Please use this identifier to cite or link to this item: https://doi.org/10.1038/s41598-021-88992-0
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dc.titlePhosIDP: a web tool to visualize the location of phosphorylation sites in disordered regions
dc.contributor.authorNicolaou, Sonia T.
dc.contributor.authorHebditch, Max
dc.contributor.authorJonathan, Owen J.
dc.contributor.authorVerma, Chandra S.
dc.contributor.authorWarwicker, Jim
dc.date.accessioned2022-10-13T06:45:55Z
dc.date.available2022-10-13T06:45:55Z
dc.date.issued2021-05-11
dc.identifier.citationNicolaou, Sonia T., Hebditch, Max, Jonathan, Owen J., Verma, Chandra S., Warwicker, Jim (2021-05-11). PhosIDP: a web tool to visualize the location of phosphorylation sites in disordered regions. Scientific Reports 11 (1) : 9930. ScholarBank@NUS Repository. https://doi.org/10.1038/s41598-021-88992-0
dc.identifier.issn2045-2322
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/233060
dc.description.abstractCharge is a key determinant of intrinsically disordered protein (IDP) and intrinsically disordered region (IDR) properties. IDPs and IDRs are enriched in sites of phosphorylation, which alters charge. Visualizing the degree to which phosphorylation modulates the charge profile of a sequence would assist in the functional interpretation of IDPs and IDRs. PhosIDP is a web tool that shows variation of charge and fold propensity upon phosphorylation. In combination with the displayed location of protein domains, the information provided by the web tool can lead to functional inferences for the consequences of phosphorylation. IDRs are components of many proteins that form biological condensates. It is shown that IDR charge, and its modulation by phosphorylation, is more tightly controlled for proteins that are essential for condensate formation than for those present in condensates but inessential. © 2021, The Author(s).
dc.publisherNature Research
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourceScopus OA2021
dc.typeArticle
dc.contributor.departmentDEPT OF BIOLOGICAL SCIENCES
dc.description.doi10.1038/s41598-021-88992-0
dc.description.sourcetitleScientific Reports
dc.description.volume11
dc.description.issue1
dc.description.page9930
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