ADPriboDB 2.0: an updated database of ADP-ribosylated proteins.
ADP-Ribosylation
Adenosine Diphosphate Ribose
/ metabolism
Binding Sites
COVID-19
/ epidemiology
Computational Biology
/ methods
Databases, Protein
/ statistics & numerical data
Humans
Protein Domains
Protein Processing, Post-Translational
Proteins
/ chemistry
SARS-CoV-2
/ metabolism
Viral Proteins
/ chemistry
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
08 01 2021
08 01 2021
Historique:
accepted:
31
10
2020
revised:
05
10
2020
received:
15
09
2020
pubmed:
3
11
2020
medline:
26
1
2021
entrez:
2
11
2020
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 33137182
pii: 5952204
doi: 10.1093/nar/gkaa941
pmc: PMC7778992
doi:
Substances chimiques
Proteins
0
Viral Proteins
0
Adenosine Diphosphate Ribose
20762-30-5
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
D261-D265Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM104135
Pays : United States
Organisme : NCI NIH HHS
ID : T32 CA009110
Pays : United States
Commentaires et corrections
Type : UpdateOf
Informations de copyright
© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.
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