40S ribosomal protein S20 (RPS20)
The protein contains 119 amino acids for an estimated molecular weight of 13373 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.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- 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.
- 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
Cellular protein metabolic process
Cytoplasmic translation
Gene expression
Nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
Positive regulation of signal transduction by p53 class mediator
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 603682
Ribosomal protein s20; rps20
The mammalian ribosome is composed of 4 RNA species (see 180450) and approximately 80 different proteins. Chu et al. (1993) isolated a human dermal vascular endothelial cell cDNA encoding ribosomal protein S20 (RPS20). The deduced 119-amino acid human RPS20 protein is identical to rat Rps20. Northern blot analysis detected an approximately 650-bp RPS20 transcript. Southern blot analysis showed that the RPS20 gene may be a member of a multigene family. By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi et al. (1998) mapped the human RPS20 gene to 8q.
ANIMAL MODEL
McGowan et al. (2008) reported 2 mouse 'dark skin' loci, Dsk3 and Dsk4, caused by mutations in Rps19 (603474) and Rps20, respectively. These mice have dark paws, tail skin, and ears, with melanocytosis limited to the epidermis. In the model proposed by McGowan et al. (2008), reduced dosage of Rps6 (180460), Rps19, or Rps20 triggers stabilization and/or activation of p53 (191170), which gives rise to a pleiotropic phenotype whose components depend on the sensitivity and response of individual cell types and on specific downstream targets of p53. Stabilization of p53 stimulates Kit ligand (KITLG; 184745) expression and, consequently, epidermal melanocytosis via a paracrine mechanism. Increased apoptosis causes erythrocyte hypoplasia and anemia, and activation of p53 causes reduced growth and decreased body size. McGowan et al. (2008) concluded that their results provide a mechanistic explanation for the diverse collection of phenotypes that accompany reduced dosage of genes encoding ribosomal proteins, and have implications for understanding normal human variation and human disease. ... 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 603682 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed