muniz JR., Vollmar M., Phillips C., Pilka ES., Kavanagh KL., von Delft F., Oppermann U., McDonough MA., Doherty AJ., Schofield CJ. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Chowdhury R., Sekirnik R., Brissett NC., Krojer T., Ho CH., Ng SS., Clifton IJ., Ge W., Kershaw NJ., Fox GC., Muniz JR., Vollmar M., Phillips C., Pilka ES., Kavanagh KL., von Delft F., Oppermann U., McDonough MA., Doherty AJ., Schofield CJ. DIP original experiment: DIP-260821X Nature 2014 IMEx Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Nature 2014 imex curation Chowdhury R., Sekirnik R., Brissett NC., Krojer T., Ho CH., Ng SS., Clifton IJ., Ge W., Kershaw NJ., Fox GC., Muniz JR., Vollmar M., Phillips C., Pilka ES., Kavanagh KL., von Delft F., Oppermann U., McDonough MA., Doherty AJ., Schofield CJ. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Chowdhury R., Sekirnik R., Brissett NC., Krojer T., Ho CH., Ng SS., Clifton IJ., Ge W., Kershaw NJ., Fox GC., Muniz JR., Vollmar M., Phillips C., Pilka ES., Kavanagh KL., von Delft F., Oppermann U., McDonough MA., Doherty AJ., Schofield CJ. DIP original experiment: DIP-260826X Nature 2014 IMEx Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Nature 2014 imex curation Chowdhury R., Sekirnik R., Brissett NC., Krojer T., Ho CH., Ng SS., Clifton IJ., Ge W., Kershaw NJ., Fox GC., Muniz JR., Vollmar M., Phillips C., Pilka ES., Kavanagh KL., von Delft F., Oppermann U., McDonough MA., Doherty AJ., Schofield CJ. 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 Chowdhury R., Sekirnik R., Brissett NC., Krojer T., Ho CH., Ng SS., Clifton IJ., Ge W., Kershaw NJ., Fox GC., Muniz JR., Vollmar M., Phillips C., Pilka ES., Kavanagh KL., von Delft F., Oppermann U., McDonough MA., Doherty AJ., Schofield CJ. DIP original experiment: DIP-260825X Nature 2014 IMEx Ribosomal oxygenases are structurally conserved from prokaryotes to humans. d0mgw1_rhom4 50S ribosomal protein L16 rplP Rmar_0849 protein protein rhom4 Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) Rhodothermus obamensis MLMPRRTKYRKQQKGRIKGLASRGTQIEFGDFGIKALEPARITSRQIEAARVAITRKLRRTGKVYIRIFPDKPVTKKPAEVRMGKGKGSVEFWVAVVEPGRILFEVGGVPEELAREALRLASHKLPIKTKFVKRPELMAAPQGR DIP protein D0MGW1 original sequence version: 29 rl27a_human 60S ribosomal protein L27a RPL27A Large ribosomal subunit protein uL15 protein protein human Homo sapiens Human MPSRLRKTRKLRGHVSHGHGRIGKHRKHPGGRGNAGGLHHHRINFDKYHPGYFGKVGMKHYHLKRNQSFCPTVNLDKLWTLVSEQTRVNAAKNKTGAAPIIDVVRSGYYKVLGKGKLPKQPVIVKAKFFSRRAEEKIKSVGGACVLVA DIP protein P46776 original sequence version: 122 DIP protein P46776 original sequence version: 124 CB5E09C91507798F q9h6w3-1 Ribosomal oxygenase 1 RIOX1 60S ribosomal protein L8 histidine hydroxylase Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66 C14orf169 Histone lysine demethylase NO66 MAPJD Myc-associated protein with JmjC domain NO66 Nucleolar protein 66 Ribosomal oxygenase NO66 protein protein human Homo sapiens Human MDGLQASAGPLRRGRPKRRRKPQPHSGSVLALPLRSRKIRKQLRSVVSRMAALRTQTLPSENSEESRVESTADDLGDALPGGAAVAAVPDAARREPYGHLGPAELLEASPAARSLQTPSARLVPASAPPARLVEVPAAPVRVVETSALLCTAQHLAAVQSSGAPATASGPQVDNTGGEPAWDSPLRRVLAELNRIPSSRRRAARLFEWLIAPMPPDHFYRRLWEREAVLVRRQDHTYYQGLFSTADLDSMLRNEEVQFGQHLDAARYINGRRETLNPPGRALPAAAWSLYQAGCSLRLLCPQAFSTTVWQFLAVLQEQFGSMAGSNVYLTPPNSQGFAPHYDDIEAFVLQLEGRKLWRVYRPRVPTEELALTSSPNFSQDDLGEPVLQTVLEPGDLLYFPRGFIHQAECQDGVHSLHLTLSTYQRNTWGDFLEAILPLAVQAAMEENVEFRRGLPRDFMDYMGAQHSDSKDPRRTAFMEKVRVLVARLGHFAPVDAVADQRAKDFIHDSLPPVLTDRERALSVYGLPIRWEAGEPVNVGAQLTTETEVHMLQDGIARLVGEGGHLFLYYTVENSRVYHLEEPKCLEIYPQQADAMELLLGSYPEFVRVGDLPCDSVEDQLSLATTLYDKGLLLTKMPLALN DIP protein Q9H6W3-1 original sequence version: 98 q8iuf8-1 Ribosomal oxygenase 2 RIOX2 60S ribosomal protein L27a histidine hydroxylase Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA Histone lysine demethylase MINA MDIG MINA MINA53 MYC-induced nuclear antigen Mineral dust-induced gene protein NO52 Nucleolar protein 52 Ribosomal oxygenase MINA protein protein human Homo sapiens Human MPKKAKPTGSGKEEGPAPCKQMKLEAAGGPSALNFDSPSSLFESLISPIKTETFFKEFWEQKPLLIQRDDPALATYYGSLFKLTDLKSLCSRGMYYGRDVNVCRCVNGKKKVLNKDGKAHFLQLRKDFDQKRATIQFHQPQRFKDELWRIQEKLECYFGSLVGSNVYITPAGSQGLPPHYDDVEVFILQLEGEKHWRLYHPTVPLAREYSVEAEERIGRPVHEFMLKPGDLLYFPRGTIHQADTPAGLAHSTHVTISTYQNNSWGDFLLDTISGLVFDTAKEDVELRTGIPRQLLLQVESTTVATRRLSGFLRTLADRLEGTKELLSSDMKKDFIMHRLPPYSAGDGAELSTPGGKLPRLDSVVRLQFKDHIVLTVLPDQDQSDEAQEKMVYIYHSLKNSRETHMMGNEEETEFHGLRFPLSHLDALKQIWNSPAISVKDLKLTTDEEKESLVLSLWTECLIQVV DIP protein Q8IUF8-1 original sequence version: 98 roxa_ecoli 50S ribosomal protein L16 3-hydroxylase roxA Ribosomal oxygenase RoxA ycfD JW1114 b1128 protein protein ecoli Escherichia coli (strain K12) MEYQLTLNWPDFLERHWQKRPVVLKRGFNNFIDPISPDELAGLAMESEVDSRLVSHQDGKWQVSHGPFESYDHLGETNWSLLVQAVNHWHEPTAALMRPFRELPDWRIDDLMISFSVPGGGVGPHLDQYDVFIIQGTGRRRWRVGEKLQMKQHCPHPDLLQVDPFEAIIDEELEPGDILYIPPGFPHEGYALENAMNYSVGFRAPNTRELISGFADYVLQRELGGNYYSDPDVPPRAHPADVLPQEMDKLREMMLELINQPEHFKQWFGEFISQSRHELDIAPPEPPYQPDEIYDALKQGEVLVRLGGLRVLRIGDDVYANGEKIDSPHRPALDALASNIALTAENFGDALEDPSFLAMLAALVNSGYWFFEG DIP protein P27431 original sequence version: 62 DIP protein P27431 original sequence version: 96 5DC601513A578FD0 d0mk34_rhom4 Rmar_0038 protein protein rhom4 Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) Rhodothermus obamensis MQLPETILGGLAPEEFLANYWQKRPLLIRQALPGFRSPITPEELAGLACEEGVTARLILEKGGAYPWEVRYGPFEPEDFVALPPTHWTLLVQEVDRLVPEVAALLETVRFVPNWRLDDIMVSYAPEGGTVGAHIDNYDVFLVQAWGRRRWQINHRPVEREELVPGLEVRLLAHFEPDAEWILEPGDVLYLPPRIPHYGVALEDCMTFSIGFRAPDQAELAEAMPRMAAWLDGGRRYADPDLTPADEPGEITPEALDQIQALLRALIDDRERLARWFGCIITEPRRGLPPEPPGRPLSAKQLHRRLQQGATLRRNAIPELAYVRHADGSATLFASGEAYELSPELADVAPLLTGRRPLTAETLRPWLERDDFLELLQTLIHSGILSLIPARKR DIP protein D0MK34 original sequence version: 28 rl8_human 60S ribosomal protein L8 RPL8 Large ribosomal subunit protein uL2 protein protein human Homo sapiens Human MGRVIRGQRKGAGSVFRAHVKHRKGAARLRAVDFAERHGYIKGIVKDIIHDPGRGAPLAKVVFRDPYRFKKRTELFIAAEGIHTGQFVYCGKKAQLNIGNVLPVGTMPEGTIVCCLEEKPGDRGKLARASGNYATVISHNPETKKTRVKLPSGSKKVISSANRAVVGVVAGGGRIDKPILKAGRAYHKYKAKRNCWPRVRGVAMNPVEHPFGGGNHQHIGKPSTIRRDAPAGRKVGLIAARRTGRLRGTKTVQEKEN DIP protein P62917 original sequence version: 107 CE1610449749318B no66-rpl8-1 3 14 unspecified role unspecified role unspecified role unspecified role Region 205-239 Region 205-239 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 10 unspecified role unspecified role unspecified role unspecified role Region 183-641 Region 183-641 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 mina-1 5 11 unspecified role unspecified role unspecified role unspecified role Region 26-465 Region 26-465 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 d0mk34_rhom4-1 2 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction mina-rpl27a-1 4 9 unspecified role unspecified role unspecified role unspecified role Region 32-50 Region 32-50 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 11 unspecified role unspecified role unspecified role unspecified role Region 26-465 Region 26-465 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 d0mk34_rhom4-rplp-1 7 8 unspecified role unspecified role unspecified role unspecified role Region 72-91 Region 72-91 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction no66-1 6 10 unspecified role unspecified role unspecified role unspecified role Region 183-641 Region 183-641 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 roxa-1 1 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction