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Ribosomal protein S27a pseudogene 5 (RPS27AP5) is classified as a processed pseudogene in the human genome, traditionally considered non-functional. However, recent studies demonstrate that RPS27AP5 is transcribed and translated, producing variant proteins including a ubiquitin variant (UbP5) and a ribosomal protein variant (S27aP5)[1][4]. The S27aP5 protein can incorporate into ribosomes, increasing the 80S monosome fraction and altering mRNA translation profiles, suggesting a potential functional role in modulating ribosome heterogeneity and possibly specialized translation[1][4][11]. Although these findings challenge the classic non-coding status of pseudogenes, RPS27AP5 itself is not regarded as a conventional therapeutic target, nor is there evidence linking it to drug action or established disease biomarkers[8][10].
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