Ribosomal protein S27a (RPS27A)

Ribosomal protein S27a (RPS27A) is a multifunctional fusion protein consisting of ubiquitin at the N-terminus and the ribosomal protein S27a at the C-terminus, encoded by the RPS27A gene. After synthesis, the ubiquitin and S27a moieties are cleaved and function independently: ubiquitin mediates protein degradation via the proteasome, while S27a incorporates into the small (40S) ribosomal subunit, playing a structural role in translation. Beyond its canonical function in ribosome assembly and protein synthesis, RPS27A is involved in cell cycle regulation, acts as a stress sensor amplifying the p53 response, regulates cell proliferation, apoptosis, and DNA repair, and exhibits tumorigenic properties through multiple cancer pathways. Clinically, aberrant expression of RPS27A is linked to poor prognosis in various cancers and has been described as a mercury exposure biomarker. Its overexpression contributes to drug resistance in certain leukemias and its critical cellular roles make it both a promising target and a challenging therapeutic candidate[1][3][5][6][7].

Other names

Ubiquitin-ribosomal protein eS31 fusion proteinUbiquitinSmall ribosomal subunit protein eS31UBA80UBCEP1UBCEP80Uba80S27AeS31CEP80HEL112UBCubiquitin carboxyl extension protein 8040S ribosomal protein S27aubiquitin Cepididymis luminal protein 112

Modulation of p53 stabilization and amplification of stress response (through interaction with MDM2); Indirectly promotes chemoresistance in leukemia cells via STAT3 upregulation