Selenium is a biologically active trace element. Being a part of several proteins, it is associated with the activity of many organs, tissues, and systems of the organism. To date, there are 25 mammalian selenoproteins, one of which is SelV (Selenoprotein V). Since this protein has a thioredoxin-like folding and a conserved motif CXXU (where C is cystein and U is selenocystein) in its catalytic center, it belongs to the redox proteins family participating in redox reactions. In this paper the redox protein SelV was shown to be able to interact with O-linked N-acetylglucosamine transferase (OGT) and proteins belonging to the ASB family (Asb-17 and Asb-9). The specificity of SelV interactions with OGT and Asb-9, but not with Asb-17, is confirmed by the coimmunoprecipitation method. In addition, expression of SelV mRNA in the later stages of spermatogenesis, as well as in puberty, and the reproductive periods of rats, is shown.