DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Nature structural & molecular biology 2008 imex curation Berndsen CE., Tsubota T., Lindner SE., Lee S., Holton JM., Kaufman PD., Keck JL., Denu JM. Only protein-protein interactions in vitro In vitro acetylase assay acetylase assay predetermined predetermined participant predetermined Berndsen CE., Tsubota T., Lindner SE., Lee S., Holton JM., Kaufman PD., Keck JL., Denu JM. DIP original experiment: DIP-132458X Nature structural & molecular biology 2008 IMEx Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Nature structural & molecular biology 2008 imex curation Berndsen CE., Tsubota T., Lindner SE., Lee S., Holton JM., Kaufman PD., Keck JL., Denu JM. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Berndsen CE., Tsubota T., Lindner SE., Lee S., Holton JM., Kaufman PD., Keck JL., Denu JM. DIP original experiment: DIP-132456X Nature structural & molecular biology 2008 IMEx Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Nature structural & molecular biology 2008 imex curation Berndsen CE., Tsubota T., Lindner SE., Lee S., Holton JM., Kaufman PD., Keck JL., Denu JM. Only protein-protein interactions ecolx Escherichia coli pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Berndsen CE., Tsubota T., Lindner SE., Lee S., Holton JM., Kaufman PD., Keck JL., Denu JM. DIP original experiment: DIP-132454X Nature structural & molecular biology 2008 IMEx Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Nature structural & molecular biology 2008 imex curation Berndsen CE., Tsubota T., Lindner SE., Lee S., Holton JM., Kaufman PD., Keck JL., Denu JM. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Berndsen CE., Tsubota T., Lindner SE., Lee S., Holton JM., Kaufman PD., Keck JL., Denu JM. DIP original experiment: DIP-132457X Nature structural & molecular biology 2008 IMEx Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Nature structural & molecular biology 2008 imex curation Berndsen CE., Tsubota T., Lindner SE., Lee S., Holton JM., Kaufman PD., Keck JL., Denu JM. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Berndsen CE., Tsubota T., Lindner SE., Lee S., Holton JM., Kaufman PD., Keck JL., Denu JM. DIP original experiment: DIP-132455X Nature structural & molecular biology 2008 IMEx Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. vps75_yeast Vacuolar protein sorting-associated protein 75 N0890 YNL246W VPS75 protein protein yeast Saccharomyces cerevisiae Baker's yeast MMSDQENENEHAKAFLGLAKCEEEVDAIEREVELYRLNKMKPVYEKRDAYIDEIAEFWKIVLSQHVSFANYIRASDFKYIDTIDKIKVEWLALESEMYDTRDFSITFHFHGIEGDFKEQQVTKVFQIKKGKDDQEDGILTSEPVPIEWPQSYDSINPDLIKDKRSPEGKKKYRQGMKTIFGWFRWTGLKPGKEFPHGDSLASLFSEEIYPFCVKYYAEAQRDLEDEEGESGLSADGDSEDDDGSLGEVDLPLSDEEPSSKKRKV 779F12CEA27B3E6B 779F12CEA27B3E6B h3tail H3 tail peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) ARTKQTARKSTGGKAPRKQL rt109_yeast Histone acetyltransferase RTT109 RTT109 KIM2 REM50 Regulator of Ty1 transposition protein 109 L1377 YLL002W KAT11 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSLNDFLSSVLPVSEQFEYLSLQSIPLETHAVVTPNKDDKRVPKSTIKTQHFFSLFHQGKVFFSLEVYVYVTLWDEADAERLIFVSKADTNGYCNTRVSVRDITKIILEFILSIDPNYYLQKVKPAIRSYKKISPELISAASTPARTLRILARRLKQSGSTVLKEIESPRFQQDLYLSFTCPREILTKICLFTRPASQYLFPDSSKNSKKHILNGEELMKWWGFILDRLLIECFQNDTQAKLRIPGEDPARVRSYLRGMKYPLWQVGDIFTSKENSLAVYNIPLFPDDPKARFIHQLAEEDRLLKVSLSSFWIELQERQEFKLSVTSSVMGISGYSLATPSLFPSSADVIVPKSRKQFRAIKKYITGEEYDTEEGAIEAFTNIRDFLLLRMATNLQSLTGKREHRERNQPVPASNINTLAITMLKPRKKAKALPKT 17825D6EF97C4BB5 17825D6EF97C4BB5 vps75-rtt109-8 3 6 unspecified role unspecified role bait bait His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecolx Escherichia coli 8 unspecified role unspecified role prey prey ecolx Escherichia coli physical association physical association vps75-3 4 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction h3tail-rtt109-1 1 7 enzyme target enzyme target substrate substrate unspecified role unspecified role in vitro In vitro 8 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli acetylation acetylation reaction acetylation vps75-4 5 6 unspecified role unspecified role unspecified role unspecified role Region 1-259 Region 1-259 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction vps75-5 2 6 unspecified role unspecified role unspecified role unspecified role P53853:p.[Cys21Glu;Val25Ser;Ile28Glu;Val32Glu] C21E/V25S/I28E/V32E mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain V E certain certain sequence position certain certain certain sequence position certain I E certain certain sequence position certain certain certain sequence position certain V S certain certain sequence position certain certain certain sequence position certain C E This feature has been corrected as a result of our quality control procedures. The original label was 'C21E/V25S/I28E/V32E'. Wed May 02 15:36:51 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys21glu,val25ser,ile28glu,val32glu' Tue Jun 30 15:48:46 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Cys21Glu;Val25Ser;Ile28Glu;Val32Glu]' ecolx Escherichia coli direct interaction direct interaction