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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....

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Autores principales: Ayyappan, Vinay, Wat, Ricky, Barber, Calvin, Vivelo, Christina A., Gauch, Kathryn, Visanpattanasin, Pat, Cook, Garth, Sazeides, Christos, Leung, Anthony K. L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory 2020
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.
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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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