60S ribosomal protein L22 (RPL22)
The protein contains 128 amino acids for an estimated molecular weight of 14787 Da.
No function (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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Biological Process
Alpha-beta T cell differentiation
Cellular protein metabolic process
Cytoplasmic translation
Gene expression
Nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
Regulation of translation at presynapse, modulating synaptic transmission
RRNA processing
SRP-dependent cotranslational protein targeting to membrane
Translation
Translational elongation
Translational initiation
Translational termination
Viral life cycle
Viral process
Viral transcription
The reference OMIM entry for this protein is 180474
Ribosomal protein l22; rpl22
Epstein-barr associated protein; eap
CLONING
Shu-Nu et al. (2000) reported that the 128-amino acid human RPL22 protein has a 9-amino acid hydrophobic N-terminal domain, followed by a central I domain, which contains KRYLK and KKYLK motifs, and a 9-amino acid C-terminal domain. Epitope-tagged RPL22 localized to the nucleolus of transfected HeLa cells.MAPPING
By PCR of a human-rodent somatic cell hybrid panel, radiation hybrid analysis, and genomic sequence analysis, Uechi et al. (2001) mapped the RPL22 gene to chromosome 1p36.3. They stated that the RPL22 copy reported by Nucifora et al. (1993) and Nucifora and Rowley (1995) on chromosome 3q26 (seeHISTORY
) is a processed pseudogene.GENE FUNCTION
By deletion analysis of RPL22, Shu-Nu et al. (2000) identified a KKKK nuclear localization signal following the N-terminal domain, as well as a KKYLKK nucleolar entry motif in the I domain. Yeast 2-hybrid analysis revealed that the isolated N terminus of RPL22 interacted with the isolated C terminus of RPL22. RPL22 lacking these domains did not target to the nucleolus. Using microarray-based copy number analysis, Rao et al. (2012) found that RPL22 was monoallelically inactivated in approximately 10% of primary human samples of T-cell acute lymphoblastic leukemia (T-ALL; see 613065).ANIMAL MODEL
Rao et al. (2012) reported that Rpl22-null mice were viable, fertile, and grossly normal, but that they had a specific block in the development of alpha-beta lineage T cells. Using transgenic mice expressing constitutively active Akt2 (164731), a mouse model of T-ALL, the authors found that haploinsufficiency of Rpl22 accelerated the development of thymic lymphoma. Rpl22-knockdown mouse embryonic fibroblasts (MEFs) revealed increased expression of the stemness factor Lin28b (611044). Knockdown of Lin28b via short hairpin RNA reduced growth rate and colony formation in RPL22-null MEFs. Inhibition of NF-kappa-B (see RELA, 164014) signaling or knockdown of Rela blocked induction of Lin28b in Rpl22-null MEFs. Since Lin28 is a negative regulator of microRNAs of the Let7 family (see MIRLET7A1, 605386), increased expression of Lin28b was accompanied by reduced expression of Let7, followed by upregulation of the Let7 targets Myc (190080) and Ras (190020). Rao et al. (2012) concluded that haploinsufficiency of RPL22 can cause T-ALL by activating a pathway that requires NF-kappa-B, LIN28, LET7, and MYC/RAS.HISTORY
A reciprocal translocation between the long arms of chromosomes 3 and 21, at bands 3q26 and 21q22, occurs as an acquired clonal chromosomal abnormality in malignant cells from patients with therapy-related myelodysplastic syndrome or acute myeloid leukemia, as well as in some patients with chronic myeloid leukemia in blast crisis. Nucifora et al. (1993) showed that the gene on chromosome 21 is AML1 (151385), which is fused to the ETO gene (133435) in 8;21 translocations. Nucifora et al. (1993) isolated a fusion cDNA clone from a t(3;21) library derived from a patient with therapy-related myelodysplastic syndrome; this clone contained sequences from AML1 and from EAP (RPL22), which they localized to chromosome 3q26 from the location of the breakpoint on chromosome 3. The fusion clone contained the DNA-binding 5-prime part of AML1 that is fused to ETO in the t(8;21) and, in addition, at least 1 other exon. The translocation replaced the last 9 codons of AML1 with the last 96 codons of EAP. The fusion does not maintain the co ... More on the omim web site
May 12, 2019: Protein entry updated
Automatic update: model status changed
Nov. 16, 2018: Protein entry updated
Automatic update: model status changed
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
Oct. 26, 2017: Protein entry updated
Automatic update: model status changed
March 15, 2016: Protein entry updated
Automatic update: OMIM entry 180474 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed