Eukaryotic translation initiation factor 4 gamma 1 (EIF4G1)
The protein contains 1599 amino acids for an estimated molecular weight of 175491 Da.
Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. As a member of the eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). (updated: April 22, 2020)
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.
- 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.
(right-click above to access to more options from the contextual menu)
Biological Process
Behavioral fear response
Cap-dependent translational initiation
Cellular macromolecule biosynthetic process
Cellular protein metabolic process
Cellular response to nutrient levels
Cytokine-mediated signaling pathway
Developmental process
Energy homeostasis
Gene expression
Insulin receptor signaling pathway
Lung development
Mitochondrion organization
Negative regulation of autophagy
Negative regulation of neuron death
Negative regulation of peptidyl-threonine phosphorylation
Nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
Nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
Nuclear-transcribed mRNA poly(A) tail shortening
Positive regulation of cell death
Positive regulation of cell growth
Positive regulation of cell population proliferation
Positive regulation of cellular protein metabolic process
Positive regulation of energy homeostasis
Positive regulation of eukaryotic translation initiation factor 4F complex assembly
Positive regulation of G1/S transition of mitotic cell cycle
Positive regulation of miRNA mediated inhibition of translation
Positive regulation of mRNA cap binding
Positive regulation of neuron differentiation
Positive regulation of peptidyl-serine phosphorylation
Positive regulation of translation in response to endoplasmic reticulum stress
Regulation of cellular response to stress
Regulation of gene silencing by miRNA
Regulation of mRNA stability
Regulation of polysome binding
Regulation of presynapse assembly
Regulation of translational initiation
Response to ethanol
Translation
Translational initiation
Viral process
Cellular Component
Cytoplasm
Cytoplasmic stress granule
Cytosol
Eukaryotic translation initiation factor 4F complex
Membrane
Nucleus
Polysome
Postsynapse
Molecular Function
ATP binding
Cadherin binding
Eukaryotic initiation factor 4E binding
Identical protein binding
Molecular adaptor activity
MRNA binding
Poly(A) RNA binding
Protein-containing complex scaffold activity
RNA binding
Translation factor activity, RNA binding
Translation initiation factor activity
Translation initiation factor binding
The reference OMIM entry for this protein is 600495
Eukaryotic translation initiation factor 4-gamma, 1; eif4g1
Eukaryotic translation initiation factor 4g; eif4g
Eif4-gamma
Eif4gi
DESCRIPTION
All eukaryotic cellular messenger RNAs are posttranscriptionally modified by addition of an m(7)GTP moiety to the 5-prime terminus, referred to as a cap. Recognition of the cap structure and unwinding of mRNA secondary structure during the initiation phase of protein synthesis is catalyzed by initiation factors of the eIF4 group. eIF4E (133440) is a 25-kD cap-binding protein. eIF4A (see 602641) is a 46-kD polypeptide that possesses ATP-dependent RNA helicase activity and RNA-dependent ATPase activity. eIF4B (603928) is a 69-kD RNA-binding protein that enhances the activity of eIF4A. eIF4-gamma, also known as p220, is a 154-kD protein that forms various complexes with the other eIF4 polypeptides. The complex of eIF4A, eIF4E, and eIF4-gamma has been referred to as either eIF4F or eIF4. Collectively, these factors facilitate the recruitment of mRNA to the ribosome, which is the rate-limiting step for protein synthesis under normal conditions. eIF4-gamma is the target for proteolytic cleavage during picornavirus infection, an event that is thought to be responsible for the inhibition of host cellular mRNA translation (Yan and Rhoads, 1995).CLONING
By screening a rabbit brain library with oligonucleotide probes based on the sequence of rabbit eIF4-gamma peptides, Yan et al. (1992) identified partial eIF4-gamma cDNAs. They used the rabbit cDNAs as probes and isolated human brain cDNAs encoding eIF4-gamma. The predicted human protein contains 1,396 amino acids. Western blot analysis of poliovirus-infected HeLa cell extracts revealed that eIF4-gamma has an apparent molecular mass of 200 to 220 kD and is cleaved by this picornavirus. Imataka and Sonenberg (1997) stated that the N-terminal region of eIF4G contains a binding site for eIF4E. They demonstrated that the central third of eIF4G contains an eIF3 (see 602039)-binding region and an eIF4A-binding domain. A second, separate eIF4A-binding site is present in the C-terminal third. Neither eIF4A-binding domain alone activates translation. In contrast to eIF4G, the eIF4G-related translation regulator p97 (602325) binds eIF4A only through its N-terminal domain, which is homologous to the central domain of eIF4G. Gradi et al. (1998) identified a second human eIF4G gene. They designated the original gene eIF4GI and the novel gene eIF4GII (EIF4G3; 603929). Imataka et al. (1998) found that the human eIF4GI protein contains an additional 156 N-terminal amino acids compared to the sequence published by Yan et al. (1992). They demonstrated that this N-terminal region binds poly(A)-binding protein (PABP; 604679).GENE FUNCTION
Imataka et al. (1998) found that, in an in vitro translation system, an N-terminal fragment of eIF4GI that included the PABP-binding site inhibited poly(A)-dependent translation, but had no effect on translation of a deadenylated mRNA. Imataka et al. (1998) concluded that eIF4G probably functions in poly(A)-dependent translation in mammalian cells. Using coimmunoprecipitation experiments, Pyronnet et al. (1999) demonstrated that MNK1 (MKNK1; 606724) is associated with the eIF4F complex via an interaction with the C-terminal region of eIF4G. They hypothesized that eIF4G provides a docking site for Mnk1 to phosphorylate eIF4E. Cytokine and protooncogene mRNAs are rapidly degraded through AU-rich elements in the 3-prime untranslated region. Rapid decay involves AU-rich binding protein AUF1 (601324), which complexes with heat-shock proteins ... More on the omim web site
April 25, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 23, 2019: 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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 600495 was added.