40S ribosomal protein S14 (RPS14)
The protein contains 151 amino acids for an estimated molecular weight of 16273 Da.
No function (updated: April 1, 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
Cellular protein metabolic process
Cytoplasmic translation
Erythrocyte differentiation
Gene expression
Maturation of SSU-rRNA
Maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
Negative regulation of transcription by RNA polymerase II
Nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
Regulation of translation
Ribosomal small subunit assembly
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 130620
Ribosomal protein s14; rps14
Emetine resistance gene; emtb
CLONING
The mammalian ribosome consists of 4 RNA species (see 180450) and approximately 80 different proteins. The ribosomal proteins are encoded by complex gene families that include at least 1 active intron-containing gene and multiple processed pseudogenes. Dana and Wasmuth (1982) isolated interspecific hybrids between normal human leukocytes and a Chinese hamster ovary (CHO) cell line that had a mutation in the EMTB locus, leading to alteration of the 40S ribosomal protein S14 and, as a result, resistance to the protein synthesis inhibitor emetine. The cell line was also chromate-resistant due to a mutation in the CHR gene (118840) and temperature-sensitive because of a mutation in the leucyl-tRNA synthetase gene (LEUS; 151350). All 3 mutations were recessive in CHO cells. Therefore, human-CHO cell hybrids were emetine-sensitive, chromate-sensitive, and temperature-resistant. By screening cDNAs derived from HeLa cell 10S to 12S mRNAs with a CHO Rps14 cDNA, Rhoads et al. (1986) isolated cDNAs encoding human RPS14. The deduced 151-amino acid human RPS14 protein is identical to CHO Rps14. The authors isolated human RPS14 genomic clones using human and CHO RPS14 cDNAs. Chen et al. (1986) reported that the RPS14 gene appears to have been stringently conserved during evolution. They found high similarity between the C termini of mammalian RPS14 and yeast ribosomal protein 59; this region includes nucleotides that are mutated in emetine-resistant CHO cells (Rhoads and Roufa, 1985).GENE STRUCTURE
Rhoads et al. (1986) determined that the human RPS14 gene contains 5 exons and spans 5.9 kb.MAPPING
All 3 genes related to emetine resistance isolated by Dana and Wasmuth (1982) appeared to be linked to the long arm of chromosome 2 in the Chinese hamster. Dana and Wasmuth (1982) showed that the genes for these 3 characteristics are carried by human chromosome 5. The results showed that synteny of the 3 genes has been long maintained in evolution. The EMTB locus, 1 of 3 genes that can be altered to give rise to the emetine-resistance phenotype, encodes ribosomal protein S14 (Madjar et al., 1982, Dana et al., 1985). Dana and Wasmuth (1982) subjected Chinese hamster-human interspecific hybrid cells, which contained human chromosome 5 and expressed the 4 syntenic genes LEUS, HEXB (606873), EMTB, and CHR, to selective conditions requiring them to retain the LEUS gene but lose either the EMTB or CHR gene. Using cytogenetic and biochemical analyses of spontaneous segregants, which arose primarily by terminal deletions of various portions of 5q, Dana and Wasmuth (1982) concluded that the order and specific locations of the linked genes are: LEUS, 5pter-5q1; HEXB, 5q13; EMTB, 5q23-5q35; and CHR, 5q35. Other ribosomal protein genes were mapped to chromosomes 8 and 17 by Nakamichi et al. (1986), using cDNA probes and hamster-human hybrid cells. The region of chromosome 8 carrying ribosomal protein genes was 8pter-q21.1. The ribosomal protein genes on chromosome 17 were on the long arm. Nakamichi et al. (1986) placed the RPS14 gene on the segment 5q23-q33. Rhoads et al. (1986) mapped a DNA fragment derived from an intron of the RPS14 gene to 5q23-q33 using somatic cell hybrid DNAs, indicating that the functional RPS14 gene is located at this locus. Kenmochi et al. (1998) confirmed the mapping assignment reported by Rhoads et al. (1986).MOLECULAR GENETICS
- Somatic RPS14 Haploinsufficiency Causes 5q Deletion Syndro ... 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 130620 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed