[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki7\/40s-ribosomal-protein-s10-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki7\/40s-ribosomal-protein-s10-wikipedia\/","headline":"40S ribosomal protein S10 – Wikipedia","name":"40S ribosomal protein S10 – Wikipedia","description":"From Wikipedia, the free encyclopedia Protein-coding gene in the species Homo sapiens 40S ribosomal protein S10 is a protein that","datePublished":"2016-09-16","dateModified":"2016-09-16","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki7\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki7\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","url":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","height":"1","width":"1"},"url":"https:\/\/wiki.edu.vn\/en\/wiki7\/40s-ribosomal-protein-s10-wikipedia\/","wordCount":5283,"articleBody":"From Wikipedia, the free encyclopediaProtein-coding gene in the species Homo sapiens40S ribosomal protein S10 is a protein that in humans is encoded by the RPS10 gene.[5][6][7]Function[edit]Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S10E family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.[7]Clinical significance[edit]Variable expression of this gene in colorectal cancers compared to adjacent normal tissues has been observed, although no correlation between the level of expression and the severity of the disease has been found.[7]Mutations in the RPS10 gene can cause Diamond\u2013Blackfan anemia, a congenital anemia sometimes associated with bone marrow failure.[8]Interactions[edit]RPS10 has been shown to interact with PTTG1.[9]References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000124614 – Ensembl, May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000052146 – Ensembl, May 2017^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ Frigerio JM, Dagorn JC, Iovanna JL (Jul 1995). “Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs”. Biochim Biophys Acta. 1262 (1): 64\u20138. doi:10.1016\/0167-4781(95)00045-i. PMID\u00a07772601.^ 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\u201323. doi:10.1101\/gr.8.5.509. PMID\u00a09582194.^ a b c “Entrez Gene: RPS10 ribosomal protein S10”.^ Doherty, L; Sheen, MR; Vlachos, A; Choesmel, V; O’Donohue, MF; Clinton, C; Schneider, HE; Sieff, CA; Newburger, PE; Ball, SE; Niewiadomska, E; Matysiak, M; Glader, B; Arceci, RJ; Farrar, JE; Atsidaftos, E; Lipton, JM; Gleizes, PE; Gazda (Feb 2010). “Ribosomal protein genes RPS10 and RPS26 are commonly mutated in Diamond\u2013Blackfan anemia. HT”. Am J Hum Genet. 86 (2): 222\u20138. doi:10.1016\/j.ajhg.2009.12.015. PMC\u00a02820177. PMID\u00a020116044.^ Pei, L (Jan 1999). “Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells”. J. Biol. Chem. 274 (5): 3151\u20138. doi:10.1074\/jbc.274.5.3151. ISSN\u00a00021-9258. PMID\u00a09915854.Further reading[edit]Wool IG, Chan YL, Gl\u00fcck A (1996). “Structure and evolution of mammalian ribosomal proteins”. Biochem. Cell Biol. 73 (11\u201312): 933\u201347. doi:10.1139\/o95-101. PMID\u00a08722009.Vladimirov SN, Ivanov AV, Karpova GG,  et\u00a0al. (1996). “Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry”. Eur. J. Biochem. 239 (1): 144\u20139. doi:10.1111\/j.1432-1033.1996.0144u.x. PMID\u00a08706699.Pei L (1999). “Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells”. J. Biol. Chem. 274 (5): 3151\u20138. doi:10.1074\/jbc.274.5.3151. PMID\u00a09915854.Malygin AA, Shaulo DD, Karpova GG (2001). “Proteins S7, S10, S16 and S19 of the human 40S ribosomal subunit are most resistant to dissociation by salt”. Biochim. Biophys. Acta. 1494 (3): 213\u20136. doi:10.1016\/s0167-4781(00)00252-9. PMID\u00a011121577.Bortoluzzi S, d’Alessi F, Romualdi C, Danieli GA (2002). “Differential expression of genes coding for ribosomal proteins in different human tissues”. Bioinformatics. 17 (12): 1152\u20137. doi:10.1093\/bioinformatics\/17.12.1152. PMID\u00a011751223.Strausberg RL, Feingold EA, Grouse LH,  et\u00a0al. (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\u2013903. Bibcode:2002PNAS…9916899M. doi:10.1073\/pnas.242603899. PMC\u00a0139241. PMID\u00a012477932.Malygin A, Baranovskaya O, Ivanov A, Karpova G (2003). “Expression and purification of human ribosomal proteins S3, S5, S10, S19, and S26”. Protein Expr. Purif. 28 (1): 57\u201362. doi:10.1016\/S1046-5928(02)00652-6. PMID\u00a012651107.Ballif BA, Vill\u00e9n J, Beausoleil SA,  et\u00a0al. (2005). “Phosphoproteomic analysis of the developing mouse brain”. Mol. Cell. Proteomics. 3 (11): 1093\u2013101. doi:10.1074\/mcp.M400085-MCP200. PMID\u00a015345747.Gerhard DS, Wagner L, Feingold EA,  et\u00a0al. (2004). “The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121\u20137. doi:10.1101\/gr.2596504. PMC\u00a0528928. PMID\u00a015489334.Rush J, Moritz A, Lee KA,  et\u00a0al. (2005). “Immunoaffinity profiling of tyrosine phosphorylation in cancer cells”. Nat. Biotechnol. 23 (1): 94\u2013101. doi:10.1038\/nbt1046. PMID\u00a015592455. S2CID\u00a07200157.Andersen JS, Lam YW, Leung AK,  et\u00a0al. (2005). “Nucleolar proteome dynamics”. Nature. 433 (7021): 77\u201383. Bibcode:2005Natur.433…77A. doi:10.1038\/nature03207. PMID\u00a015635413. S2CID\u00a04344740.Yu Y, Ji H, Doudna JA, Leary JA (2005). “Mass spectrometric analysis of the human 40S ribosomal subunit: Native and HCV IRES-bound complexes”. Protein Sci. 14 (6): 1438\u201346. doi:10.1110\/ps.041293005. PMC\u00a02253395. PMID\u00a015883184.Stelzl U, Worm U, Lalowski M,  et\u00a0al. (2005). “A human protein-protein interaction network: a resource for annotating the proteome”. Cell. 122 (6): 957\u201368. doi:10.1016\/j.cell.2005.08.029. PMID\u00a016169070.Ewing RM, Chu P, Elisma F,  et\u00a0al. (2007). “Large-scale mapping of human protein\u2013protein interactions by mass spectrometry”. Mol. Syst. Biol. 3 (1): 89. doi:10.1038\/msb4100134. PMC\u00a01847948. PMID\u00a017353931.External links[edit]"},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki7\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki7\/40s-ribosomal-protein-s10-wikipedia\/#breadcrumbitem","name":"40S ribosomal protein S10 – Wikipedia"}}]}]