RPL23A

Ribosomal protein L23a
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 4V6X​, 5AJ0​
Identifiers
Symbols	RPL23A ; L23A; MDA20
External IDs	OMIM: 602326 MGI: 3040672 HomoloGene: 133569 GeneCards: RPL23A Gene
Gene ontology Molecular function • nucleotide binding • structural constituent of ribosome • protein binding • rRNA binding • poly(A) RNA binding Cellular component • nucleus • nucleolus • cytoplasm • cytosol • cytosolic large ribosomal subunit • TORC2 complex • extracellular exosome Biological process • ribosomal large subunit assembly • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay • translation • translational initiation • translational elongation • translational termination • SRP-dependent cotranslational protein targeting to membrane • cell proliferation • gene expression • viral process • viral life cycle • viral transcription • cellular protein metabolic process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6147	268449
Ensembl	ENSG00000198242	ENSMUSG00000058546
UniProt	P62750	P62751
RefSeq (mRNA)	NM_000984	NM_207523
RefSeq (protein)	NP_000975	NP_997406
Location (UCSC)	Chr 17: 28.72 – 28.72 Mb	Chr 11: 78.18 – 78.18 Mb
PubMed search

60S ribosomal protein L23a is a protein that in humans is encoded by the RPL23A gene.^[1][2]

Function

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 60S subunit. The protein belongs to the L23P family of ribosomal proteins. It is located in the cytoplasm. The protein may be one of the target molecules involved in mediating growth inhibition by interferon. In yeast, the corresponding protein binds to a specific site on the 26S rRNA. This gene is co-transcribed with the U42A, U42B, U101A, and U101B small nucleolar RNA genes, which are located in its third, first, second, and fourth introns, respectively. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.^[2]

Clinical significance

L23a has been identified as an autoimmune target that causes a form of rheumatoid arthritis in mice and which also causes a reaction from T cells and autoantibodies from human rheumatoid arthritis patients.^[3]

References

1. Fan W, Christensen M, Eichler E, Zhang X, Lennon G (Feb 1998). "Cloning, sequencing, gene organization, and localization of the human ribosomal protein RPL23A gene". Genomics 46 (2): 234–9. doi:10.1006/geno.1997.5038. PMID 9417910.
2. "Entrez Gene: RPL23A ribosomal protein L23a".
3. Ito Y, Hashimoto M, Hirota K, Ohkura N, Morikawa H, Nishikawa H, Tanaka A, Furu M, Ito H, Fujii T, Nomura T, Yamazaki S, Morita A, Vignali DA, Kappler JW, Matsuda S, Mimori T, Sakaguchi N, Sakaguchi S (2014). "Detection of T cell responses to a ubiquitous cellular protein in autoimmune disease". Science 346 (6207): 363–8. doi:10.1126/science.1259077. PMID 25324392.

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.
• Fan W, Cai W, Parimoo S, Schwarz DC, Lennon GG, Weissman SM (1996). "Identification of seven new human MHC class I region genes around the HLA-F locus.". Immunogenetics 44 (2): 97–103. doi:10.1007/BF02660056. PMID 8662070.
• Jiang H, Lin JJ, Tao J, Fisher PB (1997). "Suppression of human ribosomal protein L23A expression during cell growth inhibition by interferon-beta.". Oncogene 14 (4): 473–80. doi:10.1038/sj.onc.1200858. PMID 9053844.
• Jäkel S, Görlich D (1998). "Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells.". EMBO J. 17 (15): 4491–502. doi:10.1093/emboj/17.15.4491. PMC 1170780. PMID 9687515.
• Rogan S, Heaphy S (2001). "The vaccinia virus E3L protein interacts with SUMO-1 and ribosomal protein L23a in a yeast two hybrid assay.". Virus Genes 21 (3): 193–5. doi:10.1023/A:1008139514123. PMID 11129635.
• Uechi T, Tanaka T, Kenmochi N (2001). "A complete map of the human ribosomal protein genes: assignment of 80 genes to the cytogenetic map and implications for human disorders.". Genomics 72 (3): 223–30. doi:10.1006/geno.2000.6470. PMID 11401437.
• Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (2002). "Directed proteomic analysis of the human nucleolus.". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
• Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions.". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.