40S ribosomal protein S27a

40S ribosomal protein S27a is a protein that in humans is encoded by the RPS27A gene.^[5][6]

RPS27A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2KTF, 2L0F, 2L0T, 2XK5, 3AXC, 3NHE, 3NOB, 3PHW, 3TBL, 4UG0, 4V6X, 5AJ0, 4R62, 5FLX, 4UJD, 4KZZ, 4UJC, 3J7P, 4KZY, 4D5L, 3J7R, 4D61, 4KZX, 4UJE, 5A2Q
Identifiers
Aliases	RPS27A, CEP80, HEL112, S27A, UBA80, UBC, UBCEP1, UBCEP80, ribosomal protein S27a
External IDs	OMIM: 191343; MGI: 1925544; HomoloGene: 37715; GeneCards: RPS27A; OMA:RPS27A - orthologs
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2p16.1 Start 55,231,903 bp[1] End 55,235,853 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 A3.3 Start 29,495,846 bp[2] End 29,498,109 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left ovary granulocyte ganglionic eminence right uterine tube canal of the cervix right ovary body of uterus ventricular zone left lobe of thyroid gland anterior pituitary Top expressed in embryo embryo epiblast urinary bladder bone marrow ventricular zone uterus pancreas adrenal gland lens More reference expression data BioGPS n/a
Gene ontology Molecular function metal ion binding structural constituent of ribosome protein binding RNA binding protein tag ubiquitin protein ligase binding Cellular component cytoplasm endocytic vesicle membrane cytosol membrane nucleus ribosome myelin sheath cytosolic small ribosomal subunit nucleolus extracellular exosome plasma membrane nucleoplasm small ribosomal subunit endosome membrane extracellular space mitochondrial outer membrane endoplasmic reticulum quality control compartment vesicle endoplasmic reticulum membrane host cell Biological process DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest negative regulation of epidermal growth factor receptor signaling pathway interstrand cross-link repair nucleotide-excision repair, DNA damage recognition positive regulation of canonical Wnt signaling pathway tumor necrosis factor-mediated signaling pathway regulation of type I interferon production TRIF-dependent toll-like receptor signaling pathway Fc-epsilon receptor signaling pathway endosomal transport global genome nucleotide-excision repair NIK/NF-kappaB signaling G2/M transition of mitotic cell cycle stress-activated MAPK cascade transforming growth factor beta receptor signaling pathway macroautophagy negative regulation of canonical Wnt signaling pathway nucleotide-excision repair, DNA gap filling viral transcription error-free translesion synthesis regulation of tumor necrosis factor-mediated signaling pathway stimulatory C-type lectin receptor signaling pathway negative regulation of transforming growth factor beta receptor signaling pathway SRP-dependent cotranslational protein targeting to membrane JNK cascade regulation of transcription from RNA polymerase II promoter in response to hypoxia nucleotide-excision repair, DNA incision I-kappaB kinase/NF-kappaB signaling innate immune response Notch signaling pathway regulation of mRNA stability protein polyubiquitination negative regulation of apoptotic process negative regulation of transcription by RNA polymerase II virion assembly positive regulation of NF-kappaB transcription factor activity anaphase-promoting complex-dependent catabolic process negative regulation of type I interferon production nuclear-transcribed mRNA catabolic process, nonsense-mediated decay nucleotide-binding oligomerization domain containing signaling pathway intracellular transport of virus viral life cycle MyD88-dependent toll-like receptor signaling pathway error-prone translesion synthesis MAPK cascade fibroblast growth factor receptor signaling pathway ion transmembrane transport glycogen biosynthetic process positive regulation of apoptotic process translational initiation positive regulation of I-kappaB kinase/NF-kappaB signaling translesion synthesis transcription-coupled nucleotide-excision repair T cell receptor signaling pathway MyD88-independent toll-like receptor signaling pathway positive regulation of transcription by RNA polymerase II regulation of signal transduction by p53 class mediator positive regulation of epidermal growth factor receptor signaling pathway Wnt signaling pathway nucleotide-excision repair, DNA duplex unwinding nucleotide-excision repair, DNA incision, 5'-to lesion protein biosynthesis rRNA processing ERBB2 signaling pathway Wnt signaling pathway, planar cell polarity pathway nucleotide-excision repair, preincision complex assembly proteasome-mediated ubiquitin-dependent protein catabolic process protein folding negative regulation of G2/M transition of mitotic cell cycle protein ubiquitination protein deubiquitination SCF-dependent proteasomal ubiquitin-dependent protein catabolic process entry of bacterium into host cell transmembrane transport regulation of necroptotic process membrane organization endoplasmic reticulum mannose trimming cellular iron ion homeostasis regulation of hematopoietic stem cell differentiation protein targeting to peroxisome cytokine-mediated signaling pathway modification-dependent protein catabolic process interleukin-1-mediated signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6233 78294 Ensembl ENSG00000143947 ENSMUSG00000020460 UniProt P62979 P62983 RefSeq (mRNA) NM_002954 NM_001135592 NM_001177413 NM_001033865 NM_024277 RefSeq (protein) NP_001129064 NP_001170884 NP_002945 NP_001029037 NP_077239 Location (UCSC) Chr 2: 55.23 – 55.24 Mb Chr 11: 29.5 – 29.5 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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.^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000143947 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020460 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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 Res. 8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID 9582194.
6. "Entrez Gene: RPS27A ribosomal protein S27a".

Further reading

• Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochem. Cell Biol. 73 (11–12): 933–47. doi:10.1139/o95-101. PMID 8722009.
• Adams SM, Sharp MG, Walker RA, et al. (1992). "Differential expression of translation-associated genes in benign and malignant human breast tumours". Br. J. Cancer. 65 (1): 65–71. doi:10.1038/bjc.1992.12. PMC 1977345. PMID 1370760.
• 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. PMID 1657614. S2CID 23901646.
• 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. PMID 1660345.
• 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. doi:10.1016/S0021-9258(19)84967-0. PMID 2537304.
• Redman KL, Rechsteiner M (1989). "Identification of the long ubiquitin extension as ribosomal protein S27a". Nature. 338 (6214): 438–40. Bibcode:1989Natur.338..438R. doi:10.1038/338438a0. PMID 2538756. S2CID 4360107.
• 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. doi:10.1016/S0021-9258(17)39652-7. PMID 2581967.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• 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. PMID 8706699.
• 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". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• 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. PMID 10772958.
• Petersen BO, Wagener C, Marinoni F, et al. (2000). "Cell cycle– and cell growth–regulated proteolysis of mammalian CDC6 is dependent on APC–CDH1". Genes Dev. 14 (18): 2330–43. doi:10.1101/gad.832500. PMC 316932. PMID 10995389.
• 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. PMID 11733996.
• Yoshihama M, Uechi T, Asakawa S, et al. (2002). "The Human Ribosomal Protein Genes: Sequencing and Comparative Analysis of 73 Genes". Genome Res. 12 (3): 379–90. doi:10.1101/gr.214202. PMC 155282. PMID 11875025.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Cohen BD, Bariteau JT, Magenis LM, Dias JA (2003). "Regulation of follitropin receptor cell surface residency by the ubiquitin-proteasome pathway". Endocrinology. 144 (10): 4393–402. doi:10.1210/en.2002-0063. PMID 12960054.
• 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. PMID 14702039.
• Li H, Seth A (2004). "An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein". Oncogene. 23 (10): 1801–8. doi:10.1038/sj.onc.1207319. PMID 14755250. S2CID 37253372.