PhosIDP: a web tool to visualize the location of phosphorylation sites in disordered regions
AuthorsNicolaou, Sonia T.
Jonathan, Owen J.
Verma, Chandra S.
Warwicker, Jim; email: firstname.lastname@example.org
MetadataShow full item record
AbstractAbstract: Charge 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.
CitationScientific Reports, volume 11, issue 1, page 9930
PublisherNature Publishing Group UK
DescriptionFrom Springer Nature via Jisc Publications Router
History: received 2021-03-15, accepted 2021-04-19, registration 2021-04-20, online 2021-05-11, pub-electronic 2021-05-11, collection 2021-12
Publication status: Published
Funder: Agency for Science, Technology and Research; doi: http://dx.doi.org/10.13039/501100001348; Grant(s): IDs H17/01/a0/010, IDs H17/01/a0/010
Funder: Engineering and Physical Sciences Research Council; doi: http://dx.doi.org/10.13039/501100000266; Grant(s): EP/N024796/1, EP/N024796/1