Elongation factor 1-gamma (EEF1G)
The protein contains 437 amino acids for an estimated molecular weight of 50119 Da.
Probably plays a role in anchoring the complex to other cellular components. (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.
- 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.
- 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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The reference OMIM entry for this protein is 130593
Eukaryotic translation elongation factor 1, gamma; eef1g
Elongation factor 1, gamma; ef1g
Eef1b-gamma
DESCRIPTION
Eukaryotic elongation factor-1 (EF1) consists of 4 subunits, EF1-alpha (EEF1A1; 130590), EF1-beta (EEF1B2; 600655), EF1-gamma, and EF1-delta (EEF1D; 130592). EIF-alpha-GTP transfers aminoacyl-tRNA to the ribosome, and the release of animoacyl-tRNA from EIF-alpha-GTP is driven by GTP hydrolysis. EF1-alpha-GDP is recycled to EF1-alpha-GTP by the EF1-beta, -gamma, and -delta subunits (Sanders et al., 1996).CLONING
Using RT-PCR with degenerate oligonucleotides based on 2 peptides conserved between Artemia and Xenopus EF1-gamma, Sanders et al. (1992) isolated a human fibroblast cDNA encoding EEF1G. The predicted 437-amino acid human protein is 60% and 85% similar to the Artemia and Xenopus proteins, respectively. Using computer methods for protein sequence analyses, Koonin et al. (1994) found that EEF1G contains an N-terminal domain related to the theta class of glutathione S-transferases (GSTs; e.g., 600436). They proposed that the GST domain in EEF1G is involved in regulating the assembly of multisubunit complexes containing EEF1G and aminoacyl-tRNA synthetases. By immunofluorescence analysis, Sanders et al. (1996) found that EF1-beta, -gamma, and -delta showed a perinuclear distribution and colocalized with an endoplasmic reticulum resident protein in human foreskin fibroblasts. In contrast, EF1-alpha showed strong nuclear staining and diffuse cytoplasmic staining.GENE FUNCTION
Using Northern blot analysis, Sanders et al. (1992) found that expression of the Eef1g, Eef1b2, and Ef1a genes was 20-fold higher in cultured rat cells than in rat tissues. However, oncogenic transformation of human and rat cells did not have a major effect on EF1 mRNA levels. Sanders et al. (1992) suggested that the levels of the EF1 mRNAs rise as a result of a loss of contact inhibition, leading to the increases seen in tumors and cultured cells. Lew et al. (1992) found that EEF1G mRNA was expressed at higher levels in 7 of 9 pancreatic tumors than in the corresponding normal tissues. ... 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
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 130593 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed