40S ribosomal protein S27a is a protein that in humans is encoded by the RPS27Agene.
Ubiquitin, a highly conserved protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome, is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the N terminus and ribosomal protein S27a at the C terminus. When expressed in yeast, the protein is post-translationally processed, generating free ubiquitin monomer and ribosomal protein S27a. Ribosomal protein S27a is a component of the 40S subunit of the ribosome and belongs to the S27AE family of ribosomal proteins. It contains C4-type zinc finger domains and is located in the cytoplasm. Pseudogenes derived from this gene are present in the genome. As with ribosomal protein S27a, ribosomal protein L40 is also synthesized as a fusion protein with ubiquitin; similarly, ribosomal protein S30 is synthesized as a fusion protein with the ubiquitin-like protein fubi.
^Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC (Aug 1998). "A map of 75 human ribosomal protein genes". Genome Res8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID9582194.
Pancré V, Pierce RJ, Fournier F et al. (1991). "Effect of ubiquitin on platelet functions: possible identity with platelet activity suppressive lymphokine (PASL)". Eur. J. Immunol.21 (11): 2735–41. doi:10.1002/eji.1830211113. PMID1657614.
Kanayama H, Tanaka K, Aki M et al. (1992). "Changes in expressions of proteasome and ubiquitin genes in human renal cancer cells". Cancer Res.51 (24): 6677–85. PMID1660345.
Monia BP, Ecker DJ, Jonnalagadda S et al. (1989). "Gene synthesis, expression, and processing of human ubiquitin carboxyl extension proteins". J. Biol. Chem.264 (7): 4093–103. PMID2537304.
Redman KL, Rechsteiner M (1989). "Identification of the long ubiquitin extension as ribosomal protein S27a". Nature338 (6214): 438–40. doi:10.1038/338438a0. PMID2538756.
Lund PK, Moats-Staats BM, Simmons JG et al. (1985). "Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor". J. Biol. Chem.260 (12): 7609–13. PMID2581967.
Vladimirov SN, Ivanov AV, Karpova GG et al. (1996). "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry". Eur. J. Biochem.239 (1): 144–9. doi:10.1111/j.1432-1033.1996.0144u.x. PMID8706699.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Kirschner LS, Stratakis CA (2000). "Structure of the human ubiquitin fusion gene Uba80 (RPS27a) and one of its pseudogenes". Biochem. Biophys. Res. Commun.270 (3): 1106–10. doi:10.1006/bbrc.2000.2568. PMID10772958.
Bolton D, Evans PA, Stott K, Broadhurst RW (2002). "Structure and properties of a dimeric N-terminal fragment of human ubiquitin". J. Mol. Biol.314 (4): 773–87. doi:10.1006/jmbi.2001.5181. PMID11733996.
Cohen BD, Bariteau JT, Magenis LM, Dias JA (2003). "Regulation of follitropin receptor cell surface residency by the ubiquitin-proteasome pathway". Endocrinology144 (10): 4393–402. doi:10.1210/en.2002-0063. PMID12960054.
Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet.36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.