RPL22 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Aliases | RPL22 , EAP, HBP15, HBP15/L22, L22, ribosomal protein L22 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 180474 MGI: 99262 HomoloGene: 37378 GeneCards: RPL22 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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60S ribosomal protein L22 is a protein that in humans is encoded by the RPL22 gene on Chromosome 1. [5] [6]
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 RNA (EBER) 1. 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. [6]
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. [7] 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. [8]
60S ribosomal protein L10 is a protein that in humans is encoded by the RPL10 gene.
60S ribosomal protein L4 is a protein that in humans is encoded by the RPL4 gene.
60S ribosomal protein L31 is a protein that in humans is encoded by the RPL31 gene.
60S ribosomal protein L28 is a protein that in humans is encoded by the RPL28 gene.
60S ribosomal protein L10a is a protein that in humans is encoded by the RPL10A gene.
40S ribosomal protein S24 is a protein that in humans is encoded by the RPS24 gene.
60S ribosomal protein L23 is a protein that in humans is encoded by the RPL23 gene.
60S ribosomal protein L13a is a protein that in humans is encoded by the RPL13A gene.
60S ribosomal protein L19 is a protein that in humans is encoded by the RPL19 gene.
40S ribosomal protein S8 is a protein that in humans is encoded by the RPS8 gene.
60S ribosomal protein L34 is a protein that in humans is encoded by the RPL34 gene.
40S ribosomal protein S12 is a protein that in humans is encoded by the RPS12 gene.
Large ribosomal subunit protein uL22 is a protein that in humans is encoded by the RPL17 gene.
60S ribosomal protein L30 is a protein that in humans is encoded by the RPL30 gene.
60S ribosomal protein L26 is a protein that in humans is encoded by the RPL26 gene.
60S ribosomal protein L37 is a protein that in humans is encoded by the RPL37 gene.
60S ribosomal protein L27a is a protein that in humans is encoded by the RPL27A gene.
60S ribosomal protein L39 is a protein that in humans is encoded by the RPL39 gene.
The Epstein–Barr virus–encoded small RNAs (EBERs) are small non-coding RNAs localized in the nucleus of human cells infected with Epstein–Barr virus (EBV). First discovered in 1981, EBERs are the most abundant RNAs present in infected cells. EBERs interact with several host proteins to form ribonucleoprotein (RNP) complexes. Although a precise function for EBERs remains elusive, roles in transformation and oncogenesis are proposed. They have also been shown to be present in exosomes released from infected cells and could be involved in cell to cell interaction.
Ribosomal protein L22 like 1 (RPL22L1), or eL22L1, is a protein that in humans is encoded by the RPL22L1 gene.