DisCanVis

DisCanVis visualizes and integrates cancer mutation data with structural and functional annotations to contextualize mutations within intrinsically disordered proteins (IDPs) and support interpretation of their roles in cancer.


Key Features:

  • Integration of Genomic and Protein Data: Combines genome-level information from cancer genome projects with structural and functional protein annotations to contextualize cancer mutations within proteins.
  • Visualization of Mutations and Annotations: Maps cancer mutations onto protein sequences highlighting intrinsically disordered regions, structural annotations, and functional sites.
  • Integration of Experimental IDP Characterizations: Incorporates experimental characterizations of intrinsically disordered proteins alongside genomic mutation data.
  • REST API Interface: Provides a REST API for programmatic access and batch analyses across sets of proteins.
  • Precompiled Tables: Supplies precompiled tables for efficient retrieval and analysis of mutation and annotation data.

Scientific Applications:

  • Cancer genomics and proteomics analysis: Supports analysis of cancer mutation landscapes in the context of protein disorder and function.
  • Interpretation of mutation impact in IDPs: Enables investigation of how mutations within disordered regions may affect protein function and contribute to cancer development and progression.
  • Discovery of disease-associated disordered regions: Facilitates identification of novel intrinsically disordered regions with potential disease associations.

Methodology:

Systematic integration of data from cancer genome projects with experimental characterizations of IDPs and with structural and functional protein annotations, with data exposed via precompiled tables and a REST API.

Topics

Details

License:
Not licensed
Tool Type:
web application
Operating Systems:
Mac, Linux, Windows
Added:
2/19/2023
Last Updated:
11/24/2024

Operations

Publications

Deutsch N, Pajkos M, Erdős G, Dosztányi Z. DisCanVis: Visualizing integrated structural and functional annotations to better understand the effect of cancer mutations located within disordered proteins. Protein Science. 2022;32(1). doi:10.1002/pro.4522. PMID:36452990. PMCID:PMC9793970.

Documentation