Protein arginine methyltransferase 5 (PRMT5) belongs to the class II arginine methyltransferases and catalyzes monomethylation and symmetrical dimethylation of arginines on proteins. It has recently emerged as a promising cancer drug target, and two PRMT5 inhibitors are currently in clinical trials for a range malignancies. Despite the recognized therapeutic potential, it is unclear which PRMT5 functions underlie its oncogenic activity.

A group of scientists from the Laboratory of Molecular Bases of Embryogenesis, IBCh RAS, together with colleagues from the Laboratory of Mathematical Methods and Models in Bioinformatics, IPPI RAS developed a bioinformatics method that allows one to reveal genes that appear or disappear at a certain stage of evolution. Using this method, a number of genes were found that disappeared in warm-blooded animals, including humans.

All genomes contain millions of short open reading frames (<100 codons) that are discarded during genome annotation. Recently, it has been shown that peptides encoded by short open reading frames can perform many important functions in animal cells.