Selenocysteine-specific elongation factor (EEFSEC)
The protein contains 596 amino acids for an estimated molecular weight of 65305 Da.
Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP. (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.
- 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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| Variant | Description |
|---|---|
| dbSNP:rs34326479 |
The reference OMIM entry for this protein is 607695
Eukaryotic elongation factor, selenocysteine-trna-specific; eefsec
Selenoprotein translation factor selb; selb
Efsec
CLONING
Decoding of UGA selenocysteine (sec) codons in eubacteria is mediated by the specialized elongation factor SelB, which conveys the charged tRNA(sec) to the A site of the ribosome, through binding to the sec insertion sequence (SECIS) mRNA hairpin. By searching an EST database for SelB homologs, followed by 5-prime RACE and screening a HeLa cell cDNA library, Fagegaltier et al. (2000) obtained a partial human cDNA encoding SELB. Using the partial human sequence for further EST database searching, they identified a full-length cDNA encoding mouse SelB. The deduced 583-amino acid mouse SelB protein and the partial 526-amino acid human SELB protein share 88% amino acid identity.GENE FUNCTION
Fagegaltier et al. (2000) determined that the putative mouse SelB protein binds GTP, recognizes sec-tRNA(sec) in vitro and in vivo, and is required for efficient selenoprotein translation in vivo. In contrast to the eubacterial SelB, recombinant mouse SelB alone was unable to bind specifically the eukaryotic SECIS RNA hairpin. However, complementation with HeLa cell extracts led to the formation of a SECIS-dependent complex containing mouse SelB and at least another factor. Fagegaltier et al. (2000) concluded that the role carried out by a single elongation factor in eubacterial selenoprotein translation is devoted to 2 or more specialized proteins in eukaryotes. Zavacki et al. (2003) stated that eukaryotes employ 2 distinct factors for decoding UGA sec codons. The first, SECIS-binding protein-2 (SBP2; 607693), binds the SECIS element in the 3-prime untranslated region of the mRNA and recruits the second protein, SELB. Using coprecipitation studies, they identified the C-terminal 64 amino acids of mouse SelB as sufficient for interaction with mouse Sbp2. Selenocysteyl-tRNA was required for this interaction; the 2 factors did not coprecipitate in its absence. Selenocysteyl-tRNA stabilized the C-terminal domain of SelB. Zavacki et al. (2003) concluded that the coupling effect is critical to preventing nonproductive decoding attempts and hence forms a basis for effective selenoprotein synthesis. ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 607695 was added.