4.7 Article

iCysMod: an integrative database for protein cysteine modifications in eukaryotes

Journal

BRIEFINGS IN BIOINFORMATICS
Volume 22, Issue 5, Pages -

Publisher

OXFORD UNIV PRESS
DOI: 10.1093/bib/bbaa400

Keywords

post-translational modifications (PTMs); protein cysteine modifications (PCMs); PCM events; sequence features; crosstalk

Funding

  1. National Natural Science Foundation of China [31601067, 91953123, 31700175]
  2. Key program for Department of Science and Technology of Qinghai province [2017-ZJ-Y13]
  3. Program for Guangdong Introducing Innovative and Entrepreneurial Teams [2017ZT07S096]
  4. Tip-Top Scientific and Technical Innovative Youth Talents of Guangdong special support program [2019TQ05Y351]

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The iCysMod database was developed to provide an integrative resource for protein cysteine modifications in eukaryotes, curating over 108,000 PCM events. The database offers browse and search options for accessing the dataset, along with detailed information organized for visualization. The dataset includes information on 8 types of PCMs and analysis of sequence features around cysteine modification sites for each type, showing distinct preferences for sequence recognition.
As important post-translational modifications, protein cysteine modifications (PCMs) occurring at cysteine thiol group play critical roles in the regulation of various biological processes in eukaryotes. Due to the rapid advancement of high-throughput proteomics technologies, a large number of PCM events have been identified but remain to be curated. Thus, an integrated resource of eukaryotic PCM5 will be useful for the research community. In this work, we developed an integrative database for protein cysteine modifications in eukaryotes (iCysMod), which curated and hosted 108 030 PCM events for 85 747 experimentally identified sites on 31 483 proteins from 48 eukaryotes for 8 types of PCMs, including oxidation, S-nitrosylation (-SNO), S-glutathionylation (-SSG), disulfide formation (-SSR), S-sulfhydration (-SSH), S-sulfenylation (-SOH), S-sulfinylation (-SO2H) and S-palmitoylation (-S-palm). Then, browse and search options were provided for accessing the dataset, while various detailed information about the PCM events was well organized for visualization. With human dataset in iCysMod, the sequence features around the cysteine modification sites for each PCM type were analyzed, and the results indicated that various types of PCMs presented distinct sequence recognition preferences. Moreover, different PCMs can crosstalk with each other to synergistically orchestrate specific biological processes, and 37 841 PCM events involved in 119 types of PCM co-occurrences at the same cysteine residues were finally obtained. Taken together, we anticipate that the database of iCysMod would provide a useful resource for eukaryotic PCMs to facilitate related researches, while the online service is freely available at http://icysmod.omicsbio.info.

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