{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1361699994352071296.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1002/msb.201304521"}},{"identifier":{"@type":"URI","@value":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fmsb.201304521"}},{"identifier":{"@type":"URI","@value":"https://onlinelibrary.wiley.com/doi/pdf/10.1002/msb.201304521"}},{"identifier":{"@type":"URI","@value":"https://onlinelibrary.wiley.com/doi/full-xml/10.1002/msb.201304521"}},{"identifier":{"@type":"URI","@value":"https://www.embopress.org/doi/pdf/10.1002/msb.201304521"}}],"dc:title":[{"@value":"Evolution and functional cross‐talk of protein post‐translational modifications"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:title>Abstract</jats:title>\n                  <jats:p>\n                    Protein post‐translational modifications (\n                    <jats:styled-content style=\"fixed-case\">PTM</jats:styled-content>\n                    s) allow the cell to regulate protein activity and play a crucial role in the response to changes in external conditions or internal states. Advances in mass spectrometry now enable proteome wide characterization of\n                    <jats:styled-content style=\"fixed-case\">PTM</jats:styled-content>\n                    s and have revealed a broad functional role for a range of different types of modifications. Here we review advances in the study of the evolution and function of\n                    <jats:styled-content style=\"fixed-case\">PTM</jats:styled-content>\n                    s that were spurred by these technological improvements. We provide an overview of studies focusing on the origin and evolution of regulatory enzymes as well as the evolutionary dynamics of modification sites. Finally, we discuss different mechanisms of altering protein activity via post‐translational regulation and progress made in the large‐scale functional characterization of\n                    <jats:styled-content style=\"fixed-case\">PTM</jats:styled-content>\n                    function.\n                  </jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1381699994352071296","@type":"Researcher","foaf:name":[{"@value":"Pedro Beltrao"}],"jpcoar:affiliationName":[{"@value":"European Molecular Biology Laboratory European Bioinformatics Institute (EMBL‐EBI)  Cambridge UK"}]},{"@id":"https://cir.nii.ac.jp/crid/1381699994352071424","@type":"Researcher","foaf:name":[{"@value":"Peer Bork"}],"jpcoar:affiliationName":[{"@value":"Structural and Computational Biology Unit European Molecular Biology Laboratory  Heidelberg Germany"},{"@value":"Max‐Delbruck‐Centre for Molecular Medicine  Berlin‐Buch Germany"}]},{"@id":"https://cir.nii.ac.jp/crid/1381699994352071425","@type":"Researcher","foaf:name":[{"@value":"Nevan J. Krogan"}],"jpcoar:affiliationName":[{"@value":"Department of Cellular and Molecular Pharmacology University of California  San Francisco California USA"},{"@value":"California Institute for Quantitative Biosciences  San Francisco California USA"},{"@value":"J. David Gladstone Institutes  San Francisco California USA"}]},{"@id":"https://cir.nii.ac.jp/crid/1380016868406167424","@type":"Researcher","foaf:name":[{"@value":"Vera van Noort"}],"jpcoar:affiliationName":[{"@value":"Structural and Computational Biology Unit European Molecular Biology Laboratory  Heidelberg Germany"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"17444292"},{"@type":"EISSN","@value":"17444292"}],"prism:publicationName":[{"@value":"Molecular Systems Biology"}],"dc:publisher":[{"@value":"Springer Science and Business Media LLC"}],"prism:publicationDate":"2013-01","prism:volume":"9","prism:number":"1","prism:startingPage":"714"},"reviewed":"false","dc:rights":["http://creativecommons.org/licenses/by-nc-sa/3.0/"],"url":[{"@id":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fmsb.201304521"},{"@id":"https://onlinelibrary.wiley.com/doi/pdf/10.1002/msb.201304521"},{"@id":"https://onlinelibrary.wiley.com/doi/full-xml/10.1002/msb.201304521"},{"@id":"https://www.embopress.org/doi/pdf/10.1002/msb.201304521"}],"createdAt":"2013-12-19","modifiedAt":"2025-12-06","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360002220648327424","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Physicochemical mechanisms of protein regulation by phosphorylation"}]},{"@id":"https://cir.nii.ac.jp/crid/1360283691661084288","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Large-Scale Identification of Phosphorylation Sites for Profiling Protein Kinase Selectivity"}]},{"@id":"https://cir.nii.ac.jp/crid/1360585255518467840","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Accurate models of substrate preferences of post-translational modification enzymes from a combination of mRNA display and deep learning"}]},{"@id":"https://cir.nii.ac.jp/crid/1360848658067182976","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Identifications of Putative PKA Substrates with Quantitative Phosphoproteomics and Primary-Sequence-Based Scoring"}]},{"@id":"https://cir.nii.ac.jp/crid/1361975846298450304","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Role of SIRT1 in Modulating Acetylation of the Sarco-Endoplasmic Reticulum Ca\n            <sup>2+</sup>\n            -ATPase in Heart Failure"}]},{"@id":"https://cir.nii.ac.jp/crid/1390564238105600384","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Selected Reaction Monitoring of Kinase Activity-Targeted Phosphopeptides"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1002/msb.201304521"},{"@type":"CROSSREF","@value":"10.3389/fgene.2014.00270_references_DOI_LWk3VwvKBywd9zjOZXdUdL7ABSV"},{"@type":"CROSSREF","@value":"10.1021/acs.jproteome.7b00087_references_DOI_LWk3VwvKBywd9zjOZXdUdL7ABSV"},{"@type":"CROSSREF","@value":"10.1021/acscentsci.2c00223_references_DOI_LWk3VwvKBywd9zjOZXdUdL7ABSV"},{"@type":"CROSSREF","@value":"10.15583/jpchrom.2019.005_references_DOI_LWk3VwvKBywd9zjOZXdUdL7ABSV"},{"@type":"CROSSREF","@value":"10.1021/pr500319y_references_DOI_LWk3VwvKBywd9zjOZXdUdL7ABSV"},{"@type":"CROSSREF","@value":"10.1161/circresaha.118.313865_references_DOI_LWk3VwvKBywd9zjOZXdUdL7ABSV"}]}