Eukaryotic translation initiation factor 3 subunit B (EIF3B)
The protein contains 814 amino acids for an estimated molecular weight of 92482 Da.
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:9388245, PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:9388245, PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773).', '(Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
- 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:rs9690787 | |
| dbSNP:rs1063257 |
Biological Process
Formation of cytoplasmic translation initiation complex
IRES-dependent viral translational initiation
Regulation of translational initiation
Translational initiation
Viral translational termination-reinitiation
The reference OMIM entry for this protein is 603917
Eukaryotic translation initiation factor 3, subunit b; eif3b
Protein synthesis defective at 36 degrees celsius 1, s. cerevisiae, homolog of; prt1
Eif3-p116
Eukaryotic translation initiation factor 3, subunit 9, formerly; eif3s9, formerly
Eukaryotic initiation factor-3 (eIF3) is the largest of the eIFs and consists of at least 10 nonidentical subunits in mammals. See p66 (EIF3S7; 603915). The S. cerevisiae Prt1, or p90, protein is an integral subunit of eIF3. Mutations in Prt1 impair translation initiation at 37 degrees Celsius. By searching an EST database, Methot et al. (1997) identified a cDNA encoding a human Prt1 homolog. The predicted 873-amino acid human PRT1 protein is 31% identical to yeast Prt1. PRT1 is an acidic protein, with a predicted pI of 4.8, and contains an RNA recognition motif (RRM). Immunologic experiments demonstrated that PRT1 corresponds to the 115-kD polypeptide of eIF3 and is part of the eIF3 complex. PRT1 interacts directly with the p170 (602039) subunit of eIF3, and the region required for this association is located within the RRM. Northern blot analysis revealed that PRT1 is expressed as a 3.1-kb mRNA in HeLa cells. Asano et al. (1997) demonstrated that the 115-kD component of HeLa cell eIF3 is actually composed of 2 proteins, p116 (PRT1) and an unrelated 110-kD protein (p110; 603916). Chaudhuri et al. (1997) isolated cDNAs encoding PRT1, which they called p110 based on the size of the corresponding component of rabbit eIF3. Chaudhuri et al. (1997) noted that their protein sequence differs from that of PRT1 reported by Methot et al. (1997) in that the latter contains an additional 59 C-terminal amino acids. ... More on the omim web site
Nov. 17, 2018: Protein entry updated
Automatic update: OMIM entry 603917 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).