ADPriboDB 2.0: an updated database of ADP-ribosylated proteins

Nucleic Acids Res. 2021 Jan 8;49(D1):D261-D265. doi: 10.1093/nar/gkaa941.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

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

Substances

  • Proteins
  • Viral Proteins
  • Adenosine Diphosphate Ribose