40S ribosomal protein S24 (RPS24)
The protein contains 133 amino acids for an estimated molecular weight of 15423 Da.
Required for processing of pre-rRNA and maturation of 40S ribosomal subunits. (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.
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.
(right-click above to access to more options from the contextual menu)
Biological Process
Cellular protein metabolic process
Cytoplasmic translation
Erythrocyte homeostasis
Gene expression
Maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
Nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
Ribosomal small subunit biogenesis
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 602412
Ribosomal protein s24; rps24
DESCRIPTION
The RPS24 gene encodes a protein involved in ribosomal RNA biogenesis (summary by Choesmel et al., 2008).CLONING
Eukaryotic ribosomes are composed of 4 RNA species (see 180450) and at least 80 proteins. Brown et al. (1990) isolated a human ribosomal protein gene encoding a predicted 133-amino acid protein by probing a fibrosarcoma cDNA library with a ribosomal protein gene from Chinese hamster. By comparing the in vitro translation product with S24 from purified ribosomes on 2-dimensional gels, Brown et al. (1990) showed that the gene encodes the 40S ribosomal subunit protein S24 (RPS24).GENE STRUCTURE
Xu and Roufa (1996) reported that RPS24 is organized into 6 exons and is differentially spliced to yield 2 isoforms, S24a and S24c, that are present in varying ratios in different tissues.MAPPING
Jones et al. (1997) used PCR of radiation and somatic cell hybrid panels to map the RPS24 gene to 10q22-q23. Kenmochi et al. (1998) confirmed the RPS24 mapping assignment reported by Jones et al. (1997).GENE FUNCTION
Choesmel et al. (2008) demonstrated that RPS24 is required for the pre-rRNA processing at the 5-prime external transcribed spacer (ETS) of the 45S rRNA precursor molecule.BIOCHEMICAL FEATURES
- Crystal Structure Choesmel et al. (2008) determined the crystal structure of the P. abyssi RPS24e protein, which is homologous to human RPS24. The protein is built around a 4-stranded anti-parallel beta-sheet surrounded by 3 short alpha-helices. It shows homology to the prokaryotic ribosomal protein L23, which is a component of the large ribosomal subunit.MOLECULAR GENETICS
Diamond-Blackfan anemia (DBA) is a rare congenital red cell aplasia characterized by anemia, bone marrow erythroblastopenia, and congenital anomalies. In approximately 25% of probands, heterozygous mutations in the ribosomal protein S19 gene (RPS19; 603474) have been found; see DBA1 (105650). Gazda et al. (2006) reported identification of de novo nonsense and splice site mutations in another ribosomal protein, RPS24 (602412.0001-602412.0003), in approximately 2% of RPS19 mutation-negative probands with Diamond-Blackfan anemia (DBA3; 610629). This finding strongly suggested that DBA is a disorder of ribosome synthesis and that mutations in other ribosomal proteins or associated genes that lead to disrupted ribosomal biogenesis and/or function may also cause DBA. Choesmel et al. (2008) found that lymphoblastoid cells derived from DBA3 patients with RPS24 mutations (602412.0001-612412.0003) had altered pre-rRNA processing, with lower levels of 41S pre-rRNA and accumulation of the 30S species, resulting in a lower 41S/30S ratio compared to controls. There was also less 21S and 18S-E pre-rRNA compared to controls, but the 21S/18S-E ratio was similar to controls. HeLa cells with siRNA against RPS24 showed a loss of free 40S ribosomal subunits and an accumulation of 60S subunits, indicating that RPS24 is essential for the production of the small ribosomal subunit 40S. Pulse-chase labeling and Northern blot studies of siRNA-knockdown cells showed lack of formation of 41S, 21S, and 18S-E pre-rRNA, although 28S was normal and 30S was increased. These findings suggested inhibition of cleavage at the 5-prime external transcribed spacer (ETS), as well as blocking of the subsequent processing of internal spacer-1 (ITS1) at the 3-prime end of the 18S rRNA. The pattern of the 60S rRNA subunit was ... 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 602412 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed