40S ribosomal protein S25

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; OMA:RPS25 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) [1] Band 11q23.3 Start 119,015,712 bp [1] End 119,018,691 bp [1]
Gene location (Mouse) Chr. Chromosome 9 (mouse) [2] Band 9|9 A5.2 Start 44,318,436 bp [2] End 44,321,724 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left ovary right ovary Achilles tendon pituitary gland anterior pituitary right uterine tube gastric mucosa thyroid gland left lobe of thyroid gland right lobe of thyroid gland Top expressed in morula embryo blastocyst embryo ventricular zone yolk sac lip genital tubercle tail of embryo granulocyte More reference expression data BioGPS n/a
Gene ontology Molecular function protein binding RNA binding structural constituent of ribosome Cellular component cytosol ribosome cytosolic small ribosomal subunit nucleolus small ribosomal subunit extracellular exosome nucleus nucleoplasm extracellular matrix 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 ENSG00000118181 ENSMUSG00000009927 UniProt P62851 P62852 RefSeq (mRNA) NM_001028 NM_024266 RefSeq (protein) NP_001019 NP_077228 Location (UCSC) Chr 11: 119.02 – 119.02 Mb Chr 9: 44.32 – 44.32 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

40S ribosomal protein S25 (eS25) is a protein that in humans is encoded by the RPS25 gene. ^{[5] [6]}

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. ^[6]

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. ^[7] Additionally, eS25 has been shown to interact with CDC5L. ^[8]

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. ^{[9] [10]} Studies have implicated eS25 in the control of several specialized forms of translation, including that mediated by viral IRESs. ^{[11] [12]}

See also

• Eukaryotic translation
• 40S ribosomal subunit
• IRES

References

1. GRCh38: Ensembl release 89: ENSG00000118181 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000009927 – 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. 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.
6. "Entrez Gene: RPS25 ribosomal protein S25".
7. 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.
8. 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.
9. 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.
10. 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.
11. 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.
12. 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. Bibcode:1992FEBSL.298..142L. doi: 10.1016/0014-5793(92)80041-E . PMID   1544436. S2CID   9001148.
• 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. Bibcode:1988FEBSL.232..281M. doi: 10.1016/0014-5793(88)80753-1 . PMID   3378620. S2CID   44333810.
• 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. S2CID   25682899.
• 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. S2CID   8235923.