DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ choi-2010-34 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. DIP original experiment: DIP-218349X Nature structural & molecular biology 2010 IMEx Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions imex curation choi-2010-35 in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. DIP original experiment: DIP-218362X Nature structural & molecular biology 2010 IMEx Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions imex curation choi-2010-36 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. DIP original experiment: DIP-218354X Nature structural & molecular biology 2010 IMEx Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions imex curation choi-2010-37 in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. DIP original experiment: DIP-218358X Nature structural & molecular biology 2010 IMEx Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions imex curation choi-2010-38 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. DIP original experiment: DIP-218350X Nature structural & molecular biology 2010 IMEx Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions imex curation choi-2010-39 in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. DIP original experiment: DIP-218359X Nature structural & molecular biology 2010 IMEx Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions imex curation choi-2010-40 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. DIP original experiment: DIP-218355X Nature structural & molecular biology 2010 IMEx Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions imex curation choi-2010-41 in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. DIP original experiment: DIP-218363X Nature structural & molecular biology 2010 IMEx Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions imex curation choi-2010-42 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. DIP original experiment: DIP-218351X Nature structural & molecular biology 2010 IMEx Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions imex curation choi-2010-43 in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. DIP original experiment: DIP-218356X Nature structural & molecular biology 2010 IMEx Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions imex curation choi-2010-44 in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. DIP original experiment: DIP-218360X Nature structural & molecular biology 2010 IMEx Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions imex curation choi-2010-45 in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. DIP original experiment: DIP-218364X Nature structural & molecular biology 2010 IMEx Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions imex curation choi-2010-46 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. DIP original experiment: DIP-218352X Nature structural & molecular biology 2010 IMEx Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions imex curation choi-2010-47 in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. DIP original experiment: DIP-218361X Nature structural & molecular biology 2010 IMEx Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions imex curation choi-2010-48 in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. DIP original experiment: DIP-218357X Nature structural & molecular biology 2010 IMEx Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions imex curation choi-2010-49 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. DIP original experiment: DIP-218353X Nature structural & molecular biology 2010 IMEx Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions imex curation rlges N-end rule peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) RLGES ubr1_yeast E3 ubiquitin-protein ligase UBR1 UBR1 PTR1 N-recognin-1 N-end-recognizing protein RING-type E3 ubiquitin transferase UBR1 G7168 YGR184C protein protein yeast Saccharomyces cerevisiae Baker's yeast MSVADDDLGSLQGHIRRTLRSIHNLPYFRYTRGPTERADMSRALKEFIYRYLYFVISNSGENLPTLFNAHPKQKLSNPELTVFPDSLEDAVDIDKITSQQTIPFYKIDESRIGDVHKHTGRNCGRKFKIGEPLYRCHECGCDDTCVLCIHCFNPKDHVNHHVCTDICTEFTSGICDCGDEEAWNSPLHCKAEEQENDISEDPATNADIKEEDVWNDSVNIALVELVLAEVFDYFIDVFNQNIEPLPTIQKDITIKLREMTQQGKMYERAQFLNDLKYENDYMFDGTTTAKTSPSNSPEASPSLAKIDPENYTVIIYNDEYHNYSQATTALRQGVPDNVHIDLLTSRIDGEGRAMLKCSQDLSSVLGGFFAVQTNGLSATLTSWSEYLHQETCKYIILWITHCLNIPNSSFQTTFRNMMGKTLCSEYLNATECRDMTPVVEKYFSNKFDKNDPYRYIDLSILADGNQIPLGHHKILPESSTHSLSPLINDVETPTSRTYSNTRLQHILYFDNRYWKRLRKDIQNVIIPTLASSNLYKPIFCQQVVEIFNHITRSVAYMDREPQLTAIRECVVQLFTCPTNAKNIFENQSFLDIVWSIIDIFKEFCKVEGGVLIWQRVQKSNLTKSYSISFKQGLYTVETLLSKVHDPNIPLRPKEIISLLTLCKLFNGAWKIKRKEGEHVLHEDQNFISYLEYTTSIYSIIQTAEKVSEKSKDSIDSKLFLNAIRIISSFLGNRSLTYKLIYDSHEVIKFSVSHERVAFMNPLQTMLSFLIEKVSLKDAYEALEDCSDFLKISDFSLRSVVLCSQIDVGFWVRNGMSVLHQASYYKNNPELGSYSRDIHLNQLAILWERDDIPRIIYNILDRWELLDWFTGEVDYQHTVYEDKISFIIQQFIAFIYQILTERQYFKTFSSLKDRRMDQIKNSIIYNLYMKPLSYSKLLRSVPDYLTEDTTEFDEALEEVSVFVEPKGLADNGVFKLKASLYAKVDPLKLLNLENEFESSATIIKSHLAKDKDEIAKVVLIPQVSIKQLDKDALNLGAFTRNTVFAKVVYKLLQVCLDMEDSTFLNELLHLVHGIFRDDELINGKDSIPEAYLSKPICNLLLSIANAKSDVFSESIVRKADYLLEKMIMKKPNELFESLIASFGNQYVNDYKDKKLRQGVNLQETEKERKRRLAKKHQARLLAKFNNQQTKFMKEHESEFDEQDNDVDMVGEKVYESEDFTCALCQDSSSTDFFVIPAYHDHSPIFRPGNIFNPNEFMPMWDGFYNDDEKQAYIDDDVLEALKENGSCGSRKVFVSCNHHIHHNCFKRYVQKKRFSSNAFICPLCQTFSNCTLPLCQTSKANTGLSLDMFLESELSLDTLSRLFKPFTEENYRTINSIFSLMISQCQGFDKAVRKRANFSHKDVSLILSVHWANTISMLEIASRLEKPYSISFFRSREQKYKTLKNILVCIMLFTFVIGKPSMEFEPYPQQPDTVWNQNQLFQYIVRSALFSPVSLRQTVTEALTTFSRQFLRDFLQGLSDAEQVTKLYAKASKIGDVLKVSEQMLFALRTISDVRMEGLDSESIIYDLAYTFLLKSLLPTIRRCLVFIKVLHELVKDSENETLVINGHEVEEELEFEDTAEFVNKALKMITEKESLVDLLTTQESIVSHPYLENIPYEYCGIIKLIDLSKYLNTYVTQSKEIKLREERSQHMKNADNRLDFKICLTCGVKVHLRADRHEMTKHLNKNCFKPFGAFLMPNSSEVCLHLTQPPSNIFISAPYLNSHGEVGRNAMRRGDLTTLNLKRYEHLNRLWINNEIPGYISRVMGDEFRVTILSNGFLFAFNREPRPRRIPPTDEDDEDMEEGEDGFFTEGNDEMDVDDETGQAANLFGVGAEGIAGGGVRDFFQFFENFRNTLQPQGNGDDDAPQNPPPILQFLGPQFDGATIIRNTNPRNLDEDDSDDNDDSDEREIW 33E4CD3A031AF523 reaa N-end rule peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) REAA rdaa N-end rule peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) RDAA kiaa N-end rule peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) KIAA riaaa N-end rule peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) RIAAA hiaa N-end rule peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) HIAA raaa N-end rule peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) RAAA rraa N-end rule peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) RRAA rlaa N-end rule peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) RLAA rlges-ubr1-1 3214379 N/A 3214395 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3214396 unspecified role unspecified role unspecified role unspecified role UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false reaa-ubr1-1 3214380 N/A 3214397 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3214396 unspecified role unspecified role unspecified role unspecified role UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false rdaa-ubr1-1 3214381 N/A 3214398 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3214396 unspecified role unspecified role unspecified role unspecified role UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false kiaa-ubr1-1 3214382 N/A 3214399 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3214396 unspecified role unspecified role unspecified role unspecified role UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false P19812:p.Asp142Ala D142A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false P19812:p.Asp179Ala D179A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false riaaa-ubr1-1 3214383 N/A 3214400 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3214396 unspecified role unspecified role unspecified role unspecified role UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false hiaa-ubr1-1 3214384 N/A 3214401 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3214396 unspecified role unspecified role unspecified role unspecified role P19812:p.Asp179Ala D179A mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false P19812:p.Asp142Ala D142A mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false P19812:p.Thr144Ala T144A mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false reaa-ubr1-2 3214385 N/A 3214397 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3214396 unspecified role unspecified role unspecified role unspecified role UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false raaa-ubr1-1 3214386 N/A 3214402 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3214396 unspecified role unspecified role unspecified role unspecified role UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false kiaa-ubr1-2 3214387 N/A 3214399 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3214396 unspecified role unspecified role unspecified role unspecified role UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false rlges-ubr1-2 3214388 N/A 3214395 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3214396 unspecified role unspecified role unspecified role unspecified role UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false rraa-ubr1-1 3214389 N/A 3214403 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3214396 unspecified role unspecified role unspecified role unspecified role UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false rlaa-ubr1-1 3214390 N/A 3214404 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3214396 unspecified role unspecified role unspecified role unspecified role UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false hiaa-ubr1-2 3214391 N/A 3214401 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3214396 unspecified role unspecified role unspecified role unspecified role UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false rdaa-ubr1-2 3214392 N/A 3214398 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3214396 unspecified role unspecified role unspecified role unspecified role UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false riaaa-ubr1-2 3214393 N/A 3214400 unspecified role unspecified role unspecified role unspecified role Region 1-4 Region 1-4 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false in vitro In vitro N/A 3214396 unspecified role unspecified role unspecified role unspecified role UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false P19812:p.Asp142Ala D142A mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false P19812:p.Asp179Ala D179A mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false rraa-ubr1-2 3214394 N/A 3214403 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3214396 unspecified role unspecified role unspecified role unspecified role UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false