UbiBrowser 2.0

UbiBrowser 2.0 provides an integrated database of known and predicted interactions between ubiquitin ligases (E3s), deubiquitinases, and their substrates to support analysis of ubiquitination-mediated protein regulation.


Key Features:

  • Extensive data collection: Manually curated 4,068 known E3–substrate interactions (ESIs) and 967 deubiquitinase–substrate interactions (DSIs), and computationally predicts approximately 2.2 million highly confident ESIs/DSIs.
  • Expanded species coverage: Includes curated and predicted interactions across 39 eukaryotic organisms.
  • Simultaneous exploration: Enables investigation of both upstream E3 ligases and deubiquitinases for specific substrates.
  • Uniform confidence scoring: Applies a standardized confidence scoring system to rank predicted ESIs and DSIs.
  • Scale expansion: Total data volume increased by more than 210-fold compared to the predecessor.

Scientific Applications:

  • Ubiquitination dynamics: Supports research into the balance between ubiquitin ligase-mediated ubiquitination and deubiquitinase-mediated deubiquitination.
  • Protein degradation regulation: Aids analysis of regulatory mechanisms governing ubiquitin-dependent protein degradation pathways.
  • Target discovery: Facilitates identification of candidate ubiquitination-related drug targets in diseases with dysregulated ubiquitination.

Methodology:

Manual curation of 4,068 ESIs and 967 DSIs, computational prediction of approximately 2.2 million ESIs/DSIs across 39 organisms, and application of a standardized confidence scoring system to rank predicted interactions.

Topics

Details

Cost:
Free of charge
Tool Type:
web application
Operating Systems:
Mac, Linux, Windows
Added:
3/9/2022
Last Updated:
3/9/2022

Operations

Data Inputs & Outputs

Fold recognition

Publications

Wang X, Li Y, He M, Kong X, Jiang P, Liu X, Diao L, Zhang X, Li H, Ling X, Xia S, Liu Z, Liu Y, Cui C, Wang Y, Tang L, Zhang L, He F, Li D. UbiBrowser 2.0: a comprehensive resource for proteome-wide known and predicted ubiquitin ligase/deubiquitinase–substrate interactions in eukaryotic species. Nucleic Acids Research. 2021;50(D1):D719-D728. doi:10.1093/nar/gkab962. PMID:34669962. PMCID:PMC8728189.

PMID: 34669962
PMCID: PMC8728189
Funding: - National Natural Science Foundation of China: 31871341, 32088101 - National Key Research and Development Program of China: 2020YFE0202200