{"corpus_id":22553668,"paper_sha":"b828fe2683d7bfab1a782dc1ac829ffeb6f8c33d","doi":"10.1074/JBC.M501677200","arxiv_id":null,"pmid":15824120,"pmcid":null,"mag_id":2131898220,"dblp_id":null,"acl_id":null,"title":"SUMOylation of the Polyglutamine Repeat Protein, Ataxin-1, Is Dependent on a Functional Nuclear Localization Signal*","year":2005,"publication_date":"2005-06-10","venue":"Journal of Biological Chemistry","journal":{"name":"Journal of Biological Chemistry","pages":"21942 - 21948","volume":"280"},"journal_issn":null,"journal_title":null,"publication_types":["JournalArticle"],"pubmed_pub_types":["Journal Article","Research Support, N.I.H., Extramural","Research Support, U.S. Gov't, P.H.S."],"s2_fields_of_study":["Biology","Medicine"],"reference_count":54,"citation_count":97,"influential_citation_count":4,"is_open_access":true,"arxiv_categories":null,"arxiv_license":null,"arxiv_journal_ref":null,"mesh_headings":[{"d":"Active Transport, Cell Nucleus","mj":false,"ui":"D021581"},{"d":"Amino Acid Motifs","mj":false,"ui":"D020816"},{"d":"Animals","mj":false,"ui":"D000818"},{"d":"Antigens, Nuclear","mj":false,"qs":[{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D034961"},{"d":"Ataxin-1","mj":false,"ui":"D000067696"},{"d":"Ataxins","mj":false,"ui":"D000067528"},{"d":"Autoantigens","mj":false,"qs":[{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D001324"},{"d":"Binding Sites","mj":false,"ui":"D001665"},{"d":"COS Cells","mj":false,"ui":"D019556"},{"d":"Cell Line","mj":false,"ui":"D002460"},{"d":"Cell Nucleus","mj":false,"qs":[{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D002467"},{"d":"Detergents","mj":false,"qs":[{"q":"pharmacology","mj":false,"ui":"Q000494"}],"ui":"D003902"},{"d":"Immunoprecipitation","mj":false,"ui":"D047468"},{"d":"Lysine","mj":false,"qs":[{"q":"chemistry","mj":false,"ui":"Q000737"}],"ui":"D008239"},{"d":"Microscopy, Fluorescence","mj":false,"ui":"D008856"},{"d":"Neoplasm Proteins","mj":false,"qs":[{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D009363"},{"d":"Nerve Tissue Proteins","mj":false,"qs":[{"q":"chemistry","mj":false,"ui":"Q000737"},{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D009419"},{"d":"Nuclear Localization Signals","mj":false,"ui":"D019913"},{"d":"Nuclear Proteins","mj":false,"qs":[{"q":"chemistry","mj":false,"ui":"Q000737"},{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D009687"},{"d":"Octoxynol","mj":false,"qs":[{"q":"pharmacology","mj":false,"ui":"Q000494"}],"ui":"D017830"},{"d":"Peptides","mj":false,"qs":[{"q":"chemistry","mj":false,"ui":"Q000737"},{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D010455"},{"d":"Phosphorylation","mj":false,"ui":"D010766"},{"d":"Plasmids","mj":false,"qs":[{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D010957"},{"d":"Protein Binding","mj":false,"ui":"D011485"},{"d":"Protein Structure, Tertiary","mj":false,"ui":"D017434"},{"d":"Small Ubiquitin-Related Modifier Proteins","mj":false,"qs":[{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D025841"},{"d":"Transcription Factors","mj":false,"qs":[{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D014157"},{"d":"Transcription, Genetic","mj":false,"ui":"D014158"},{"d":"Transfection","mj":false,"ui":"D014162"},{"d":"Tumor Suppressor Proteins","mj":false,"ui":"D025521"}],"chemicals":[{"n":"ATXN1 protein, human","ui":"C000593749","reg":"0"},{"n":"Antigens, Nuclear","ui":"D034961","reg":"0"},{"n":"Ataxin-1","ui":"D000067696","reg":"0"},{"n":"Ataxins","ui":"D000067528","reg":"0"},{"n":"Autoantigens","ui":"D001324","reg":"0"},{"n":"Detergents","ui":"D003902","reg":"0"},{"n":"Neoplasm Proteins","ui":"D009363","reg":"0"},{"n":"Nerve Tissue Proteins","ui":"D009419","reg":"0"},{"n":"Nuclear Localization Signals","ui":"D019913","reg":"0"},{"n":"Nuclear Proteins","ui":"D009687","reg":"0"},{"n":"Peptides","ui":"D010455","reg":"0"},{"n":"Small Ubiquitin-Related Modifier Proteins","ui":"D025841","reg":"0"},{"n":"Transcription Factors","ui":"D014157","reg":"0"},{"n":"Tumor Suppressor Proteins","ui":"D025521","reg":"0"},{"n":"SP100 protein, human","ui":"C066642","reg":"135844-47-2"},{"n":"polyglutamine","ui":"C097188","reg":"26700-71-0"},{"n":"Octoxynol","ui":"D017830","reg":"9002-93-1"},{"n":"Lysine","ui":"D008239","reg":"K3Z4F929H6"}],"comments_corrections":null,"source_flags":5,"s2_open_access_pdf_url":"http://www.jbc.org/article/S0021925820691372/pdf","s2_open_access_landing_url":"https://www.semanticscholar.org/paper/b828fe2683d7bfab1a782dc1ac829ffeb6f8c33d","s2_open_access_license":"CCBY","s2_open_access_status":"HYBRID","pmc_open_access_pdf_url":null,"pmc_open_access_landing_url":null,"pmc_open_access_license":null,"pmc_open_access_status":null,"unpaywall_open_access_pdf_url":null,"unpaywall_open_access_landing_url":null,"unpaywall_open_access_license":null,"unpaywall_open_access_status":null,"abstract":"SUMO (small ubiquitin-like modifier) is a member of the ubiquitin family of proteins. SUMO targets include proteins involved in numerous roles including nuclear transport and transcriptional regulation. The previous finding that mutant ataxin-1[82Q] disrupted promyelocytic leukemia (PML) oncogenic domains prompted us to determine whether ataxin-1 disrupts another component of PML oncogenic domains, Sp100 (100-kDa Speckled protein). Similar to the PML protein, mutant ataxin-1[82Q] redistributed Sp100 to mutant ataxin-1[82Q] nuclear inclusions. Based on the ability of PML and Sp100 to be covalently modified by SUMO, we investigated the ability of ataxin-1 to be SUMOylated. SUMO-1 was found to covalently modify the polyglutamine repeat protein ataxin-1. There was a decrease in ataxin-1 SUMOylation in the presence of the expanded polyglutamine tract, ataxin-1[82Q]. The phospho-mutant, ataxin-1[82Q]-S776A, restored SUMO levels to those of wild-type ataxin-1[30Q]. SUMOylation of ataxin-1 was dependent on a functional nuclear localization signal. Ataxin-1 SUMOylation was mapped to at least five lysine residues. Lys16, Lys194 preceding the polyglutamine tract, Lys610/Lys697 in the C-terminal ataxin high mobility group domain, and Lys746 all contribute to ataxin-1 SUMOylation.","claims":[{"public_id":"cl_b1ab0160bb0bf72f9f337ea57152c599","status":"active","text":"At least five lysine residues, including Lys16, Lys194, Lys610/Lys697, and Lys746, contribute to ataxin-1 SUMOylation.","confidence":0.95,"contributors":[{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["extraction"],"url":"https://sah.borca.ai/u/12632b8b5f"}],"url":"https://sah.borca.ai/claims/cl_b1ab0160bb0bf72f9f337ea57152c599"},{"public_id":"cl_3f9175c69ff6150cc71ab373e42ecf55","status":"active","text":"Ataxin-1 SUMOylation depends on a functional nuclear localization signal.","confidence":0.97,"contributors":[{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous 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