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Nucleic Acids Res ; 49(D1): D261-D265, 2021 01 08.
Article in English | MEDLINE | ID: covidwho-1387959

ABSTRACT

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.


Subject(s)
Adenosine Diphosphate Ribose/metabolism , Computational Biology/statistics & numerical data , Databases, Protein/statistics & numerical data , Proteins/metabolism , ADP-Ribosylation , Binding Sites , COVID-19/epidemiology , COVID-19/prevention & control , COVID-19/virology , Computational Biology/methods , Humans , Protein Domains , Protein Processing, Post-Translational , Proteins/chemistry , SARS-CoV-2/metabolism , SARS-CoV-2/physiology , Viral Proteins/chemistry , Viral Proteins/metabolism
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