Pseudogenes are copies of already existing genes, and while their sequences resemble the original parental gene, they contain mutations which generally render them non-functional. However, recent advances in genome analysis suggest that pseudogenes can in fact be translated and have specific functions. Ubiquitin (Ub) is an abundant protein transcribed from four different genes, increasing the potential for the generation of several pseudogenes. Through human genome analysis datamining, we gathered information regarding Ub and Ub like (Ubl) pseudogenes in order to identify potentially functional variants. Through experimental validation, we found a candidate gene RPS27AP5 which not only expresses a Ub (UbP5) but a ribosomal protein (S27aP5) as well. The precursor fusion protein is matured through cleavage and both proteins behave as their respective counterparts following translation. S27aP5 is able to integrate into translating ribosomes and its expression increases the 80S, monosomal, ribosomal fraction. The existence of a functional S27a pseudogene supports the idea that ribosomes are flexible complexes and that by exchanging certain subunits; they can perform specific translational functions giving rise to specialised ribosomes.