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 the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nature structural & molecular biology 2010 imex curation Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions 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. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nature structural & molecular biology 2010 imex curation Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions 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. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nature structural & molecular biology 2010 imex curation Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. 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 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. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nature structural & molecular biology 2010 imex curation Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions 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. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nature structural & molecular biology 2010 imex curation Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. 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 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. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nature structural & molecular biology 2010 imex curation Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. 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 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. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nature structural & molecular biology 2010 imex curation Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. 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 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. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nature structural & molecular biology 2010 imex curation Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions 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. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nature structural & molecular biology 2010 imex curation Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions 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. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nature structural & molecular biology 2010 imex curation Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions 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. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nature structural & molecular biology 2010 imex curation Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions 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. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nature structural & molecular biology 2010 imex curation Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions 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. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nature structural & molecular biology 2010 imex curation Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. 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 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. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nature structural & molecular biology 2010 imex curation Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. Only protein-protein interactions 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. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nature structural & molecular biology 2010 imex curation Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. 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 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. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nature structural & molecular biology 2010 imex curation Choi WS., Jeong BC., Joo YJ., Lee MR., Kim J., Eck MJ., Song HK. 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 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. hiaa N-end rule peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) HIAA 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 raaa N-end rule peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) RAAA rdaa N-end rule peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) RDAA rlaa N-end rule peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) RLAA rlges N-end rule peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) RLGES rraa N-end rule peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) RRAA 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 33E4CD3A031AF523 reaa N-end rule peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) REAA rlges-ubr1-1 7 23 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 25 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 ecolx Escherichia coli direct interaction direct interaction reaa-ubr1-1 8 26 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 25 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 ecolx Escherichia coli direct interaction direct interaction rdaa-ubr1-1 5 21 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 25 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 ecolx Escherichia coli direct interaction direct interaction kiaa-ubr1-1 14 18 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 25 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 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 D A This feature has been corrected as a result of our quality control procedures. The original label was 'D142A'. Wed May 02 17:42:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp142ala' Tue Jun 30 17:44:10 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp142Ala' 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 D A This feature has been corrected as a result of our quality control procedures. The original label was 'D179A'. Wed May 02 20:30:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp179ala' Tue Jun 30 20:25:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp179Ala' ecolx Escherichia coli direct interaction direct interaction riaaa-ubr1-1 13 19 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 25 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 ecolx Escherichia coli direct interaction direct interaction hiaa-ubr1-1 9 17 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 25 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 D A This feature has been corrected as a result of our quality control procedures. The original label was 'D179A'. Wed May 02 19:41:42 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp179ala' Tue Jun 30 18:55:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp179Ala' 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 D A This feature has been corrected as a result of our quality control procedures. The original label was 'D142A'. Wed May 02 16:55:57 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp142ala' Tue Jun 30 15:53:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp142Ala' UBR-box domain Region 115-194 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 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 T A This feature has been corrected as a result of our quality control procedures. The original label was 'T144A'. Wed May 02 19:59:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr144ala' Tue Jun 30 19:27:16 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr144Ala' ecolx Escherichia coli direct interaction direct interaction reaa-ubr1-2 15 26 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 25 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 ecolx Escherichia coli direct interaction direct interaction raaa-ubr1-1 2 20 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 25 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 ecolx Escherichia coli direct interaction direct interaction kiaa-ubr1-2 16 18 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 25 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 ecolx Escherichia coli direct interaction direct interaction rlges-ubr1-2 4 23 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 25 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 ecolx Escherichia coli direct interaction direct interaction rraa-ubr1-1 11 24 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 25 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 ecolx Escherichia coli direct interaction direct interaction rlaa-ubr1-1 12 22 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 25 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 ecolx Escherichia coli direct interaction direct interaction hiaa-ubr1-2 6 17 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 25 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 ecolx Escherichia coli direct interaction direct interaction rdaa-ubr1-2 10 21 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 25 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 ecolx Escherichia coli direct interaction direct interaction riaaa-ubr1-2 1 19 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 in vitro In vitro 25 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 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 D A This feature has been corrected as a result of our quality control procedures. The original label was 'D142A'. Wed May 02 19:36:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp142ala' Tue Jun 30 17:55:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp142Ala' 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 D A This feature has been corrected as a result of our quality control procedures. The original label was 'D179A'. Wed May 02 18:01:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp179ala' Tue Jun 30 17:32:20 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp179Ala' ecolx Escherichia coli direct interaction direct interaction rraa-ubr1-2 3 24 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 25 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 ecolx Escherichia coli direct interaction direct interaction