Structural analysis of mammalian protein phosphorylation at a proteome level
Published by Elsevier Ltd..
Phosphorylation is an essential post-translational modification for almost all cellular processes. Several global phosphoproteomics analyses have revealed phosphorylation profiles under different conditions. Beyond identification of phospho-sites, protein structures add another layer of information about their functionality. In this study, we systematically characterize phospho-sites based on their 3D locations in the protein and establish a location map for phospho-sites. More than 250,000 phospho-sites have been analyzed, of which 8,686 sites match at least one structure and are stratified based on their respective 3D positions. Core phospho-sites possess two distinct groups based on their dynamicity. Dynamic core phosphorylations are significantly more functional compared with static ones. The dynamic core and the interface phospho-sites are the most functional among all 3D phosphorylation groups. Our analysis provides global characterization and stratification of phospho-sites from a structural perspective that can be utilized for predicting functional relevance and filtering out false positives in phosphoproteomic studies.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2021 |
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| Erschienen: |
2021 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:29 |
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| Enthalten in: |
Structure (London, England : 1993) - 29(2021), 11 vom: 04. Nov., Seite 1219-1229.e3 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Kamacioglu, Altug [VerfasserIn] |
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| Links: |
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| Themen: |
Cell cycle |
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| Anmerkungen: |
Date Completed 16.03.2022 Date Revised 16.03.2022 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.str.2021.06.008 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 520 | |a Published by Elsevier Ltd. | ||
| 520 | |a Phosphorylation is an essential post-translational modification for almost all cellular processes. Several global phosphoproteomics analyses have revealed phosphorylation profiles under different conditions. Beyond identification of phospho-sites, protein structures add another layer of information about their functionality. In this study, we systematically characterize phospho-sites based on their 3D locations in the protein and establish a location map for phospho-sites. More than 250,000 phospho-sites have been analyzed, of which 8,686 sites match at least one structure and are stratified based on their respective 3D positions. Core phospho-sites possess two distinct groups based on their dynamicity. Dynamic core phosphorylations are significantly more functional compared with static ones. The dynamic core and the interface phospho-sites are the most functional among all 3D phosphorylation groups. Our analysis provides global characterization and stratification of phospho-sites from a structural perspective that can be utilized for predicting functional relevance and filtering out false positives in phosphoproteomic studies | ||
| 650 | 4 | |a Journal Article | |
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| 650 | 4 | |a dynamic phospho-site | |
| 650 | 4 | |a phospho-site structural stratification | |
| 650 | 4 | |a phosphoproteomics | |
| 650 | 4 | |a static phospho-site | |
| 650 | 7 | |a Phosphoproteins |2 NLM | |
| 650 | 7 | |a Proteome |2 NLM | |
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| 700 | 1 | |a Ozlu, Nurhan |e verfasserin |4 aut | |
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