RedoxDB--a curated database for experimentally verified protein oxidative modification

Bioinformatics. 2012 Oct 1;28(19):2551-2. doi: 10.1093/bioinformatics/bts468. Epub 2012 Jul 25.


Summary: Redox regulation and signaling, which are involved in various cellular processes, have become one of the research focuses in the past decade. Cysteine thiol groups are particularly susceptible to post-translational modification, and their reversible oxidation is of critical role in redox regulation and signaling. With the tremendous improvement of techniques, hundreds of redox proteins along with their redox-sensitive cysteines have been reported, and the number is still fast growing. However, until now there is no database to accommodate the rapid accumulation of information on protein oxidative modification. Here we present RedoxDB-a manually curated database for experimentally validated redox proteins. RedoxDB (version 1.0) consists of two datasets (A and B, for proteins with or without verified modified cysteines, respectively) and includes 2157 redox proteins containing 2203 cysteine residues with oxidative modification. For each modified cysteine, the exact position, modification type and flanking sequence are provided. Additional information, including gene name, organism, sequence, literature references and links to UniProt and PDB, is also supplied. The database supports several functions including data search, blast and browsing. Bulk download of the entire dataset is also available. We expect that RedoxDB will be useful for both experimental studies and computational analyses of protein oxidative modification.

Availability: The database is freely available at:


Supplementary information: Supplementary data are available at Bioinformatics Online.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Computational Biology
  • Cysteine / chemistry*
  • Databases, Protein*
  • Oxidation-Reduction*
  • Protein Processing, Post-Translational
  • Proteins / chemistry*
  • Sulfhydryl Compounds / chemistry
  • User-Computer Interface


  • Proteins
  • Sulfhydryl Compounds
  • Cysteine