Background
Propionylation of lysine, structurally similar to lysine acetylation, is a newly identified reversible modification controlling protein activity. The reversible lysine propionylation has been well demonstrated in both prokaryotes and eukaryotes in wide ranges of proteins including histones and non-histone substrates, such as p53. It is speculated that lysine propionylation plays a vital role in the regulation of multiple cellular processes including chromatin dynamics, plasticity, and DNA transcriptional regulation by sharing same regulative enzymes with lysine acetylation or with its unique regulative enzymes.
Cellular location
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