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From the research laboratory to the database: the Caenorhabditis elegans kinome in UniProtKB
Protein kinases form one of the largest protein families and are found in all species, from viruses to humans. They catalyze the reversible phosphorylation of proteins, often modifying their activity and localization. They are implicated in virtually all cellular processes and are one of the most in...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5290486/ https://www.ncbi.nlm.nih.gov/pubmed/28159896 http://dx.doi.org/10.1042/BCJ20160991 |
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author | Zaru, Rossana Magrane, Michele O'Donovan, Claire |
author_facet | Zaru, Rossana Magrane, Michele O'Donovan, Claire |
author_sort | Zaru, Rossana |
collection | PubMed |
description | Protein kinases form one of the largest protein families and are found in all species, from viruses to humans. They catalyze the reversible phosphorylation of proteins, often modifying their activity and localization. They are implicated in virtually all cellular processes and are one of the most intensively studied protein families. In recent years, they have become key therapeutic targets in drug development as natural mutations affecting kinase genes are the cause of many diseases. The vast amount of data contained in the primary literature and across a variety of biological data collections highlights the need for a repository where this information is stored in a concise and easily accessible manner. The UniProt Knowledgebase meets this need by providing the scientific community with a comprehensive, high-quality and freely accessible resource of protein sequence and functional information. Here, we describe the expert curation process for kinases, focusing on the Caenorhabditis elegans kinome. The C. elegans kinome is composed of 438 kinases and almost half of them have been functionally characterized, highlighting that C. elegans is a valuable and versatile model organism to understand the role of kinases in biological processes. |
format | Online Article Text |
id | pubmed-5290486 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-52904862017-02-08 From the research laboratory to the database: the Caenorhabditis elegans kinome in UniProtKB Zaru, Rossana Magrane, Michele O'Donovan, Claire Biochem J Review Articles Protein kinases form one of the largest protein families and are found in all species, from viruses to humans. They catalyze the reversible phosphorylation of proteins, often modifying their activity and localization. They are implicated in virtually all cellular processes and are one of the most intensively studied protein families. In recent years, they have become key therapeutic targets in drug development as natural mutations affecting kinase genes are the cause of many diseases. The vast amount of data contained in the primary literature and across a variety of biological data collections highlights the need for a repository where this information is stored in a concise and easily accessible manner. The UniProt Knowledgebase meets this need by providing the scientific community with a comprehensive, high-quality and freely accessible resource of protein sequence and functional information. Here, we describe the expert curation process for kinases, focusing on the Caenorhabditis elegans kinome. The C. elegans kinome is composed of 438 kinases and almost half of them have been functionally characterized, highlighting that C. elegans is a valuable and versatile model organism to understand the role of kinases in biological processes. Portland Press Ltd. 2017-02-15 2017-02-03 /pmc/articles/PMC5290486/ /pubmed/28159896 http://dx.doi.org/10.1042/BCJ20160991 Text en © 2017 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) . |
spellingShingle | Review Articles Zaru, Rossana Magrane, Michele O'Donovan, Claire From the research laboratory to the database: the Caenorhabditis elegans kinome in UniProtKB |
title | From the research laboratory to the database: the Caenorhabditis elegans kinome in UniProtKB |
title_full | From the research laboratory to the database: the Caenorhabditis elegans kinome in UniProtKB |
title_fullStr | From the research laboratory to the database: the Caenorhabditis elegans kinome in UniProtKB |
title_full_unstemmed | From the research laboratory to the database: the Caenorhabditis elegans kinome in UniProtKB |
title_short | From the research laboratory to the database: the Caenorhabditis elegans kinome in UniProtKB |
title_sort | from the research laboratory to the database: the caenorhabditis elegans kinome in uniprotkb |
topic | Review Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5290486/ https://www.ncbi.nlm.nih.gov/pubmed/28159896 http://dx.doi.org/10.1042/BCJ20160991 |
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