Posttranslational modifications of human histone H3: an update

Proteomics. 2014 Sep;14(17-18):2047-60. doi: 10.1002/pmic.201300435. Epub 2014 Aug 8.


Histone proteins, the fundamental components of chromatin, are highly conserved proteins that present in eukaryotic nuclei. They organize genomic DNA to form nucleosomes, the basic units of chromatin. PTMs of histones play essential roles in many biological processes, such as chromatin condensation, gene expression, cell differentiation, and apoptosis. With the advancement of proteomic technology, a growing number of histone PTMs have been identified, including ADP-ribosylation, biotinylation, citrullination, crotonylation, O-GlcNAcylation, glutathionylation, succinylation, and so on. Because of the fast growing list of these PTMs in just a few years, the functions of these marks are being studied intensively. As histone H3 has the most number of PTMs among the histone members, in this review, we would like to present the overall concepts of the more familiar PTMs as well as discussing all the recently identified yet less well-known PTMs on human histone H3.

Keywords: Cell biology; Histone H3; Mass spectrometry; Novel posttranslational modifications; Tandem mass spectrometry.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Biochemical Phenomena
  • Histones / chemistry*
  • Histones / metabolism*
  • Humans
  • Mass Spectrometry
  • Protein Processing, Post-Translational*


  • Histones