40S ribosomal protein S25

40S ribosomal protein S25 (eS25) is a protein that in humans is encoded by the RPS25 gene.[4][5]

RPS25
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4UG0, 4V6X, 5A2Q, 5AJ0, 5FLX
Identifiers
Aliases	RPS25, S25, ribosomal protein S25
External IDs	OMIM: 180465 MGI: 1922867 HomoloGene: 133893 GeneCards: RPS25
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11q23.3 Start 119,015,712 bp[1] End 119,018,691 bp[1]
Gene ontology Molecular function • GO:0001948 protein binding • RNA binding • structural constituent of ribosome Cellular component • cytosol • ribosome • cytosolic small ribosomal subunit • nucleolus • small ribosomal subunit • extracellular exosome • cell nucleus • nucleoplasm • extracellular matrix • GO:0097483, GO:0097481 postsynaptic density Biological process • viral transcription • SRP-dependent cotranslational protein targeting to membrane • translational initiation • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay • rRNA processing • protein biosynthesis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6230	75617
Ensembl	ENSG00000280831 ENSG00000118181	n/a
UniProt	P62851	P62852
RefSeq (mRNA)	NM_001028	NM_024266
RefSeq (protein)	NP_001019	NP_077228
Location (UCSC)	Chr 11: 119.02 – 119.02 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

Ribosomes are cellular macromolecules that catalyze protein synthesis across all kingdoms of life. The eukaryotic ribosome consists of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 distinct proteins. The RPS25 gene encodes the eukaryote-specific ribosomal protein eS25 that is a component of the 40S subunit. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.[5]

Interactions

Besides the interactions that position eS25 at its location in the E site region of the 40S ribosomal subunit, eS25 has been suggested to interact with other cellular proteins. One study has found that eS25 interacts with MDM2 as part of a regulatory feedback loop that stabilizes p53.[6] Additionally, eS25 has been shown to interact with CDC5L.[7]

Function

As a ribosomal protein, eS25 likely plays a role in general protein synthesis; however, the RPS25 gene is non-essential for cellular viability in budding yeast and in select mammalian cell lines, implying that it is not essential for eukaryotic protein synthesis.[8][9] Studies have implicates eS25 in the control of several specialized forms of translation, including that mediated by viral IRESs.[10][11]

See also

• Eukaryotic translation
• 40S ribosomal subunit
• IRES

References

1. ENSG00000118181 GRCh38: Ensembl release 89: ENSG00000280831, ENSG00000118181 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Li ML, Latoud C, Center MS (November 1991). "Cloning and sequencing a cDNA encoding human ribosomal protein S25". Gene. 107 (2): 329–33. doi:10.1016/0378-1119(91)90335-9. PMID 1748303.
5. "Entrez Gene: RPS25 ribosomal protein S25".
6. Zhang X, Wang W, Wang H, Wang MH, Xu W, Zhang R (May 2013). "Identification of ribosomal protein S25 (RPS25)-MDM2-p53 regulatory feedback loop". Oncogene. 32 (22): 2782–91. doi:10.1038/onc.2012.289. PMC 6714567. PMID 22777350.
7. Ajuh P, Kuster B, Panov K, Zomerdijk JC, Mann M, Lamond AI (December 2000). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". The EMBO Journal. 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. PMC 305846. PMID 11101529.
8. Steffen KK, McCormick MA, Pham KM, MacKay VL, Delaney JR, Murakami CJ, et al. (May 2012). "Ribosome deficiency protects against ER stress in Saccharomyces cerevisiae". Genetics. 191 (1): 107–18. doi:10.1534/genetics.111.136549. PMC 3338253. PMID 22377630.
9. Fuchs G, Petrov AN, Marceau CD, Popov LM, Chen J, O'Leary SE, et al. (January 2015). "Kinetic pathway of 40S ribosomal subunit recruitment to hepatitis C virus internal ribosome entry site". Proceedings of the National Academy of Sciences of the United States of America. 112 (2): 319–25. Bibcode:2015PNAS..112..319F. doi:10.1073/pnas.1421328111. PMC 4299178. PMID 25516984.
10. Landry DM, Hertz MI, Thompson SR (December 2009). "RPS25 is essential for translation initiation by the Dicistroviridae and hepatitis C viral IRESs". Genes & Development. 23 (23): 2753–64. doi:10.1101/gad.1832209. PMC 2788332. PMID 19952110.
11. Hertz MI, Landry DM, Willis AE, Luo G, Thompson SR (March 2013). "Ribosomal protein S25 dependency reveals a common mechanism for diverse internal ribosome entry sites and ribosome shunting". Molecular and Cellular Biology. 33 (5): 1016–26. doi:10.1128/MCB.00879-12. PMC 3623076. PMID 23275440.

Further reading

• Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochemistry and Cell Biology. 73 (11–12): 933–47. doi:10.1139/o95-101. PMID 8722009.
• Li M, Center MS (February 1992). "Regulation of ribosomal protein S25 in HL60 cells isolated for resistance to adriamycin". FEBS Letters. 298 (2–3): 142–4. doi:10.1016/0014-5793(92)80041-E. PMID 1544436.
• Marion MJ, Marion C (May 1988). "Ribosomal proteins S2, S6, S10, S14, S15 and S25 are localized on the surface of mammalian 40 S subunits and stabilize their conformation. A study with immobilized trypsin". FEBS Letters. 232 (2): 281–5. doi:10.1016/0014-5793(88)80753-1. PMID 3378620.
• Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N, et al. (December 1994). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.
• Imai T, Sudo K, Miwa T (March 1994). "Assignment of the human ribosomal protein S25 gene (RPS25) to chromosome 11q23.3 by sequence analysis of the marker D11S456". Genomics. 20 (1): 142–3. doi:10.1006/geno.1994.1145. PMID 8020948.
• Miwa T, Sudo K, Nakamura Y, Imai T (July 1993). "Fifty sequenced-tagged sites on human chromosome 11". Genomics. 17 (1): 211–4. doi:10.1006/geno.1993.1304. PMID 8406452.
• Vladimirov SN, Ivanov AV, Karpova GG, Musolyamov AK, Egorov TA, Thiede B, et al. (July 1996). "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry". European Journal of Biochemistry. 239 (1): 144–9. doi:10.1111/j.1432-1033.1996.0144u.x. PMID 8706699.
• Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, et al. (May 1998). "A map of 75 human ribosomal protein genes". Genome Research. 8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID 9582194.
• Kubota S, Copeland TD, Pomerantz RJ (February 1999). "Nuclear and nucleolar targeting of human ribosomal protein S25: common features shared with HIV-1 regulatory proteins". Oncogene. 18 (7): 1503–14. doi:10.1038/sj.onc.1202429. PMID 10050887.
• Ajuh P, Kuster B, Panov K, Zomerdijk JC, Mann M, Lamond AI (December 2000). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". The EMBO Journal. 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. PMC 305846. PMID 11101529.
• Yoshihama M, Uechi T, Asakawa S, Kawasaki K, Kato S, Higa S, et al. (March 2002). "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes". Genome Research. 12 (3): 379–90. doi:10.1101/gr.214202. PMC 155282. PMID 11875025.
• Lehner B, Sanderson CM (July 2004). "A protein interaction framework for human mRNA degradation". Genome Research. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
• Yu Y, Ji H, Doudna JA, Leary JA (June 2005). "Mass spectrometric analysis of the human 40S ribosomal subunit: native and HCV IRES-bound complexes". Protein Science. 14 (6): 1438–46. doi:10.1110/ps.041293005. PMC 2253395. PMID 15883184.
• Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, et al. (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070.