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ADPriboDB v2.0: 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....
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7523110/ https://www.ncbi.nlm.nih.gov/pubmed/32995784 http://dx.doi.org/10.1101/2020.09.24.298851 |
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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 9,097 ADP-ribosylated proteins, of which 6,708 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-7523110 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Cold Spring Harbor Laboratory |
record_format | MEDLINE/PubMed |
spelling | pubmed-75231102020-09-30 ADPriboDB v2.0: 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. bioRxiv Article 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 9,097 ADP-ribosylated proteins, of which 6,708 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. Cold Spring Harbor Laboratory 2020-09-25 /pmc/articles/PMC7523110/ /pubmed/32995784 http://dx.doi.org/10.1101/2020.09.24.298851 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/It is made available under a CC-BY-NC-ND 4.0 International license (https://creativecommons.org/licenses/by-nc-nd/4.0/) |
spellingShingle | Article Ayyappan, Vinay Wat, Ricky Barber, Calvin Vivelo, Christina A. Gauch, Kathryn Visanpattanasin, Pat Cook, Garth Sazeides, Christos Leung, Anthony K. L. ADPriboDB v2.0: An Updated Database of ADP-ribosylated Proteins |
title | ADPriboDB v2.0: An Updated Database of ADP-ribosylated Proteins |
title_full | ADPriboDB v2.0: An Updated Database of ADP-ribosylated Proteins |
title_fullStr | ADPriboDB v2.0: An Updated Database of ADP-ribosylated Proteins |
title_full_unstemmed | ADPriboDB v2.0: An Updated Database of ADP-ribosylated Proteins |
title_short | ADPriboDB v2.0: An Updated Database of ADP-ribosylated Proteins |
title_sort | adpribodb v2.0: an updated database of adp-ribosylated proteins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7523110/ https://www.ncbi.nlm.nih.gov/pubmed/32995784 http://dx.doi.org/10.1101/2020.09.24.298851 |
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