DIGGER: exploring the functional role of alternative splicing in protein interactions.
Alternative Splicing
Binding Sites
Computational Biology
/ methods
Databases, Protein
Exons
Humans
Internet
Models, Molecular
Protein Binding
Protein Biosynthesis
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Protein Interaction Mapping
/ methods
Protein Isoforms
Proteome
/ chemistry
RNA, Messenger
/ genetics
Software
Thermodynamics
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:
04
09
2020
revised:
01
09
2020
received:
17
07
2020
pubmed:
26
9
2020
medline:
21
1
2021
entrez:
25
9
2020
Statut:
ppublish
Résumé
Alternative splicing plays a major role in regulating the functional repertoire of the proteome. However, isoform-specific effects to protein-protein interactions (PPIs) are usually overlooked, making it impossible to judge the functional role of individual exons on a systems biology level. We overcome this barrier by integrating protein-protein interactions, domain-domain interactions and residue-level interactions information to lift exon expression analysis to a network level. Our user-friendly database DIGGER is available at https://exbio.wzw.tum.de/digger and allows users to seamlessly switch between isoform and exon-centric views of the interactome and to extract sub-networks of relevant isoforms, making it an essential resource for studying mechanistic consequences of alternative splicing.
Identifiants
pubmed: 32976589
pii: 5911747
doi: 10.1093/nar/gkaa768
pmc: PMC7778957
doi:
Substances chimiques
Protein Isoforms
0
Proteome
0
RNA, Messenger
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
D309-D318Informations de copyright
© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.
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