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PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse

PhosphoSitePlus (http://www.phosphosite.org) is an open, comprehensive, manually curated and interactive resource for studying experimentally observed post-translational modifications, primarily of human and mouse proteins. It encompasses 1 30 000 non-redundant modification sites, primarily phosphor...

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Autores principales: Hornbeck, Peter V., Kornhauser, Jon M., Tkachev, Sasha, Zhang, Bin, Skrzypek, Elżbieta, Murray, Beth, Latham, Vaughan, Sullivan, Michael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3245126/
https://www.ncbi.nlm.nih.gov/pubmed/22135298
http://dx.doi.org/10.1093/nar/gkr1122
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author Hornbeck, Peter V.
Kornhauser, Jon M.
Tkachev, Sasha
Zhang, Bin
Skrzypek, Elżbieta
Murray, Beth
Latham, Vaughan
Sullivan, Michael
author_facet Hornbeck, Peter V.
Kornhauser, Jon M.
Tkachev, Sasha
Zhang, Bin
Skrzypek, Elżbieta
Murray, Beth
Latham, Vaughan
Sullivan, Michael
author_sort Hornbeck, Peter V.
collection PubMed
description PhosphoSitePlus (http://www.phosphosite.org) is an open, comprehensive, manually curated and interactive resource for studying experimentally observed post-translational modifications, primarily of human and mouse proteins. It encompasses 1 30 000 non-redundant modification sites, primarily phosphorylation, ubiquitinylation and acetylation. The interface is designed for clarity and ease of navigation. From the home page, users can launch simple or complex searches and browse high-throughput data sets by disease, tissue or cell line. Searches can be restricted by specific treatments, protein types, domains, cellular components, disease, cell types, cell lines, tissue and sequences or motifs. A few clicks of the mouse will take users to substrate pages or protein pages with sites, sequences, domain diagrams and molecular visualization of side-chains known to be modified; to site pages with information about how the modified site relates to the functions of specific proteins and cellular processes and to curated information pages summarizing the details from one record. PyMOL and Chimera scripts that colorize reactive groups on residues that are modified can be downloaded. Features designed to facilitate proteomic analyses include downloads of modification sites, kinase–substrate data sets, sequence logo generators, a Cytoscape plugin and BioPAX download to enable pathway visualization of the kinase–substrate interactions in PhosphoSitePlus®.
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spelling pubmed-32451262012-01-10 PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse Hornbeck, Peter V. Kornhauser, Jon M. Tkachev, Sasha Zhang, Bin Skrzypek, Elżbieta Murray, Beth Latham, Vaughan Sullivan, Michael Nucleic Acids Res Articles PhosphoSitePlus (http://www.phosphosite.org) is an open, comprehensive, manually curated and interactive resource for studying experimentally observed post-translational modifications, primarily of human and mouse proteins. It encompasses 1 30 000 non-redundant modification sites, primarily phosphorylation, ubiquitinylation and acetylation. The interface is designed for clarity and ease of navigation. From the home page, users can launch simple or complex searches and browse high-throughput data sets by disease, tissue or cell line. Searches can be restricted by specific treatments, protein types, domains, cellular components, disease, cell types, cell lines, tissue and sequences or motifs. A few clicks of the mouse will take users to substrate pages or protein pages with sites, sequences, domain diagrams and molecular visualization of side-chains known to be modified; to site pages with information about how the modified site relates to the functions of specific proteins and cellular processes and to curated information pages summarizing the details from one record. PyMOL and Chimera scripts that colorize reactive groups on residues that are modified can be downloaded. Features designed to facilitate proteomic analyses include downloads of modification sites, kinase–substrate data sets, sequence logo generators, a Cytoscape plugin and BioPAX download to enable pathway visualization of the kinase–substrate interactions in PhosphoSitePlus®. Oxford University Press 2012-01 2011-11-30 /pmc/articles/PMC3245126/ /pubmed/22135298 http://dx.doi.org/10.1093/nar/gkr1122 Text en © The Author(s) 2011. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Articles
Hornbeck, Peter V.
Kornhauser, Jon M.
Tkachev, Sasha
Zhang, Bin
Skrzypek, Elżbieta
Murray, Beth
Latham, Vaughan
Sullivan, Michael
PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
title PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
title_full PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
title_fullStr PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
title_full_unstemmed PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
title_short PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
title_sort phosphositeplus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3245126/
https://www.ncbi.nlm.nih.gov/pubmed/22135298
http://dx.doi.org/10.1093/nar/gkr1122
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