DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Ubiquitin chain conformation regulates recognition and activity of interacting proteins. Ubiquitin chain conformation regulates recognition and activity of interacting proteins. Nature 2012 imex curation Ye Y., Blaser G., Horrocks MH., Ruedas-Rama MJ., Ibrahim S., Zhukov AA., Orte A., Klenerman D., Jackson SE., Komander D. Only protein-protein interactions in vitro In vitro fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Ye Y., Blaser G., Horrocks MH., Ruedas-Rama MJ., Ibrahim S., Zhukov AA., Orte A., Klenerman D., Jackson SE., Komander D. DIP original experiment: DIP-252120X Nature 2012 IMEx Ubiquitin chain conformation regulates recognition and activity of interacting proteins. Ubiquitin chain conformation regulates recognition and activity of interacting proteins. Ubiquitin chain conformation regulates recognition and activity of interacting proteins. Nature 2012 imex curation Ye Y., Blaser G., Horrocks MH., Ruedas-Rama MJ., Ibrahim S., Zhukov AA., Orte A., Klenerman D., Jackson SE., Komander D. Only protein-protein interactions in vitro In vitro fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Ye Y., Blaser G., Horrocks MH., Ruedas-Rama MJ., Ibrahim S., Zhukov AA., Orte A., Klenerman D., Jackson SE., Komander D. DIP original experiment: DIP-252119X Nature 2012 IMEx Ubiquitin chain conformation regulates recognition and activity of interacting proteins. Ubiquitin chain conformation regulates recognition and activity of interacting proteins. Ubiquitin chain conformation regulates recognition and activity of interacting proteins. Nature 2012 imex curation Ye Y., Blaser G., Horrocks MH., Ruedas-Rama MJ., Ibrahim S., Zhukov AA., Orte A., Klenerman D., Jackson SE., Komander D. Only protein-protein interactions in vitro In vitro fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Ye Y., Blaser G., Horrocks MH., Ruedas-Rama MJ., Ibrahim S., Zhukov AA., Orte A., Klenerman D., Jackson SE., Komander D. DIP original experiment: DIP-252121X Nature 2012 IMEx Ubiquitin chain conformation regulates recognition and activity of interacting proteins. Ubiquitin chain conformation regulates recognition and activity of interacting proteins. Ubiquitin chain conformation regulates recognition and activity of interacting proteins. Nature 2012 imex curation Ye Y., Blaser G., Horrocks MH., Ruedas-Rama MJ., Ibrahim S., Zhukov AA., Orte A., Klenerman D., Jackson SE., Komander D. Only protein-protein interactions in vitro In vitro fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Ye Y., Blaser G., Horrocks MH., Ruedas-Rama MJ., Ibrahim S., Zhukov AA., Orte A., Klenerman D., Jackson SE., Komander D. DIP original experiment: DIP-252118X Nature 2012 IMEx Ubiquitin chain conformation regulates recognition and activity of interacting proteins. ubiq_human UBIQ_HUMAN protein protein human Homo sapiens Human MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG q9uk80-1 Ubiquitin carboxyl-terminal hydrolase 21 USP21 USP23 Ubiquitin thioesterase 21 Ubiquitin-specific-processing protease 21 PP1490 Deubiquitinating enzyme 21 protein protein human Homo sapiens Human MPQASEHRLGRTREPPVNIQPRVGSKLPFAPRARSKERRNPASGPNPMLRPLPPRPGLPDERLKKLELGRGRTSGPRPRGPLRADHGVPLPGSPPPTVALPLPSRTNLARSKSVSSGDLRPMGIALGGHRGTGELGAALSRLALRPEPPTLRRSTSLRRLGGFPGPPTLFSIRTEPPASHGSFHMISARSSEPFYSDDKMAHHTLLLGSGHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVIGALWHPDSCEAVNPTRFRAVFQKYVPSFSGYSQQDAQEFLKLLMERLHLEINRRGRRAPPILANGPVPSPPRRGGALLEEPELSDDDRANLMWKRYLEREDSKIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKVSLRDCFNLFTKEEELESENAPVCDRCRQKTRSTKKLTVQRFPRILVLHLNRFSASRGSIKKSSVGVDFPLQRLSLGDFASDKAGSPVYQLYALCNHSGSVHYGHYTALCRCQTGWHVYNDSRVSPVSENQVASSEGYVLFYQLMQEPPRCL DIP protein Q9UK80-1 original sequence version: 116 q96fw1-1 Ubiquitin thioesterase OTUB1 OTUB1 OTB1 OTU1 Deubiquitinating enzyme OTUB1 OTU domain-containing ubiquitin aldehyde-binding protein 1 Otubain-1 Ubiquitin-specific-processing protease OTUB1 HSPC263 Otubain-1 protein protein human Homo sapiens Human MAAEEPQQQKQEPLGSDSEGVNCLAYDEAIMAQQDRIQQEIAVQNPLVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSAKSKEDLVSQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVKEFCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHIFPEGSEPKVYLLYRPGHYDILYK DIP protein Q96FW1-1 original sequence version: 98 DIP protein Q96FW1-1 original sequence version: 106 DIP protein Q96FW1-1 original sequence version: 112 stabp_human STAM-binding protein AMSH STAMBP Associated molecule with the SH3 domain of STAM Endosome-associated ubiquitin isopeptidase protein protein human Homo sapiens Human MSDHGDVSLPPEDRVRALSQLGSAVEVNEDIPPRRYFRSGVEIIRMASIYSEEGNIEHAFILYNKYITLFIEKLPKHRDYKSAVIPEKKDTVKKLKEIAFPKAEELKAELLKRYTKEYTEYNEEKKKEAEELARNMAIQQELEKEKQRVAQQKQQQLEQEQFHAFEEMIRNQELEKERLKIVQEFGKVDPGLGGPLVPDLEKPSLDVFPTLTVSSIQPSDCHTTVRPAKPPVVDRSLKPGALSNSESIPTIDGLRHVVVPGRLCPQFLQLASANTARGVETCGILCGKLMRNEFTITHVLIPKQSAGSDYCNTENEEELFLIQDQQGLITLGWIHTHPTQTAFLSSVDLHTHCSYQMMLPESVAIVCSPKFQETGFFKLTDHGLEEISSCRQKGFHPHSKDPPLFCSCSHVTVVDRAVTITDLR DIP protein O95630 original sequence version: 125 DIP protein O95630 original sequence version: 88 DIP protein O95630 original sequence version: 103 7B6E08A245BD9D43 ub-stambp-1 4 8 unspecified role unspecified role unspecified role unspecified role O95630:p.Glu280Ala E280A mutation mutation certain certain sequence position certain certain certain sequence position certain E A This feature has been corrected as a result of our quality control procedures. The original label was 'E280A'. Wed May 02 19:57:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu280ala' Tue Jun 30 20:04:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu280Ala' ecolx Escherichia coli 5 unspecified role unspecified role fluorescence donor fluorescence donor K63Ub K63Ub ubiquitinylated lysine ubiquitinylated lysine certain certain sequence position certain certain certain sequence position certain Alexa488-label Alexa488-label alexa 488 label alexa 488 label c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal ecolx Escherichia coli 5 unspecified role unspecified role fluorescence accept fluorescence acceptor fluorescence accept lys63arg K63R mutation mutation certain certain sequence position certain certain certain sequence position certain Alexa647-label Alexa647-label alexa label alexa label n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal ecolx Escherichia coli direct interaction direct interaction ub-otub1-1 3 7 unspecified role unspecified role unspecified role unspecified role Q96FW1-1:p.Cys91Ala C91A mutation mutation certain certain sequence position certain certain certain sequence position certain C A This feature has been corrected as a result of our quality control procedures. The original label was 'C91A'. Wed May 02 20:26:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys91ala' Tue Jun 30 17:38:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys91Ala' Region 40-271 Region 40-271 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 5 unspecified role unspecified role fluorescence accept fluorescence acceptor fluorescence accept K48Ub K48Ub ubiquitinylated lysine ubiquitinylated lysine certain certain sequence position certain certain certain sequence position certain Alexa647-label Alexa647-label alexa label alexa label c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal ecolx Escherichia coli 5 unspecified role unspecified role fluorescence donor fluorescence donor lys48arg K48R mutation mutation certain certain sequence position certain certain certain sequence position certain Alexa488-label Alexa488-label alexa 488 label alexa 488 label n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal ecolx Escherichia coli direct interaction direct interaction ub-usp21-1 1 6 unspecified role unspecified role unspecified role unspecified role Region 196-565 Region 196-565 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9UK80-1:p.Cys221Ala C221A mutation mutation certain certain sequence position certain certain certain sequence position certain C A This feature has been corrected as a result of our quality control procedures. The original label was 'C221A'. Wed May 02 19:13:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys221ala' Tue Jun 30 17:03:49 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys221Ala' ecolx Escherichia coli 5 unspecified role unspecified role fluorescence accept fluorescence acceptor fluorescence accept K48Ub K48Ub ubiquitinylated lysine ubiquitinylated lysine certain certain sequence position certain certain certain sequence position certain Alexa647-label Alexa647-label alexa label alexa label c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal ecolx Escherichia coli 5 unspecified role unspecified role fluorescence donor fluorescence donor lys48arg K48R mutation mutation certain certain sequence position certain certain certain sequence position certain Alexa488-label Alexa488-label alexa 488 label alexa 488 label n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal ecolx Escherichia coli direct interaction direct interaction ub-usp21-2 2 6 unspecified role unspecified role unspecified role unspecified role Q9UK80-1:p.Cys221Ala C221A mutation mutation certain certain sequence position certain certain certain sequence position certain C A This feature has been corrected as a result of our quality control procedures. The original label was 'C221A'. Wed May 02 16:33:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys221ala' Tue Jun 30 16:13:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys221Ala' Region 196-565 Region 196-565 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 5 unspecified role unspecified role fluorescence donor fluorescence donor K63Ub K63Ub ubiquitinylated lysine ubiquitinylated lysine certain certain sequence position certain certain certain sequence position certain Alexa488-label Alexa488-label alexa 488 label alexa 488 label c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal ecolx Escherichia coli 5 unspecified role unspecified role fluorescence accept fluorescence acceptor fluorescence accept lys63arg K63R mutation mutation certain certain sequence position certain certain certain sequence position certain Alexa647-label Alexa647-label alexa label alexa label n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal ecolx Escherichia coli direct interaction direct interaction