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HIstome—a relational knowledgebase of human histone proteins and histone modifying enzymes
Histones are abundant nuclear proteins that are essential for the packaging of eukaryotic DNA into chromosomes. Different histone variants, in combination with their modification ‘code’, control regulation of gene expression in diverse cellular processes. Several enzymes that catalyze the addition a...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3245077/ https://www.ncbi.nlm.nih.gov/pubmed/22140112 http://dx.doi.org/10.1093/nar/gkr1125 |
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author | Khare, Satyajeet P. Habib, Farhat Sharma, Rahul Gadewal, Nikhil Gupta, Sanjay Galande, Sanjeev |
author_facet | Khare, Satyajeet P. Habib, Farhat Sharma, Rahul Gadewal, Nikhil Gupta, Sanjay Galande, Sanjeev |
author_sort | Khare, Satyajeet P. |
collection | PubMed |
description | Histones are abundant nuclear proteins that are essential for the packaging of eukaryotic DNA into chromosomes. Different histone variants, in combination with their modification ‘code’, control regulation of gene expression in diverse cellular processes. Several enzymes that catalyze the addition and removal of multiple histone modifications have been discovered in the past decade, enabling investigations of their role(s) in normal cellular processes and diverse pathological conditions. This sudden influx of data, however, has resulted in need of an updated knowledgebase that compiles, organizes and presents curated scientific information to the user in an easily accessible format. Here, we present HIstome, a browsable, manually curated, relational database that provides information about human histone proteins, their sites of modifications, variants and modifying enzymes. HIstome is a knowledgebase of 55 human histone proteins, 106 distinct sites of their post-translational modifications (PTMs) and 152 histone-modifying enzymes. Entries have been grouped into 5 types of histones, 8 types of post-translational modifications and 14 types of enzymes that catalyze addition and removal of these modifications. The resource will be useful for epigeneticists, pharmacologists and clinicians. HIstome: The Histone Infobase is available online at http://www.iiserpune.ac.in/∼coee/histome/ and http://www.actrec.gov.in/histome/. |
format | Online Article Text |
id | pubmed-3245077 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-32450772012-01-10 HIstome—a relational knowledgebase of human histone proteins and histone modifying enzymes Khare, Satyajeet P. Habib, Farhat Sharma, Rahul Gadewal, Nikhil Gupta, Sanjay Galande, Sanjeev Nucleic Acids Res Articles Histones are abundant nuclear proteins that are essential for the packaging of eukaryotic DNA into chromosomes. Different histone variants, in combination with their modification ‘code’, control regulation of gene expression in diverse cellular processes. Several enzymes that catalyze the addition and removal of multiple histone modifications have been discovered in the past decade, enabling investigations of their role(s) in normal cellular processes and diverse pathological conditions. This sudden influx of data, however, has resulted in need of an updated knowledgebase that compiles, organizes and presents curated scientific information to the user in an easily accessible format. Here, we present HIstome, a browsable, manually curated, relational database that provides information about human histone proteins, their sites of modifications, variants and modifying enzymes. HIstome is a knowledgebase of 55 human histone proteins, 106 distinct sites of their post-translational modifications (PTMs) and 152 histone-modifying enzymes. Entries have been grouped into 5 types of histones, 8 types of post-translational modifications and 14 types of enzymes that catalyze addition and removal of these modifications. The resource will be useful for epigeneticists, pharmacologists and clinicians. HIstome: The Histone Infobase is available online at http://www.iiserpune.ac.in/∼coee/histome/ and http://www.actrec.gov.in/histome/. Oxford University Press 2012-01 2011-12-02 /pmc/articles/PMC3245077/ /pubmed/22140112 http://dx.doi.org/10.1093/nar/gkr1125 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 Khare, Satyajeet P. Habib, Farhat Sharma, Rahul Gadewal, Nikhil Gupta, Sanjay Galande, Sanjeev HIstome—a relational knowledgebase of human histone proteins and histone modifying enzymes |
title | HIstome—a relational knowledgebase of human histone proteins and histone modifying enzymes |
title_full | HIstome—a relational knowledgebase of human histone proteins and histone modifying enzymes |
title_fullStr | HIstome—a relational knowledgebase of human histone proteins and histone modifying enzymes |
title_full_unstemmed | HIstome—a relational knowledgebase of human histone proteins and histone modifying enzymes |
title_short | HIstome—a relational knowledgebase of human histone proteins and histone modifying enzymes |
title_sort | histome—a relational knowledgebase of human histone proteins and histone modifying enzymes |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3245077/ https://www.ncbi.nlm.nih.gov/pubmed/22140112 http://dx.doi.org/10.1093/nar/gkr1125 |
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