{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,26]],"date-time":"2026-02-26T20:33:51Z","timestamp":1772138031057,"version":"3.50.1"},"reference-count":59,"publisher":"Oxford University Press (OUP)","issue":"3","license":[{"start":{"date-parts":[[2019,6,4]],"date-time":"2019-06-04T00:00:00Z","timestamp":1559606400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"name":"Informatics Institute of the School of Medicine at UAB"},{"DOI":"10.13039\/501100012226","name":"Fundamental Research Funds for the Central Universities","doi-asserted-by":"publisher","award":["3132019175"],"award-info":[{"award-number":["3132019175"]}],"id":[{"id":"10.13039\/501100012226","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Key Research and Development Program of Shaanxi Province, China","award":["2017GY-197"],"award-info":[{"award-number":["2017GY-197"]}]},{"name":"Monash Major Inter-Disciplinary Research"},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01 AI111965"],"award-info":[{"award-number":["R01 AI111965"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000923","name":"Australian Research Council","doi-asserted-by":"publisher","award":["DP120104460"],"award-info":[{"award-number":["DP120104460"]}],"id":[{"id":"10.13039\/501100000923","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000923","name":"Australian Research Council","doi-asserted-by":"publisher","award":["LP110200333"],"award-info":[{"award-number":["LP110200333"]}],"id":[{"id":"10.13039\/501100000923","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","award":["1127948"],"award-info":[{"award-number":["1127948"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","award":["1144652"],"award-info":[{"award-number":["1144652"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2020,5,21]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Post-translational modifications (PTMs) play very important roles in various cell signaling pathways and biological process. Due to PTMs\u2019 extremely important roles, many major PTMs have been studied, while the functional and mechanical characterization of major PTMs is well documented in several databases. However, most currently available databases mainly focus on protein sequences, while the real 3D structures of PTMs have been largely ignored. Therefore, studies of PTMs 3D structural signatures have been severely limited by the deficiency of the data. Here, we develop PRISMOID, a novel publicly available and free 3D structure database for a wide range of PTMs. PRISMOID represents an up-to-date and interactive online knowledge base with specific focus on 3D structural contexts of PTMs sites and mutations that occur on PTMs and in the close proximity of PTM sites with functional impact. The first version of PRISMOID encompasses 17\u00a0145 non-redundant modification sites on 3919 related protein 3D structure entries pertaining to 37 different types of PTMs. Our entry web page is organized in a comprehensive manner, including detailed PTM annotation on the 3D structure and biological information in terms of mutations affecting PTMs, secondary structure features and per-residue solvent accessibility features of PTM sites, domain context, predicted natively disordered regions and sequence alignments. In addition, high-definition JavaScript packages are employed to enhance information visualization in PRISMOID. PRISMOID equips a variety of interactive and customizable search options and data browsing functions; these capabilities allow users to access data via keyword, ID and advanced options combination search in an efficient and user-friendly way. A download page is also provided to enable users to download the SQL file, computational structural features and PTM sites\u2019 data. We anticipate PRISMOID will swiftly become an invaluable online resource, assisting both biologists and bioinformaticians to conduct experiments and develop applications supporting discovery efforts in the sequence\u2013structural\u2013functional relationship of PTMs and providing important insight into mutations and PTM sites interaction mechanisms. The PRISMOID database is freely accessible at http:\/\/prismoid.erc.monash.edu\/. The database and web interface are implemented in MySQL, JSP, JavaScript and HTML with all major browsers supported.<\/jats:p>","DOI":"10.1093\/bib\/bbz050","type":"journal-article","created":{"date-parts":[[2019,4,2]],"date-time":"2019-04-02T15:20:19Z","timestamp":1554218419000},"page":"1069-1079","source":"Crossref","is-referenced-by-count":35,"title":["PRISMOID: a comprehensive 3D structure database for post-translational modifications and mutations with functional impact"],"prefix":"10.1093","volume":"21","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5216-3213","authenticated-orcid":false,"given":"Fuyi","family":"Li","sequence":"first","affiliation":[{"name":"Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria, Australia"},{"name":"Monash Centre for Data Science, Faculty of Information Technology, Monash University, Melbourne, VIC, Australia"}]},{"given":"Cunshuo","family":"Fan","sequence":"first","affiliation":[{"name":"College of Information Engineering, Northwest A&F University, Yangling, China"}]},{"given":"Tatiana T","family":"Marquez-Lago","sequence":"first","affiliation":[{"name":"Department of Genetics and Department of Cell, Developmental and Integrative Biology, School of Medicine, University of Alabama at Birmingham, AL, USA"}]},{"given":"Andr\u00e9","family":"Leier","sequence":"first","affiliation":[{"name":"Department of Genetics and Department of Cell, Developmental and Integrative Biology, School of Medicine, University of Alabama at Birmingham, AL, USA"}]},{"given":"Jerico","family":"Revote","sequence":"first","affiliation":[{"name":"Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria, Australia"}]},{"given":"Cangzhi","family":"Jia","sequence":"first","affiliation":[{"name":"College of Science, Dalian Maritime University, Dalian, China"},{"name":"School of Computer Science and Engineering, Nanyang Technological University, Singapore, Singapore"}]},{"given":"Yan","family":"Zhu","sequence":"first","affiliation":[{"name":"Biomedicine Discovery Institute and Department of Microbiology, Monash University, Melbourne, Victoria, Australia"}]},{"given":"A Ian","family":"Smith","sequence":"first","affiliation":[{"name":"Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria, Australia"}]},{"given":"Geoffrey I","family":"Webb","sequence":"first","affiliation":[{"name":"Monash Centre for Data Science, Faculty of Information Technology, Monash University, Melbourne, VIC, Australia"}]},{"given":"Quanzhong","family":"Liu","sequence":"first","affiliation":[{"name":"College of Information Engineering, Northwest A&F University, Yangling, China"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1444-190X","authenticated-orcid":false,"given":"Leyi","family":"Wei","sequence":"first","affiliation":[{"name":"School of Computer Science and Technology, College of Intelligence and Computing, Tianjin University, Tianjin, China"}]},{"given":"Jian","family":"Li","sequence":"first","affiliation":[{"name":"Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria, Australia"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8031-9086","authenticated-orcid":false,"given":"Jiangning","family":"Song","sequence":"first","affiliation":[{"name":"Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria, Australia"},{"name":"Monash Centre for Data Science, Faculty of Information Technology, Monash University, Melbourne, VIC, Australia"}]}],"member":"286","published-online":{"date-parts":[[2019,6,4]]},"reference":[{"key":"2020061712232807400_ref1","doi-asserted-by":"crossref","first-page":"1413","DOI":"10.1038\/ng.259","article-title":"Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing","volume":"40","author":"Pan","year":"2008","journal-title":"Nat Genet"},{"key":"2020061712232807400_ref2","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1007\/s00018-014-1661-9","article-title":"Exceptionally abundant exceptions: comprehensive characterization of intrinsic disorder in all domains of life","volume":"72","author":"Peng","year":"2015","journal-title":"Cell Mol Life Sci"},{"key":"2020061712232807400_ref3","doi-asserted-by":"crossref","first-page":"3069","DOI":"10.1007\/s00018-017-2555-4","article-title":"Comprehensive review of methods for prediction of intrinsic disorder and its molecular functions","volume":"74","author":"Meng","year":"2017","journal-title":"Cell Mol Life Sci"},{"key":"2020061712232807400_ref4","first-page":"bty522","article-title":"Quokka: a comprehensive tool for rapid and accurate prediction of kinase family-specific phosphorylation sites in the human proteome","volume":"2018","author":"Li","journal-title":"Bioinformatics"},{"key":"2020061712232807400_ref5","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1038\/nmeth.2519","article-title":"Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation","volume":"10","author":"Swaney","year":"2013","journal-title":"Nat Methods"},{"key":"2020061712232807400_ref6","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1038\/sj.leu.2401657","article-title":"Serine\/threonine phosphorylation in cytokine signal transduction","volume":"14","author":"McCubrey","year":"2000","journal-title":"Leukemia"},{"key":"2020061712232807400_ref7","doi-asserted-by":"crossref","first-page":"1807","DOI":"10.1016\/j.str.2011.09.021","article-title":"Phosphorylation in protein-protein binding: effect on stability and function","volume":"19","author":"Nishi","year":"2011","journal-title":"Structure"},{"key":"2020061712232807400_ref8","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1004049","article-title":"The roles of post-translational modifications in the context of protein interaction networks","volume":"11","author":"Duan","year":"2015","journal-title":"PLoS Comput Biol"},{"key":"2020061712232807400_ref9","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0074299","article-title":"The role of N-glycosylation in folding, trafficking, and functionality of lysosomal protein CLN5","volume":"8","author":"Moharir","year":"2013","journal-title":"Plos One"},{"key":"2020061712232807400_ref10","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1038\/nchembio.437","article-title":"A systematic approach to protein glycosylation analysis: a path through the maze","volume":"6","author":"Marino","year":"2010","journal-title":"Nat Chem Biol"},{"key":"2020061712232807400_ref11","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1186\/s12859-019-2700-1","article-title":"Positive-unlabelled learning of glycosylation sites in the human proteome","volume":"20","author":"Li","year":"2019","journal-title":"BMC Bioinformatics"},{"key":"2020061712232807400_ref12","first-page":"43","article-title":"Biological importance of glycosylation","volume":"96","author":"Dwek","year":"1998","journal-title":"Characterization Of Biotechnology Pharmaceutical Products"},{"key":"2020061712232807400_ref13","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1093\/bib\/5.2.164","article-title":"Bioinformatics for glycomics: status, methods, requirements and perspectives","volume":"5","author":"von der Lieth","year":"2004","journal-title":"Brief Bioinform"},{"key":"2020061712232807400_ref14","doi-asserted-by":"crossref","first-page":"reviews0006","DOI":"10.1186\/gb-2002-3-5-reviews0006","article-title":"The diversity of acetylated proteins","volume":"3","author":"Polevoda","year":"2002","journal-title":"Genome Biol"},{"key":"2020061712232807400_ref15","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.gene.2005.09.010","article-title":"Acetylation and deacetylation of non-histone proteins","volume":"363","author":"Glozak","year":"2005","journal-title":"Gene"},{"key":"2020061712232807400_ref16","doi-asserted-by":"crossref","first-page":"1000","DOI":"10.1126\/science.1179689","article-title":"Regulation of cellular metabolism by protein lysine acetylation","volume":"327","author":"Zhao","year":"2010","journal-title":"Science"},{"key":"2020061712232807400_ref17","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1016\/S1097-2765(01)00347-1","article-title":"Ubiquitin enters the new millennium","volume":"8","author":"Pickart","year":"2001","journal-title":"Mol Cell"},{"key":"2020061712232807400_ref18","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0126270","article-title":"Mutation of androgen receptor N-terminal phosphorylation site Tyr-267 leads to inhibition of nuclear translocation and DNA binding","volume":"10","author":"Karaca","year":"2015","journal-title":"PLoS One"},{"key":"2020061712232807400_ref19","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1038\/nrc.2015.18","article-title":"The kinome \u2018at large\u2019 in cancer","volume":"16","author":"Fleuren","year":"2016","journal-title":"Nat Rev Cancer"},{"key":"2020061712232807400_ref20","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1038\/nrc3982","article-title":"Glycosylation in cancer: mechanisms and clinical implications","volume":"15","author":"Pinho","year":"2015","journal-title":"Nat Rev Cancer"},{"key":"2020061712232807400_ref21","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/S0076-6879(05)02007-0","article-title":"Peptide sequence analysis","volume":"402","author":"Medzihradszky","year":"2005","journal-title":"Methods Enzymol"},{"key":"2020061712232807400_ref22","doi-asserted-by":"crossref","first-page":"D512","DOI":"10.1093\/nar\/gku1267","article-title":"PhosphoSitePlus, 2014: mutations, PTMs and recalibrations","volume":"43","author":"Hornbeck","year":"2015","journal-title":"Nucleic Acids Res"},{"key":"2020061712232807400_ref23","doi-asserted-by":"crossref","first-page":"D261","DOI":"10.1093\/nar\/gkr1122","article-title":"PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse","volume":"40","author":"Hornbeck","year":"2012","journal-title":"Nucleic Acids Res"},{"key":"2020061712232807400_ref24","doi-asserted-by":"crossref","first-page":"D435","DOI":"10.1093\/nar\/gkv1240","article-title":"dbPTM 2016: 10-year anniversary of a resource for post-translational modification of proteins","volume":"44","author":"Huang","year":"2016","journal-title":"Nucleic Acids Res"},{"key":"2020061712232807400_ref25","doi-asserted-by":"crossref","first-page":"D622","DOI":"10.1093\/nar\/gkj083","article-title":"dbPTM: an information repository of protein post-translational modification","volume":"34","author":"Lee","year":"2006","journal-title":"Nucleic Acids Res"},{"key":"2020061712232807400_ref26","doi-asserted-by":"crossref","first-page":"bau025","DOI":"10.1093\/database\/bau025","article-title":"SysPTM 2.0: an updated systematic resource for post-translational modification","volume":"2014","author":"Li","year":"2014","journal-title":"Database (Oxford)"},{"key":"2020061712232807400_ref27","doi-asserted-by":"crossref","first-page":"1839","DOI":"10.1074\/mcp.M900030-MCP200","article-title":"SysPTM: a systematic resource for proteomic research on post-translational modifications","volume":"8","author":"Li","year":"2009","journal-title":"Mol Cell Proteomics"},{"key":"2020061712232807400_ref28","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/j.jgg.2017.03.007","article-title":"PLMD: an updated data resource of protein lysine modifications","volume":"44","author":"Xu","year":"2017","journal-title":"J Genet Genomics"},{"key":"2020061712232807400_ref29","doi-asserted-by":"crossref","first-page":"D261","DOI":"10.1093\/nar\/gkq1104","article-title":"Phospho.ELM: a database of phosphorylation sites--update 2011","volume":"39","author":"Dinkel","year":"2011","journal-title":"Nucleic Acids Res"},{"key":"2020061712232807400_ref30","doi-asserted-by":"crossref","first-page":"2699","DOI":"10.1093\/nar\/gky092","article-title":"UniProt: the universal protein knowledgebase","volume":"46","author":"UniProt Consortium","year":"2018","journal-title":"Nucleic Acids Res"},{"key":"2020061712232807400_ref31","doi-asserted-by":"crossref","DOI":"10.1093\/database\/bau041","article-title":"PTM-SD: a database of structurally resolved and annotated posttranslational modifications in proteins","volume":"2014","author":"Craveur","year":"2014","journal-title":"Database (Oxford)"},{"key":"2020061712232807400_ref32","doi-asserted-by":"crossref","first-page":"2047","DOI":"10.1093\/bioinformatics\/btx101","article-title":"BioJava-ModFinder: identification of protein modifications in 3D structures from the Protein Data Bank","volume":"33","author":"Gao","year":"2017","journal-title":"Bioinformatics"},{"key":"2020061712232807400_ref33","article-title":"AAM: Yeast Amino Acid Modifications Database, Database (Oxford)","author":"Ledesma","year":"2018"},{"key":"2020061712232807400_ref34","doi-asserted-by":"crossref","first-page":"1411","DOI":"10.1093\/bioinformatics\/btu852","article-title":"GlycoMine: a machine learning-based approach for predicting N-, C- and O-linked glycosylation in the human proteome","volume":"31","author":"Li","year":"2015","journal-title":"Bioinformatics"},{"key":"2020061712232807400_ref35","doi-asserted-by":"crossref","first-page":"2029","DOI":"10.1093\/bioinformatics\/bty039","article-title":"O-GlcNAcPRED-II: an integrated classification algorithm for identifying O-GlcNAcylation sites based on fuzzy undersampling and a K-means PCA oversampling technique","volume":"34","author":"Jia","year":"2018","journal-title":"Bioinformatics"},{"key":"2020061712232807400_ref36","doi-asserted-by":"crossref","first-page":"1598","DOI":"10.1074\/mcp.M700574-MCP200","article-title":"GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy","volume":"7","author":"Xue","year":"2008","journal-title":"Mol Cell Proteomics"},{"key":"2020061712232807400_ref37","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1093\/bib\/bbu031","article-title":"Towards more accurate prediction of ubiquitination sites: a comprehensive review of current methods, tools and features","volume":"16","author":"Chen","year":"2015","journal-title":"Brief Bioinform"},{"key":"2020061712232807400_ref38","doi-asserted-by":"crossref","first-page":"1757","DOI":"10.1002\/jcc.25353","article-title":"Predicting lysine-malonylation sites of proteins using sequence and predicted structural features","volume":"39","author":"Taherzadeh","year":"2018","journal-title":"J Comput Chem"},{"key":"2020061712232807400_ref39","article-title":"GlycoMine(struct): a new bioinformatics tool for highly accurate mapping of the human N-linked and O-linked glycoproteomes by incorporating structural features","volume":"6","author":"Li","year":"2016","journal-title":"Sci Rep"},{"key":"2020061712232807400_ref40","doi-asserted-by":"crossref","first-page":"2249","DOI":"10.1093\/bioinformatics\/bts426","article-title":"Computational prediction of N-linked glycosylation incorporating structural properties and patterns","volume":"28","author":"Chuang","year":"2012","journal-title":"Bioinformatics"},{"key":"2020061712232807400_ref41","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1186\/1471-2105-10-117","article-title":"Detection and characterization of 3D-signature phosphorylation site motifs and their contribution towards improved phosphorylation site prediction in proteins","volume":"10","author":"Durek","year":"2009","journal-title":"BMC Bioinformatics"},{"key":"2020061712232807400_ref42","doi-asserted-by":"crossref","first-page":"D901","DOI":"10.1093\/nar\/gkx973","article-title":"ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins","volume":"46","author":"Krassowski","year":"2018","journal-title":"Nucleic Acids Res"},{"key":"2020061712232807400_ref43","doi-asserted-by":"crossref","first-page":"D411","DOI":"10.1093\/nar\/gkq1105","article-title":"A series of PDB related databases for everyday needs","volume":"39","author":"Joosten","year":"2011","journal-title":"Nucleic Acids Res"},{"key":"2020061712232807400_ref44","volume-title":"University College of London","author":"Hubbard","year":"1992"},{"key":"2020061712232807400_ref45","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1093\/nar\/28.1.235","article-title":"The Protein Data Bank","volume":"28","author":"Berman","year":"2000","journal-title":"Nucleic Acids Res"},{"key":"2020061712232807400_ref46","doi-asserted-by":"crossref","first-page":"3389","DOI":"10.1093\/nar\/25.17.3389","article-title":"Gapped BLAST and PSI-BLAST: a new generation of protein database search programs","volume":"25","author":"Altschul","year":"1997","journal-title":"Nucleic Acids Res"},{"key":"2020061712232807400_ref47","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1002\/humu.20021","article-title":"The Swiss-Prot variant page and the ModSNP database: a resource for sequence and structure information on human protein variants","volume":"23","author":"Yip","year":"2004","journal-title":"Hum Mutat"},{"issue":"Suppl","key":"2020061712232807400_ref48","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1038\/ng1090","article-title":"Discovering genotypes underlying human phenotypes: past successes for mendelian disease, future approaches for complex disease","volume":"33","author":"Botstein","year":"2003","journal-title":"Nat Genet"},{"issue":"Suppl 2","key":"2020061712232807400_ref49","doi-asserted-by":"crossref","first-page":"S7","DOI":"10.1186\/1755-8794-8-S2-S7","article-title":"Detection and analysis of disease-associated single nucleotide polymorphism influencing post-translational modification","volume":"8","author":"Kim","year":"2015","journal-title":"BMC Med Genomics"},{"key":"2020061712232807400_ref50","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1038\/nmeth.3396","article-title":"MIMP: predicting the impact of mutations on kinase-substrate phosphorylation","volume":"12","author":"Wagih","year":"2015","journal-title":"Nat Methods"},{"key":"2020061712232807400_ref51","doi-asserted-by":"crossref","first-page":"1473","DOI":"10.1093\/bioinformatics\/btx822","article-title":"Computational identification of binding energy hot spots in protein-RNA complexes using an ensemble approach","volume":"34","author":"Pan","year":"2018","journal-title":"Bioinformatics"},{"key":"2020061712232807400_ref52","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.jtbi.2018.01.023","article-title":"PREvaIL, an integrative approach for inferring catalytic residues using sequence, structural, and network features in a machine-learning framework","volume":"443","author":"Song","year":"2018","journal-title":"J Theor Biol"},{"key":"2020061712232807400_ref53","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.visinf.2018.04.011","article-title":"ECharts: a declarative framework for rapid construction of web-based visualization","volume":"2","author":"Li","year":"2018","journal-title":"Vis Inform"},{"key":"2020061712232807400_ref54","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.1093\/bioinformatics\/btu829","article-title":"3Dmol.js: molecular visualization with WebGL","volume":"31","author":"Rego","year":"2015","journal-title":"Bioinformatics"},{"key":"2020061712232807400_ref55","doi-asserted-by":"crossref","first-page":"D508","DOI":"10.1093\/nar\/gks1226","article-title":"D(2)P(2): database of disordered protein predictions","volume":"41","author":"Oates","year":"2013","journal-title":"Nucleic Acids Res"},{"key":"2020061712232807400_ref56","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1093\/bioinformatics\/btt614","article-title":"Sequence alignment visualization in HTML5 without Java","volume":"30","author":"Gille","year":"2014","journal-title":"Bioinformatics"},{"key":"2020061712232807400_ref57","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1042\/BJ20050341","article-title":"Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications","volume":"390","author":"Christensen","year":"2005","journal-title":"Biochem J"},{"key":"2020061712232807400_ref58","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1016\/S0955-0674(03)00003-6","article-title":"Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation","volume":"15","author":"Brooks","year":"2003","journal-title":"Curr Opin Cell Biol"},{"key":"2020061712232807400_ref59","doi-asserted-by":"crossref","first-page":"158","DOI":"10.3389\/fgene.2018.00158","article-title":"Intrinsic disorder and posttranslational modifications: the darker side of the biological dark matter","volume":"9","author":"Darling","year":"2018","journal-title":"Front Genet"}],"container-title":["Briefings in Bioinformatics"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/bib\/article-pdf\/21\/3\/1069\/33398999\/bbz050.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/academic.oup.com\/bib\/article-pdf\/21\/3\/1069\/33398999\/bbz050.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,6,17]],"date-time":"2020-06-17T13:48:13Z","timestamp":1592401693000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/bib\/article\/21\/3\/1069\/5510293"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,6,4]]},"references-count":59,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2019,6,4]]},"published-print":{"date-parts":[[2020,5,21]]}},"URL":"https:\/\/doi.org\/10.1093\/bib\/bbz050","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/523308","asserted-by":"object"}]},"ISSN":["1467-5463","1477-4054"],"issn-type":[{"value":"1467-5463","type":"print"},{"value":"1477-4054","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2020,5]]},"published":{"date-parts":[[2019,6,4]]}}}