DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Structure (London, England : 1993) 2016 imex curation Fetics S., Thureau A., Campanacci V., Aumont-Nicaise M., Dang I., Gautreau A., Pérez J., Cherfils J. Only protein-protein interactions in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Fetics S., Thureau A., Campanacci V., Aumont-Nicaise M., Dang I., Gautreau A., Pérez J., Cherfils J. DIP original experiment: DIP-268444X Structure (London, England : 1993) 2016 IMEx Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Structure (London, England : 1993) 2016 imex curation Fetics S., Thureau A., Campanacci V., Aumont-Nicaise M., Dang I., Gautreau A., Pérez J., Cherfils J. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Fetics S., Thureau A., Campanacci V., Aumont-Nicaise M., Dang I., Gautreau A., Pérez J., Cherfils J. DIP original experiment: DIP-268445X Structure (London, England : 1993) 2016 IMEx Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Structure (London, England : 1993) 2016 imex curation Fetics S., Thureau A., Campanacci V., Aumont-Nicaise M., Dang I., Gautreau A., Pérez J., Cherfils J. 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 Fetics S., Thureau A., Campanacci V., Aumont-Nicaise M., Dang I., Gautreau A., Pérez J., Cherfils J. DIP original experiment: DIP-268443X Structure (London, England : 1993) 2016 IMEx Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Structure (London, England : 1993) 2016 imex curation Fetics S., Thureau A., Campanacci V., Aumont-Nicaise M., Dang I., Gautreau A., Pérez J., Cherfils J. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Fetics S., Thureau A., Campanacci V., Aumont-Nicaise M., Dang I., Gautreau A., Pérez J., Cherfils J. DIP original experiment: DIP-268446X Structure (London, England : 1993) 2016 IMEx Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Structure (London, England : 1993) 2016 imex curation Fetics S., Thureau A., Campanacci V., Aumont-Nicaise M., Dang I., Gautreau A., Pérez J., Cherfils J. 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 Fetics S., Thureau A., Campanacci V., Aumont-Nicaise M., Dang I., Gautreau A., Pérez J., Cherfils J. DIP original experiment: DIP-268447X Structure (London, England : 1993) 2016 IMEx Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. q7z6k5-1 Arpin ARPIN C15orf38 Arp2/3 inhibition protein protein protein human Homo sapiens Human MSRIYHDGALRNKAVQSVRLPGAWDPAAHQGGNGVLLEGELIDVSRHSILDTHGRKERYYVLYIRPSHIHRRKFDAKGNEIEPNFSATRKVNTGFLMSSYKVEAKGDTDRLTPEALKGLVNKPELLALTESLTPDHTVAFWMPESEMEVMELELGAGVRLKTRGDGPFLDSLAKLEAGTVTKCNFTGDGKTGASWTDNIMAQKCSKGAAAEIREQGDGAEDEEWDD DIP protein Q7Z6K5-1 original sequence version: 75 DIP protein Q7Z6K5-1 original sequence version: 96 tnks2_human Poly [ADP-ribose] polymerase tankyrase-2 TNKS2 PARP5B TANK2 TNKL Poly [ADP-ribose] polymerase 5B TNKS-2 TRF1-interacting ankyrin-related ADP-ribose polymerase 2 Tankyrase II Tankyrase-like protein Tankyrase-related protein ADP-ribosyltransferase diphtheria toxin-like 6 Protein poly-ADP-ribosyltransferase tankyrase-2 Tankyrase-2 protein protein human Homo sapiens Human MSGRRCAGGGAACASAAAEAVEPAARELFEACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLADPSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNKSAIDLAPTPQLKERLAYEFKGHSLLQAAREADVTRIKKHLSLEMVNFKHPQTHETALHCAAASPYPKRKQICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTALQMGNENVQQLLQEGISLGNSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDIQDLLRGDAALLDAAKKGCLARVKKLSSPDNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADDVSALLTAAMPPSALPSCYKPQVLNGVRSPGATADALSSGPSSPSSLSAASSLDNLSGSFSELSSVVSSSGTEGASSLEKKEVPGVDFSITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERLISGQQGLNPYLTLNTSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLLFCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIMRPEGMVDG DIP protein Q9H2K2 original sequence version: 154 DIP protein Q9H2K2 original sequence version: 107 4C8B3B8D97CEF704 arpin-tnks2-1 3 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role Region 489-649 Region 489-649 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction arpin-tnks2-2 5 6 unspecified role unspecified role unspecified role unspecified role Region 211-222 Region 211-222 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 7 unspecified role unspecified role unspecified role unspecified role Region 489-649 Region 489-649 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction arpin-tnks2-3 4 6 unspecified role unspecified role unspecified role unspecified role Q7Z6K5-1:p.Arg213Ala R213A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R213A'. Wed May 02 17:51:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg213ala' Tue Jun 30 16:57:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg213Ala' Region 211-222 Region 211-222 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 7 unspecified role unspecified role unspecified role unspecified role Region 489-649 Region 489-649 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction arpin-tnks2-4 1 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role Region 489-649 Region 489-649 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction arpin-tnks2-5 2 6 unspecified role unspecified role unspecified role unspecified role Q7Z6K5-1:p.Arg213Ala R213A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R213A'. Wed May 02 16:57:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg213ala' Tue Jun 30 19:15:46 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg213Ala' ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role Region 489-649 Region 489-649 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction