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The PhosphoGRID Saccharomyces cerevisiae protein phosphorylation site database: version 2.0 update
PhosphoGRID is an online database that curates and houses experimentally verified in vivo phosphorylation sites in the Saccharomyces cerevisiae proteome (www.phosphogrid.org). Phosphosites are annotated with specific protein kinases and/or phosphatases, along with the condition(s) under which the ph...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3653121/ https://www.ncbi.nlm.nih.gov/pubmed/23674503 http://dx.doi.org/10.1093/database/bat026 |
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author | Sadowski, Ivan Breitkreutz, Bobby-Joe Stark, Chris Su, Ting-Cheng Dahabieh, Matthew Raithatha, Sheetal Bernhard, Wendy Oughtred, Rose Dolinski, Kara Barreto, Kris Tyers, Mike |
author_facet | Sadowski, Ivan Breitkreutz, Bobby-Joe Stark, Chris Su, Ting-Cheng Dahabieh, Matthew Raithatha, Sheetal Bernhard, Wendy Oughtred, Rose Dolinski, Kara Barreto, Kris Tyers, Mike |
author_sort | Sadowski, Ivan |
collection | PubMed |
description | PhosphoGRID is an online database that curates and houses experimentally verified in vivo phosphorylation sites in the Saccharomyces cerevisiae proteome (www.phosphogrid.org). Phosphosites are annotated with specific protein kinases and/or phosphatases, along with the condition(s) under which the phosphorylation occurs and/or the effects on protein function. We report here an updated data set, including nine additional high-throughput (HTP) mass spectrometry studies. The version 2.0 data set contains information on 20 177 unique phosphorylated residues, representing a 4-fold increase from version 1.0, and includes 1614 unique phosphosites derived from focused low-throughput (LTP) studies. The overlap between HTP and LTP studies represents only ∼3% of the total unique sites, but importantly 45% of sites from LTP studies with defined function were discovered in at least two independent HTP studies. The majority of new phosphosites in this update occur on previously documented proteins, suggesting that coverage of phosphoproteins in the yeast proteome is approaching saturation. We will continue to update the PhosphoGRID data set, with the expectation that the integration of information from LTP and HTP studies will enable the development of predictive models of phosphorylation-based signaling networks. Database URL: http://www.phosphogrid.org/ |
format | Online Article Text |
id | pubmed-3653121 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-36531212013-05-14 The PhosphoGRID Saccharomyces cerevisiae protein phosphorylation site database: version 2.0 update Sadowski, Ivan Breitkreutz, Bobby-Joe Stark, Chris Su, Ting-Cheng Dahabieh, Matthew Raithatha, Sheetal Bernhard, Wendy Oughtred, Rose Dolinski, Kara Barreto, Kris Tyers, Mike Database (Oxford) Original Article PhosphoGRID is an online database that curates and houses experimentally verified in vivo phosphorylation sites in the Saccharomyces cerevisiae proteome (www.phosphogrid.org). Phosphosites are annotated with specific protein kinases and/or phosphatases, along with the condition(s) under which the phosphorylation occurs and/or the effects on protein function. We report here an updated data set, including nine additional high-throughput (HTP) mass spectrometry studies. The version 2.0 data set contains information on 20 177 unique phosphorylated residues, representing a 4-fold increase from version 1.0, and includes 1614 unique phosphosites derived from focused low-throughput (LTP) studies. The overlap between HTP and LTP studies represents only ∼3% of the total unique sites, but importantly 45% of sites from LTP studies with defined function were discovered in at least two independent HTP studies. The majority of new phosphosites in this update occur on previously documented proteins, suggesting that coverage of phosphoproteins in the yeast proteome is approaching saturation. We will continue to update the PhosphoGRID data set, with the expectation that the integration of information from LTP and HTP studies will enable the development of predictive models of phosphorylation-based signaling networks. Database URL: http://www.phosphogrid.org/ Oxford University Press 2013-05-11 /pmc/articles/PMC3653121/ /pubmed/23674503 http://dx.doi.org/10.1093/database/bat026 Text en © The Author(s) 2013. Published by Oxford University Press. http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Article Sadowski, Ivan Breitkreutz, Bobby-Joe Stark, Chris Su, Ting-Cheng Dahabieh, Matthew Raithatha, Sheetal Bernhard, Wendy Oughtred, Rose Dolinski, Kara Barreto, Kris Tyers, Mike The PhosphoGRID Saccharomyces cerevisiae protein phosphorylation site database: version 2.0 update |
title | The PhosphoGRID Saccharomyces cerevisiae protein phosphorylation site database: version 2.0 update |
title_full | The PhosphoGRID Saccharomyces cerevisiae protein phosphorylation site database: version 2.0 update |
title_fullStr | The PhosphoGRID Saccharomyces cerevisiae protein phosphorylation site database: version 2.0 update |
title_full_unstemmed | The PhosphoGRID Saccharomyces cerevisiae protein phosphorylation site database: version 2.0 update |
title_short | The PhosphoGRID Saccharomyces cerevisiae protein phosphorylation site database: version 2.0 update |
title_sort | phosphogrid saccharomyces cerevisiae protein phosphorylation site database: version 2.0 update |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3653121/ https://www.ncbi.nlm.nih.gov/pubmed/23674503 http://dx.doi.org/10.1093/database/bat026 |
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