PhosIDP : a web tool to visualize the location of phosphorylation sites in disordered regions
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 as...
| Main Authors: | , , , , |
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| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
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2021
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| Online Access: | https://hdl.handle.net/10356/151998 |
| _version_ | 1811693888065241088 |
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| author | Nicolaou, Sonia T. Hebditch, Max Jonathan, Owen J. Verma, Chandra Shekhar Warwicker, Jim |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Nicolaou, Sonia T. Hebditch, Max Jonathan, Owen J. Verma, Chandra Shekhar Warwicker, Jim |
| author_sort | Nicolaou, Sonia T. |
| collection | NTU |
| description | 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. |
| first_indexed | 2024-10-01T06:58:50Z |
| format | Journal Article |
| id | ntu-10356/151998 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T06:58:50Z |
| publishDate | 2021 |
| record_format | dspace |
| spelling | ntu-10356/1519982023-02-28T17:08:10Z PhosIDP : a web tool to visualize the location of phosphorylation sites in disordered regions Nicolaou, Sonia T. Hebditch, Max Jonathan, Owen J. Verma, Chandra Shekhar Warwicker, Jim School of Biological Sciences Bioinformatics Institute, A*STAR Science::Biological sciences Computational Biophysics Intrinsically Disordered Proteins 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. Agency for Science, Technology and Research (A*STAR) Published version The authors would like to acknowledge that this work has been supported by the University of Manchester and the Agency for Science, Technology, and Research (A*STAR) Singapore, and by the UK EPSRC (grant EP/N024796/1). CSV thanks A*STAR for grants (grant IDs H17/01/a0/010, IAF111213C, H18/01/a0/015). 2021-11-17T03:11:54Z 2021-11-17T03:11:54Z 2021 Journal Article Nicolaou, S. T., Hebditch, M., Jonathan, O. J., Verma, C. S. & Warwicker, J. (2021). PhosIDP : a web tool to visualize the location of phosphorylation sites in disordered regions. Scientific Reports, 11(1), 9930-. https://dx.doi.org/10.1038/s41598-021-88992-0 2045-2322 https://hdl.handle.net/10356/151998 10.1038/s41598-021-88992-0 33976270 2-s2.0-85105767371 1 11 9930 en H17/01/a0/010 IAF111213C H18/01/a0/015 Scientific Reports © 2021 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. application/pdf |
| spellingShingle | Science::Biological sciences Computational Biophysics Intrinsically Disordered Proteins Nicolaou, Sonia T. Hebditch, Max Jonathan, Owen J. Verma, Chandra Shekhar Warwicker, Jim PhosIDP : a web tool to visualize the location of phosphorylation sites in disordered regions |
| title | PhosIDP : a web tool to visualize the location of phosphorylation sites in disordered regions |
| title_full | PhosIDP : a web tool to visualize the location of phosphorylation sites in disordered regions |
| title_fullStr | PhosIDP : a web tool to visualize the location of phosphorylation sites in disordered regions |
| title_full_unstemmed | PhosIDP : a web tool to visualize the location of phosphorylation sites in disordered regions |
| title_short | PhosIDP : a web tool to visualize the location of phosphorylation sites in disordered regions |
| title_sort | phosidp a web tool to visualize the location of phosphorylation sites in disordered regions |
| topic | Science::Biological sciences Computational Biophysics Intrinsically Disordered Proteins |
| url | https://hdl.handle.net/10356/151998 |
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