60S ribosomal protein L22

RPL22
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4UG0, 4V6X, 5AJ0, 4UJD, 4D67, 4D5Y, 4UJE, 4UJC
Identifiers
Aliases	RPL22, EAP, HBP15, HBP15/L22, L22, ribosomal protein L22
External IDs	OMIM: 180474; MGI: 99262; HomoloGene: 37378; GeneCards: RPL22; OMA:RPL22 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1p36.31 Start 6,185,020 bp End 6,209,389 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4|4 E2 Start 152,410,199 bp End 152,418,528 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon ganglionic eminence left ovary monocyte ventricular zone right ovary canal of the cervix body of uterus skin of abdomen granulocyte Top expressed in transitional epithelium of urinary bladder medial ganglionic eminence dermis endothelial cell of lymphatic vessel efferent ductule endocardial cushion maxillary prominence mandibular prominence migratory enteric neural crest cell skin of abdomen More reference expression data BioGPS More reference expression data
Gene ontology Molecular function heparin binding protein binding structural constituent of ribosome RNA binding translation regulator activity Cellular component cytoplasm cytosol ribosome focal adhesion intracellular anatomical structure cytosolic large ribosomal subunit extracellular exosome nucleus extracellular matrix ribonucleoprotein complex presynapse glutamatergic synapse Biological process cytoplasmic translation protein biosynthesis viral transcription SRP-dependent cotranslational protein targeting to membrane translational initiation nuclear-transcribed mRNA catabolic process, nonsense-mediated decay rRNA processing alpha-beta T cell differentiation regulation of translation at presynapse, modulating synaptic transmission Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6146 19934 Ensembl ENSG00000116251 ENSMUSG00000028936 UniProt P35268 P67984 RefSeq (mRNA) NM_000983 NM_001277113 NM_001277114 NM_009079 RefSeq (protein) NP_000974 NP_001264042 NP_001264043 NP_033105 Location (UCSC) Chr 1: 6.19 – 6.21 Mb Chr 4: 152.41 – 152.42 Mb PubMed search
Wikidata
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60S ribosomal protein L22 is a protein that in humans is encoded by the RPL22 gene on Chromosome 1.

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 cytoplasmic ribosomal protein that is a component of the 60S subunit. The protein belongs to the L22E family of ribosomal proteins. Its initiating methionine residue is post-translationally removed. The protein can bind specifically to Epstein–Barr virus-encoded small RNAs (EBERs) 1 and 2. The mouse protein has been shown to be capable of binding to heparin. Transcript variants utilizing alternative polyA signals exist. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. It was previously thought that this gene mapped to 3q26 and that it was fused to the acute myeloid leukemia 1 (AML1) gene located at 21q22 in some therapy-related myelodysplastic syndrome patients with 3;21 translocations; however, these fusions actually involve a ribosomal protein L22 pseudogene located at 3q26, and this gene actually maps to 1p36.3-p36.2.

Insects

The gene may play a role in Insect toxicity resistance. In culex mosquitos, it was one of several ribosomal proteins which were overexpressed in strains resistant to the insecticide deltamethrin. More focused analysis revealed that resistant mosquitoes expressed RPL22 at a level more than 2.5x higher than susceptible strains; however, the same study found that over-expression of RPL22 in transfected cells caused a down-regulation of a different deltamethrin-resistance gene (CYP6A1) and made these cells overall less resistant to the insecticide.

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.
• Toczyski DP, Steitz JA (February 1991). "EAP, a highly conserved cellular protein associated with Epstein-Barr virus small RNAs (EBERs)". The EMBO Journal. 10 (2): 459–66. doi:10.1002/j.1460-2075.1991.tb07968.x. PMC 452667. PMID 1846807.
• Fujita Y, Okamoto T, Noshiro M, McKeehan WL, Crabb JW, Whitney RG, Kato Y, Sato JD, Takada K (March 1994). "A novel heparin-binding protein, HBp15, is identified as mammalian ribosomal protein L22". Biochemical and Biophysical Research Communications. 199 (2): 706–13. doi:10.1006/bbrc.1994.1286. PMID 8135813.
• Sanger Centre, The; Washington University Genome Sequencing Cente, The (November 1998). "Toward a complete human genome sequence". Genome Research. 8 (11): 1097–108. doi:10.1101/gr.8.11.1097. PMID 9847074.
• Le S, Sternglanz R, Greider CW (March 2000). "Identification of two RNA-binding proteins associated with human telomerase RNA". Molecular Biology of the Cell. 11 (3): 999–1010. doi:10.1091/mbc.11.3.999. PMC 14826. PMID 10712515.
• Shu-Nu C, Lin CH, Lin A (October 2000). "An acidic amino acid cluster regulates the nucleolar localization and ribosome assembly of human ribosomal protein L22". FEBS Letters. 484 (1): 22–8. doi:10.1016/S0014-5793(00)02118-9. PMID 11056215.
• Uechi T, Tanaka T, Kenmochi N (March 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 (January 2002). "Directed proteomic analysis of the human nucleolus". Current Biology. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
• Yoshihama M, Uechi T, Asakawa S, Kawasaki K, Kato S, Higa S, Maeda N, Minoshima S, Tanaka T, Shimizu N, Kenmochi N (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.
• Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (January 2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
• Chen KC, Chiang HS, Fang CL (2005). "EBER expression of pure urinary bladder lymphoepithelioma-like carcinoma in two unique Asian patients". Urologia Internationalis. 74 (3): 280–2. doi:10.1159/000083565. PMID 15812220.
• Fok V, Mitton-Fry RM, Grech A, Steitz JA (May 2006). "Multiple domains of EBER 1, an Epstein-Barr virus noncoding RNA, recruit human ribosomal protein L22". RNA. 12 (5): 872–82. doi:10.1261/rna.2339606. PMC 1440895. PMID 16556938.
• Nakao K, Mochiki M, Nibu K, Sugasawa M, Uozaki H (April 2006). "Analysis of prognostic factors of nasopharyngeal carcinoma: impact of in situ hybridization for Epstein-Barr virus encoded small RNA 1". Otolaryngology–Head and Neck Surgery. 134 (4): 639–45. doi:10.1016/j.otohns.2005.11.022. PMID 16564389.

External links

• Overview of all the structural information available in the PDB for UniProt: P35268 (60S ribosomal protein L22) at the PDBe-KB.