Eukaryotic translation initiation factor 3 subunit G (EIF3G)

The protein contains 320 amino acids for an estimated molecular weight of 35611 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: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: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). This subunit can bind 18S rRNA.', '(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. 25, 2017)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. 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.
  3. 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.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. 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.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

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.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 30%
Model score: 26

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The reference OMIM entry for this protein is 603913

Eukaryotic translation initiation factor 3, subunit g; eif3g
Eif3-p42
Eif3-p44
Eukaryotic translation initiation factor 3, subunit 4, formerly; eif3s4, 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). By searching an EST database with partial protein sequences of the human eIF3-p44 and eIF3-p35 (603910) subunits, Block et al. (1998) isolated cDNAs encoding these 2 proteins. The predicted 320-amino acid p44 protein contains an RRM (RNA recognition motif) near the C terminus. Sequence analysis indicated that human p44 shares 97% protein sequence identity with the predicted mouse p44 homolog and 33% identity with the S. cerevisiae eIF3-p33 subunit. Using Northwestern blots, Block et al. (1998) demonstrated that p44 binds RNA, as do eIF3 subunits p170 (602039) and p66. On Far Western blots, the p44 protein interacted strong and specifically with p170, and weakly with p116 (603917)/p110 (603916), p66, p40 (603912), and itself. Northern blot analysis revealed that p44 is expressed as an approximately 1.4-kb mRNA in HeLa cells. Independently, Bandyopadhyay and Maitra (1999) cloned cDNAs encoding p44, which they called p42. When expressed in mammalian cells, epitope-tagged p42 was incorporated into endogenous eIF3. The authors found that a major fraction of endogenous eIF5 was associated with eIF3, leading them to suggest that a specific interaction between these 2 initiation factors may play an important role in the function of eIF5 during translation initiation. ... More on the omim web site

Subscribe to this protein entry history

Feb. 10, 2018: 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 603913 was added.

Jan. 24, 2016: Protein entry updated
Automatic update: model status changed