DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural basis for histone H2B deubiquitination by the SAGA DUB module. Structural basis for histone H2B deubiquitination by the SAGA DUB module. Science (New York, N.Y.) 2016 imex curation Morgan MT., Haj-Yahya M., Ringel AE., Bandi P., Brik A., Wolberger C. 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 Morgan MT., Haj-Yahya M., Ringel AE., Bandi P., Brik A., Wolberger C. DIP original experiment: DIP-269078X Science (New York, N.Y.) 2016 IMEx Structural basis for histone H2B deubiquitination by the SAGA DUB module. Structural basis for histone H2B deubiquitination by the SAGA DUB module. Structural basis for histone H2B deubiquitination by the SAGA DUB module. Science (New York, N.Y.) 2016 imex curation Morgan MT., Haj-Yahya M., Ringel AE., Bandi P., Brik A., Wolberger C. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Morgan MT., Haj-Yahya M., Ringel AE., Bandi P., Brik A., Wolberger C. DIP original experiment: DIP-269079X Science (New York, N.Y.) 2016 IMEx Structural basis for histone H2B deubiquitination by the SAGA DUB module. Structural basis for histone H2B deubiquitination by the SAGA DUB module. Structural basis for histone H2B deubiquitination by the SAGA DUB module. Science (New York, N.Y.) 2016 imex curation Morgan MT., Haj-Yahya M., Ringel AE., Bandi P., Brik A., Wolberger C. Only protein-protein interactions in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Morgan MT., Haj-Yahya M., Ringel AE., Bandi P., Brik A., Wolberger C. DIP original experiment: DIP-269080X Science (New York, N.Y.) 2016 IMEx Structural basis for histone H2B deubiquitination by the SAGA DUB module. ubp8_yeast Ubiquitin carboxyl-terminal hydrolase 8 UBP8 YMR223W YM9959.05 Ubiquitin-specific-processing protease 8 Deubiquitinating enzyme 8 Ubiquitin thioesterase 8 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSICPHIQQVFQNEKSKDGVLKTCNAARYILNHSVPKEKFLNTMKCGTCHEINSGATFMCLQCGFCGCWNHSHFLSHSKQIGHIFGINSNNGLLFCFKCEDYIGNIDLINDAILAKYWDDVCTKTMVPSMERRDGLSGLINMGSTCFMSSILQCLIHNPYFIRHSMSQIHSNNCKVRSPDKCFSCALDKIVHELYGALNTKQASSSSTSTNRQTGFIYLLTCAWKINQNLAGYSQQDAHEFWQFIINQIHQSYVLDLPNAKEVSRANNKQCECIVHTVFEGSLESSIVCPGCQNNSKTTIDPFLDLSLDIKDKKKLYECLDSFHKKEQLKDFNYHCGECNSTQDAIKQLGIHKLPSVLVLQLKRFEHLLNGSNRKLDDFIEFPTYLNMKNYCSTKEKDKHSENGKVPDIIYELIGIVSHKGTVNEGHYIAFCKISGGQWFKFNDSMVSSISQEEVLKEQAYLLFYTIRQVN BC632F12FBD0F73C BC632F12FBD0F73C ubiq_yeast Ubiquitin UBI1 RPL40A YIL148W UBI2 RPL40B YKR094C UBI3 RPS31 YLR167W L9470.14 UBI4 SCD2 YLL039C protein protein yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG obsolete protein 9AC936269D38403E h4_xenla Histone H4 protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG DIP protein P62799 original sequence version: 90 DIP protein P62799 original sequence version: 50 DIP protein P62799 original sequence version: 53 DIP protein P62799 original sequence version: 68 DIP protein P62799 original sequence version: 91 DIP protein P62799 original sequence version: 109 A9E5DFD3F8B97598 sgf73_yeast SAGA-associated factor 73 YGL066W SGF73 73 kDa SAGA-associated factor SAGA histone acetyltransferase complex 73 kDa subunit protein protein yeast Saccharomyces cerevisiae Baker's yeast MRSGDAEIKGIKPKVIEEYSLSQGSGPSNDSWKSLMSSAKDTPLQYDHMNRESLKKYFNPNAQLIEDPLDKPIQYRVCEKCGKPLALTAIVDHLENHCAGASGKSSTDPRDESTRETIRNGVESTGRNNNDDDNSNDNNNDDDDDDDNDDNEDDDDADDDDDNSNGANYKKNDSSFNPLKRSTSMESANTPNMDTKRSKTGTPQTFSSSIKKQKKVKQRNPTEKHLIDFNKQCGVELPEGGYCARSLTCKSHSMGAKRAVSGRSKPYDVLLADYHREHQTKIGAAAEKRAKQQELQKLQKQIQKEQKKHTQQQKQGQRSKQRNVNGGKSAKNGGKSTVHNGNNINEIGHVNLTPEEETTQVLNGVSRSFPLPLESTVLSSVRYRTKYFRMREMFASSFSVKPGYTSPGYGAIHSRVGCLDLDRTTDYKFRVRTPQPINHLTNQNLNPKQIQRLQQQRALQAQLLSQQQQQQQQQQQHHSPQAQAQASTQQPTQGMVPNHFPGGATNSSFNANVSSKQIQQQQQQQQHKSQDTGLTPLEIQSQQQKLRQQQLQQQKFEAAASYLANATKLMQESNQDSHLSGTHNNNSSKNGNNNLMTMKASISSPNTSVNSIQSPPSVNSVNGSGQGVSTGINVSGNNGRIEVGIGNSVNPYNGRIN 4618E2E47824321D 4618E2E47824321D sus1_yeast Transcription and mRNA export factor SUS1 SUS1 YBR111W-A protein protein yeast Saccharomyces cerevisiae Baker's yeast MTMDTAQLKSQIQQYLVESGNYELISNELKARLLQEGWVDKVKDLTKSEMNINESTNFTQILSTVEPKALEMVSDSTRETVLKQIREFLEEIVDTQ DB0DA0C9DC13FB21 DB0DA0C9DC13FB21 h2a1_xenla Histone H2A type 1 protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MSGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGGVTIAQGGVLPNIQSVLLPKKTESAKSAKSK DIP protein P06897 original sequence version: 78 DIP protein P06897 original sequence version: 122 09946ABF27FA52A9 h32_xenla Histone H3.2 protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA DIP protein P84233 original sequence version: 76 DIP protein P84233 original sequence version: 53 DIP protein P84233 original sequence version: 77 DIP protein P84233 original sequence version: 95 6FD8508EA50A0EEC h2b11_xenla Histone H2B 1.1 protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MPEPAKSAPAPKKGSKKAVTKTQKKDGKKRRKSRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK DIP protein P02281 original sequence version: 91 DIP protein P02281 original sequence version: 111 DIP protein P02281 original sequence version: 126 DA6C122EC8359FD9 sgf11_yeast SAGA-associated factor 11 SGF11 11 kDa SAGA-associated factor YPL047W protein protein yeast Saccharomyces cerevisiae Baker's yeast MTEETITIDSISNGILNNLLTTLIQDIVARETTQQQLLKTRYPDLRSYYFDPNGSLDINGLQKQQESSQYIHCENCGRDVSANRLAAHLQRCLSRGARR 31CBBD4CAA18F3F9 31CBBD4CAA18F3F9 h2a1_xenla-h2b11_xenla-1 1 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role Region 1-104 Region 1-104 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 4 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 10 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association h2a1_xenla-h2b11_xenla-2 2 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role Region 1-104 Region 1-104 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 4 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 10 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association h2a1_xenla-h2b11_xenla-3 3 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role Region 1-104 Region 1-104 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 4 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 10 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association