Mapping Citrullinated Sites in Multiple Organs of Mice Using Hypercitrullinated Library

Justyna Fert-Bober*, Vidya Venkatraman, Christie L. Hunter, Ruining Liu, Erin L. Crowgey, Rakhi Pandey, Ronald J. Holewinski, Aleksandr Stotland, Benjamin P. Berman, Jennifer E. Van Eyk

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

28 Scopus citations


Protein citrullination (or deimination), an irreversible post-translational modification, has been implicated in several physiological and pathological processes, including gene expression regulation, apoptosis, rheumatoid arthritis, and Alzheimer's disease. Several research studies have been carried out on citrullination under many conditions. However, until now, challenges in sample preparation and data analysis have made it difficult to confidently identify a citrullinated protein and assign the citrullinated site. To overcome these limitations, we generated a mouse hyper-citrullinated spectral library and set up coordinates to confidently identify and validate citrullinated sites. Using this workflow, we detect a four-fold increase in citrullinated proteome coverage across six mouse organs compared with the current state-of-the art techniques. Our data reveal that the subcellular distribution of citrullinated proteins is tissue-type-dependent and that citrullinated targets are involved in fundamental physiological processes, including the metabolic process. These data represent the first report of a hyper-citrullinated library for the mouse and serve as a central resource for exploring the role of citrullination in this organism.

Original languageAmerican English
Pages (from-to)2270-2278
Number of pages9
JournalJournal of Proteome Research
Issue number5
StatePublished - 3 May 2019
Externally publishedYes

Bibliographical note

Publisher Copyright:
© Copyright 2019 American Chemical Society.


  • citrullination
  • mass spectrometry
  • posttranslational modification
  • protein database


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