40S ribosomal protein S30 (FAU)
The protein contains 59 amino acids for an estimated molecular weight of 6648 Da.
No function (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
- 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.
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| Variant | Description |
|---|---|
| empty |
No binding partner found
Biological Process
Antibacterial humoral response
Antimicrobial humoral immune response mediated by antimicrobial peptide
Cytoplasmic translation
Defense response to Gram-positive bacterium
Innate immune response in mucosa
Nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
SRP-dependent cotranslational protein targeting to membrane
Translation
Translational initiation
Viral transcription
The reference OMIM entry for this protein is 134690
Fau gene; fau
Fbr-musv associated ubiquitously expressed gene
DESCRIPTION
The FAU gene is the cellular homolog of the fox sequence in the Finkel-Biskis-Reilly murine sarcoma virus (FBR-MuSV) (summary by Kas et al., 1992).CLONING
Kas et al. (1992) cloned and sequenced the human FAU gene. Its name is derived from 'FBR-MuSV associated ubiquitously expressed gene.' FAU encodes a fusion protein consisting of 133 amino acids. The 59 amino acids at the carboxy terminus encode the ribosomal protein S30, part of the small ribosomal subunit. The amino-terminal part of FAU (74 amino acids) shows strong homology to ubiquitin, a 76-amino acid multifunctional cellular protein.MAPPING
Kas et al. (1993) used a cosmid clone containing the human FAU gene for fluorescence in situ hybridization to localize the gene to 11q13. The localization was confirmed by hybridization against a panel of somatic cell hybrids containing different parts of chromosome 11 on a hamster background. FAU was then further mapped, both on a panel of radiation-reduced somatic cell hybrids designed to carry different parts of the 11q13 region and by pulsed field gel electrophoresis. This fine mapping placed FAU close to the PYGM gene (608455) in a region that contains oncogenes as well as the putative tumor suppressor genes MEN1 (613733) and ST3 (191181). By linkage mapping, Casteels et al. (1995) assigned the Fau gene to mouse chromosome 19. Courseaux et al. (1996) used a combination of methods to refine maps of the approximately 5-Mb region of 11q13 that includes MEN1 (613733). They proposed the following gene order: cen--PGA--FTH1--UGB--AHNAK--ROM1--MDU1--CHRM1--COX8--EMK1--FKBP2--PLCB3--[PYGM, ZFM1]--FAU--CAPN1--[MLK3, RELA]--FOSL1--SEA--CFL1--tel.OTHER FEATURES
Kapranov et al. (2010) demonstrated that human cells contain a novel type of short RNA (sRNA) with a nongenomically encoded 5-prime poly(U) tail. They proposed that the presence of these RNAs at the termini of genes, specifically at the very 3-prime ends of known mRNAs, such as that for FAU, strongly argues for the presence of a yet uncharacterized endogenous biochemical pathway in cells that can copy RNA. Kapranov et al. (2010) showed that this pathway can operate on multiple genes, with specific enrichment toward transcript-encoding components of the translational machinery. They also showed that genes are also flanked by sense, 3-prime polyadenylated sRNAs that are likely to be capped. ... More on the omim web site
Oct. 19, 2018: Protein entry updated
Automatic update: OMIM entry 134690 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).