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ADPriboDB: The database of ADP-ribosylated proteins
ADP-ribosylation refers to the addition of one or more ADP-ribose units onto proteins post-translationally. This protein modification is often added by ADP-ribosyltransferases, commonly known as PARPs, but it can also be added by other enzymes, including sirtuins or bacterial toxins. While past lite...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5210603/ https://www.ncbi.nlm.nih.gov/pubmed/27507885 http://dx.doi.org/10.1093/nar/gkw706 |
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author | Vivelo, Christina A. Wat, Ricky Agrawal, Charul Tee, Hui Yi Leung, Anthony K. L. |
author_facet | Vivelo, Christina A. Wat, Ricky Agrawal, Charul Tee, Hui Yi Leung, Anthony K. L. |
author_sort | Vivelo, Christina A. |
collection | PubMed |
description | ADP-ribosylation refers to the addition of one or more ADP-ribose units onto proteins post-translationally. This protein modification is often added by ADP-ribosyltransferases, commonly known as PARPs, but it can also be added by other enzymes, including sirtuins or bacterial toxins. While past literature has utilized a variety of methods to identify ADP-ribosylated proteins, recent proteomics studies bring the power of mass spectrometry to determine sites of the modification. To appreciate the diverse roles of ADP-ribosylation across the proteome, we have created ADPriboDB – a database of ADP-ribosylated proteins (http://ADPriboDB.leunglab.org). Each entry of ADPriboDB is annotated manually by at least two independent curators from the literature between January 1975 and July 2015. The current database includes over 12 400 protein entries from 459 publications, identifying 2389 unique proteins. Here, we describe the structure and the current state of ADPriboDB as well as the criteria for entry inclusion. Using this aggregate data, we identified a statistically significant enrichment of ADP-ribosylated proteins in non-membranous RNA granules. To our knowledge, ADPriboDB is the first publicly available database encapsulating ADP-ribosylated proteins identified from the past 40 years, with a hope to facilitate the research of both basic scientists and clinicians to better understand ADP-ribosylation at the molecular level. |
format | Online Article Text |
id | pubmed-5210603 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-52106032017-01-05 ADPriboDB: The database of ADP-ribosylated proteins Vivelo, Christina A. Wat, Ricky Agrawal, Charul Tee, Hui Yi Leung, Anthony K. L. Nucleic Acids Res Database Issue ADP-ribosylation refers to the addition of one or more ADP-ribose units onto proteins post-translationally. This protein modification is often added by ADP-ribosyltransferases, commonly known as PARPs, but it can also be added by other enzymes, including sirtuins or bacterial toxins. While past literature has utilized a variety of methods to identify ADP-ribosylated proteins, recent proteomics studies bring the power of mass spectrometry to determine sites of the modification. To appreciate the diverse roles of ADP-ribosylation across the proteome, we have created ADPriboDB – a database of ADP-ribosylated proteins (http://ADPriboDB.leunglab.org). Each entry of ADPriboDB is annotated manually by at least two independent curators from the literature between January 1975 and July 2015. The current database includes over 12 400 protein entries from 459 publications, identifying 2389 unique proteins. Here, we describe the structure and the current state of ADPriboDB as well as the criteria for entry inclusion. Using this aggregate data, we identified a statistically significant enrichment of ADP-ribosylated proteins in non-membranous RNA granules. To our knowledge, ADPriboDB is the first publicly available database encapsulating ADP-ribosylated proteins identified from the past 40 years, with a hope to facilitate the research of both basic scientists and clinicians to better understand ADP-ribosylation at the molecular level. Oxford University Press 2017-01-04 2016-08-09 /pmc/articles/PMC5210603/ /pubmed/27507885 http://dx.doi.org/10.1093/nar/gkw706 Text en © The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Database Issue Vivelo, Christina A. Wat, Ricky Agrawal, Charul Tee, Hui Yi Leung, Anthony K. L. ADPriboDB: The database of ADP-ribosylated proteins |
title | ADPriboDB: The database of ADP-ribosylated proteins |
title_full | ADPriboDB: The database of ADP-ribosylated proteins |
title_fullStr | ADPriboDB: The database of ADP-ribosylated proteins |
title_full_unstemmed | ADPriboDB: The database of ADP-ribosylated proteins |
title_short | ADPriboDB: The database of ADP-ribosylated proteins |
title_sort | adpribodb: the database of adp-ribosylated proteins |
topic | Database Issue |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5210603/ https://www.ncbi.nlm.nih.gov/pubmed/27507885 http://dx.doi.org/10.1093/nar/gkw706 |
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