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PhosphoGRID: a database of experimentally verified in vivo protein phosphorylation sites from the budding yeast Saccharomyces cerevisiae

Protein phosphorylation plays a central role in cellular regulation. Recent proteomics strategies for identifying phosphopeptides have been developed using the model organism Saccharomyces cerevisiae, and consequently, when combined with studies of individual gene products, the number of reported sp...

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Autores principales: Stark, Chris, Su, Ting-Cheng, Breitkreutz, Ashton, Lourenco, Pedro, Dahabieh, Matthew, Breitkreutz, Bobby-Joe, Tyers, Mike, Sadowski, Ivan
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2860897/
https://www.ncbi.nlm.nih.gov/pubmed/20428315
http://dx.doi.org/10.1093/database/bap026
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author Stark, Chris
Su, Ting-Cheng
Breitkreutz, Ashton
Lourenco, Pedro
Dahabieh, Matthew
Breitkreutz, Bobby-Joe
Tyers, Mike
Sadowski, Ivan
author_facet Stark, Chris
Su, Ting-Cheng
Breitkreutz, Ashton
Lourenco, Pedro
Dahabieh, Matthew
Breitkreutz, Bobby-Joe
Tyers, Mike
Sadowski, Ivan
author_sort Stark, Chris
collection PubMed
description Protein phosphorylation plays a central role in cellular regulation. Recent proteomics strategies for identifying phosphopeptides have been developed using the model organism Saccharomyces cerevisiae, and consequently, when combined with studies of individual gene products, the number of reported specific phosphorylation sites for this organism has expanded enormously. In order to systematically document and integrate these various data types, we have developed a database of experimentally verified in vivo phosphorylation sites curated from the S. cerevisiae primary literature. PhosphoGRID (www.phosphogrid.org) records the positions of over 5000 specific phosphorylated residues on 1495 gene products. Nearly 900 phosphorylated residues are reported from detailed studies of individual proteins; these in vivo phosphorylation sites are documented by a hierarchy of experimental evidence codes. Where available for specific sites, we have also noted the relevant protein kinases and/or phosphatases, the specific condition(s) under which phosphorylation occurs, and the effect(s) that phosphorylation has on protein function. The unique features of PhosphoGRID that assign both function and specific physiological conditions to each phosphorylated residue will provide a valuable benchmark for proteome-level studies and will facilitate bioinformatic analysis of cellular signal transduction networks. Database URL: http://phosphogrid.org/
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spelling pubmed-28608972010-04-28 PhosphoGRID: a database of experimentally verified in vivo protein phosphorylation sites from the budding yeast Saccharomyces cerevisiae Stark, Chris Su, Ting-Cheng Breitkreutz, Ashton Lourenco, Pedro Dahabieh, Matthew Breitkreutz, Bobby-Joe Tyers, Mike Sadowski, Ivan Database (Oxford) Original Article Protein phosphorylation plays a central role in cellular regulation. Recent proteomics strategies for identifying phosphopeptides have been developed using the model organism Saccharomyces cerevisiae, and consequently, when combined with studies of individual gene products, the number of reported specific phosphorylation sites for this organism has expanded enormously. In order to systematically document and integrate these various data types, we have developed a database of experimentally verified in vivo phosphorylation sites curated from the S. cerevisiae primary literature. PhosphoGRID (www.phosphogrid.org) records the positions of over 5000 specific phosphorylated residues on 1495 gene products. Nearly 900 phosphorylated residues are reported from detailed studies of individual proteins; these in vivo phosphorylation sites are documented by a hierarchy of experimental evidence codes. Where available for specific sites, we have also noted the relevant protein kinases and/or phosphatases, the specific condition(s) under which phosphorylation occurs, and the effect(s) that phosphorylation has on protein function. The unique features of PhosphoGRID that assign both function and specific physiological conditions to each phosphorylated residue will provide a valuable benchmark for proteome-level studies and will facilitate bioinformatic analysis of cellular signal transduction networks. Database URL: http://phosphogrid.org/ Oxford University Press 2010 2010-01-28 /pmc/articles/PMC2860897/ /pubmed/20428315 http://dx.doi.org/10.1093/database/bap026 Text en © The Author(s) 2010. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/2.5/uk/ This is Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Article
Stark, Chris
Su, Ting-Cheng
Breitkreutz, Ashton
Lourenco, Pedro
Dahabieh, Matthew
Breitkreutz, Bobby-Joe
Tyers, Mike
Sadowski, Ivan
PhosphoGRID: a database of experimentally verified in vivo protein phosphorylation sites from the budding yeast Saccharomyces cerevisiae
title PhosphoGRID: a database of experimentally verified in vivo protein phosphorylation sites from the budding yeast Saccharomyces cerevisiae
title_full PhosphoGRID: a database of experimentally verified in vivo protein phosphorylation sites from the budding yeast Saccharomyces cerevisiae
title_fullStr PhosphoGRID: a database of experimentally verified in vivo protein phosphorylation sites from the budding yeast Saccharomyces cerevisiae
title_full_unstemmed PhosphoGRID: a database of experimentally verified in vivo protein phosphorylation sites from the budding yeast Saccharomyces cerevisiae
title_short PhosphoGRID: a database of experimentally verified in vivo protein phosphorylation sites from the budding yeast Saccharomyces cerevisiae
title_sort phosphogrid: a database of experimentally verified in vivo protein phosphorylation sites from the budding yeast saccharomyces cerevisiae
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2860897/
https://www.ncbi.nlm.nih.gov/pubmed/20428315
http://dx.doi.org/10.1093/database/bap026
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