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ADPriboDB 2.0: an updated database of ADP-ribosylated proteins
ADP-ribosylation is a protein modification responsible for biological processes such as DNA repair, RNA regulation, cell cycle and biomolecular condensate formation. Dysregulation of ADP-ribosylation is implicated in cancer, neurodegeneration and viral infection. We developed ADPriboDB (adpribodb.le...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7778992/ https://www.ncbi.nlm.nih.gov/pubmed/33137182 http://dx.doi.org/10.1093/nar/gkaa941 |
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author | Ayyappan, Vinay Wat, Ricky Barber, Calvin Vivelo, Christina A Gauch, Kathryn Visanpattanasin, Pat Cook, Garth Sazeides, Christos Leung, Anthony K L |
author_facet | Ayyappan, Vinay Wat, Ricky Barber, Calvin Vivelo, Christina A Gauch, Kathryn Visanpattanasin, Pat Cook, Garth Sazeides, Christos Leung, Anthony K L |
author_sort | Ayyappan, Vinay |
collection | PubMed |
description | ADP-ribosylation is a protein modification responsible for biological processes such as DNA repair, RNA regulation, cell cycle and biomolecular condensate formation. Dysregulation of ADP-ribosylation is implicated in cancer, neurodegeneration and viral infection. We developed ADPriboDB (adpribodb.leunglab.org) to facilitate studies in uncovering insights into the mechanisms and biological significance of ADP-ribosylation. ADPriboDB 2.0 serves as a one-stop repository comprising 48 346 entries and 9097 ADP-ribosylated proteins, of which 6708 were newly identified since the original database release. In this updated version, we provide information regarding the sites of ADP-ribosylation in 32 946 entries. The wealth of information allows us to interrogate existing databases or newly available data. For example, we found that ADP-ribosylated substrates are significantly associated with the recently identified human protein interaction networks associated with SARS-CoV-2, which encodes a conserved protein domain called macrodomain that binds and removes ADP-ribosylation. In addition, we create a new interactive tool to visualize the local context of ADP-ribosylation, such as structural and functional features as well as other post-translational modifications (e.g. phosphorylation, methylation and ubiquitination). This information provides opportunities to explore the biology of ADP-ribosylation and generate new hypotheses for experimental testing. |
format | Online Article Text |
id | pubmed-7778992 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-77789922021-01-06 ADPriboDB 2.0: an updated database of ADP-ribosylated proteins Ayyappan, Vinay Wat, Ricky Barber, Calvin Vivelo, Christina A Gauch, Kathryn Visanpattanasin, Pat Cook, Garth Sazeides, Christos Leung, Anthony K L Nucleic Acids Res Database Issue ADP-ribosylation is a protein modification responsible for biological processes such as DNA repair, RNA regulation, cell cycle and biomolecular condensate formation. Dysregulation of ADP-ribosylation is implicated in cancer, neurodegeneration and viral infection. We developed ADPriboDB (adpribodb.leunglab.org) to facilitate studies in uncovering insights into the mechanisms and biological significance of ADP-ribosylation. ADPriboDB 2.0 serves as a one-stop repository comprising 48 346 entries and 9097 ADP-ribosylated proteins, of which 6708 were newly identified since the original database release. In this updated version, we provide information regarding the sites of ADP-ribosylation in 32 946 entries. The wealth of information allows us to interrogate existing databases or newly available data. For example, we found that ADP-ribosylated substrates are significantly associated with the recently identified human protein interaction networks associated with SARS-CoV-2, which encodes a conserved protein domain called macrodomain that binds and removes ADP-ribosylation. In addition, we create a new interactive tool to visualize the local context of ADP-ribosylation, such as structural and functional features as well as other post-translational modifications (e.g. phosphorylation, methylation and ubiquitination). This information provides opportunities to explore the biology of ADP-ribosylation and generate new hypotheses for experimental testing. Oxford University Press 2020-11-02 /pmc/articles/PMC7778992/ /pubmed/33137182 http://dx.doi.org/10.1093/nar/gkaa941 Text en © The Author(s) 2020. 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 Non-Commercial 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 Ayyappan, Vinay Wat, Ricky Barber, Calvin Vivelo, Christina A Gauch, Kathryn Visanpattanasin, Pat Cook, Garth Sazeides, Christos Leung, Anthony K L ADPriboDB 2.0: an updated database of ADP-ribosylated proteins |
title | ADPriboDB 2.0: an updated database of ADP-ribosylated proteins |
title_full | ADPriboDB 2.0: an updated database of ADP-ribosylated proteins |
title_fullStr | ADPriboDB 2.0: an updated database of ADP-ribosylated proteins |
title_full_unstemmed | ADPriboDB 2.0: an updated database of ADP-ribosylated proteins |
title_short | ADPriboDB 2.0: an updated database of ADP-ribosylated proteins |
title_sort | adpribodb 2.0: an updated database of adp-ribosylated proteins |
topic | Database Issue |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7778992/ https://www.ncbi.nlm.nih.gov/pubmed/33137182 http://dx.doi.org/10.1093/nar/gkaa941 |
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