Elongation factor 1-delta (EEF1D)
The protein contains 281 amino acids for an estimated molecular weight of 31122 Da.
EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome.', 'Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE). (updated: Dec. 11, 2019)
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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Biological Process
Cellular protein metabolic process
Cellular response to ionizing radiation
Gene expression
MRNA transcription
Positive regulation of I-kappaB kinase/NF-kappaB signaling
Regulation of cell death
Regulation of transcription, DNA-templated
Signal transduction
Transcription, DNA-templated
Translation
Translational elongation
The reference OMIM entry for this protein is 130592
Eukaryotic translation elongation factor 1, delta; eef1d
Elongation factor 1, delta; ef1d
Guanine nucleotide exchange protein
DESCRIPTION
Eukaryotic elongation factor-1 (EF1) consists of 4 subunits, EF1-alpha (EEF1A1; 130590), EF1-beta (EEF1B2; 600655), EF1-gamma (EEF1G; 130593), and EF1-delta. 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 Xenopus Ef1-delta to probe a human skin fibroblast cDNA library, Sanders et al. (1993) cloned EF1-delta. The deduced 281-amino acid protein has a calculated molecular mass of 31 kD. It has an N-terminal leucine zipper domain and a C-terminal domain that is similar to that of EF1-beta and is predicted to show GDP/GTP exchange activity. EF1-delta also has a conserved serine phosphorylation site. SDS-PAGE detected EF1-delta at an apparent molecular mass of 38 kD. By Western blot analysis, Sanders et al. (1996) detected 1 major and 2 minor EF1-delta bands, which they attributed to variable degrees of phosphorylation. Immunofluorescence analysis detected EF1-beta, -gamma, and -delta in a perinuclear distribution in human foreskin fibroblasts, and these subunits colocalized with an endoplasmic reticulum (ER) resident protein. In contrast, EF1-alpha showed strong nuclear staining and diffuse cytoplasmic staining.GENE FUNCTION
Human immunodeficiency virus-1 (HIV-1) Tat protein has an N-terminal domain that is a potent activator of transcription from the viral long terminal repeat promoter. Tat is also essential for viral replication and can activate or repress transcription of host cell genes. Using Tat as bait in a yeast 2-hybrid screen of a HeLa cell cDNA library, Xiao et al. (1998) isolated EF1-delta. Protein pull-down and Western blot analyses confirmed direct interaction between Tat and EF1-delta. EF1-delta specifically interacted with the Tat C-terminal domain. Titration of purified recombinant Tat into in vitro translation reactions showed that Tat inhibited translation of cellular, but not viral, proteins. Xiao et al. (1998) hypothesized that by binding EF1-delta, Tat redirects the protein synthesis machinery toward producing large amounts of viral proteins. Using yeast 2-hybrid analysis, Ong et al. (2003) found that kinectin (KTN1; 600381) interacted directly with EF1-delta. Using peptide fragments, Ong et al. (2003) showed that a 60-amino acid domain near the kinectin C terminus was required for EF1-delta binding. Endogenous kinectin colocalized with EF1-delta in the ER. Expression of the kinectin EF1-delta-binding domain disrupted EF1-delta localization, suggesting that kinectin anchors EF1-delta to the ER membrane. Ong et al. (2003) also showed that CDC2 (116940) phosphorylated HeLa cell EF1-delta in vitro. ... More on the omim web site
Jan. 22, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
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 130592 was added.