EIF3G

Eukaryotic translation initiation factor 3, subunit G

PDB rendering based on 2cq0.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2CQ0

Identifiers

Symbols

EIF3G ; EIF3-P42; EIF3S4; eIF3-delta; eIF3-p44

External IDs

OMIM: 603913 MGI: 1858258 HomoloGene: 2784 GeneCards: EIF3G Gene

Gene ontology
Molecular function	• nucleotide binding • translation initiation factor activity • protein binding • poly(A) RNA binding
Cellular component	• nucleus • cytosol • eukaryotic translation initiation factor 3 complex • eukaryotic 43S preinitiation complex • eukaryotic 48S preinitiation complex • perinuclear region of cytoplasm
Biological process	• formation of translation preinitiation complex • translation • translational initiation • regulation of translational initiation • gene expression • cellular protein metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
10.23 – 10.23 Mb

Chr 9:
20.89 – 20.9 Mb

PubMed search

Eukaryotic translation initiation factor 3 subunit G is a protein that in humans is encoded by the EIF3G gene.^[1]^[2]

Interactions

EIF3G has been shown to interact with Band 4.1,^[3] EIF3C^[1]^[4] and EIF3A.^[1]^[5]

References

↑ 1.0 1.1 1.2 Block KL, Vornlocher HP, Hershey JW (December 1998). "Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3". J. Biol. Chem. 273 (48): 31901–8. doi:10.1074/jbc.273.48.31901. PMID 9822659. CS1 maint: Date and year (link)
↑ "Entrez Gene: EIF3S4 eukaryotic translation initiation factor 3, subunit 4 delta, 44kDa".
↑ Hou CL, Tang C, Roffler SR, Tang TK (July 2000). "Protein 4.1R binding to eIF3-p44 suggests an interaction between the cytoskeletal network and the translation apparatus". Blood 96 (2): 747–53. PMID 10887144. CS1 maint: Date and year (link)
↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N et al. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. CS1 maint: Date and year (link)
↑ Mayeur GL, Fraser CS, Peiretti F, Block KL, Hershey JW (October 2003). "Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor elF3". Eur. J. Biochem. 270 (20): 4133–9. doi:10.1046/j.1432-1033.2003.03807.x. PMID 14519125. CS1 maint: Date and year (link)

Hillier LD, Lennon G, Becker M, Bonaldo MF, Chiapelli B, Chissoe S et al. (1996). "Generation and analysis of 280,000 human expressed sequence tags". Genome Res. 6 (9): 807–28. doi:10.1101/gr.6.9.807. PMID 8889549.
Asano K, Kinzy TG, Merrick WC, Hershey JW (1997). "Conservation and diversity of eukaryotic translation initiation factor eIF3". J. Biol. Chem. 272 (2): 1101–9. doi:10.1074/jbc.272.2.1101. PMID 8995409.
Méthot N, Rom E, Olsen H, Sonenberg N (1997). "The human homologue of the yeast Prt1 protein is an integral part of the eukaryotic initiation factor 3 complex and interacts with p170". J. Biol. Chem. 272 (2): 1110–6. doi:10.1074/jbc.272.2.1110. PMID 8995410. Vancouver style error (help)
Bandyopadhyay A, Maitra U (1999). "Cloning and characterization of the p42 subunit of mammalian translation initiation factor 3 (eIF3): demonstration that eIF3 interacts with eIF5 in mammalian cells". Nucleic Acids Res. 27 (5): 1331–7. doi:10.1093/nar/27.5.1331. PMC 148320. PMID 9973622.
Hou CL, Tang C, Roffler SR, Tang TK (2000). "Protein 4.1R binding to eIF3-p44 suggests an interaction between the cytoskeletal network and the translation apparatus". Blood 96 (2): 747–53. PMID 10887144.
Mayeur GL, Fraser CS, Peiretti F, Block KL, Hershey JW (2003). "Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor elF3". Eur. J. Biochem. 270 (20): 4133–9. doi:10.1046/j.1432-1033.2003.03807.x. PMID 14519125.
Fraser CS, Lee JY, Mayeur GL, Bushell M, Doudna JA, Hershey JW (2004). "The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro". J. Biol. Chem. 279 (10): 8946–56. doi:10.1074/jbc.M312745200. PMID 14688252.
Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935. Vancouver style error (help)
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Ogawa F, Kasai M, Akiyama T (2005). "A functional link between Disrupted-In-Schizophrenia 1 and the eukaryotic translation initiation factor 3". Biochem. Biophys. Res. Commun. 338 (2): 771–6. doi:10.1016/j.bbrc.2005.10.013. PMID 16243297.
Kim JT, Kim KD, Song EY, Lee HG, Kim JW, Kim JW et al. (2006). "Apoptosis-inducing factor (AIF) inhibits protein synthesis by interacting with the eukaryotic translation initiation factor 3 subunit p44 (eIF3g)". FEBS Lett. 580 (27): 6375–83. doi:10.1016/j.febslet.2006.10.049. PMID 17094969.
Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

PDB gallery

2cq0: solution structure of RNA binding domain in eukaryotic translation initiation factor 3 subunit 4

Protein biosynthesis: translation (prokaryotic, eukaryotic)

Ribosomal proteins

Initiation factor

Prokaryotic

Archaeal

aIF1
aIF2
aIF5
aIF6

Eukaryotic

eIF1	EIF1AX AY 1B

eIF2	EIF2S1 EIF2S2 EIF2S3 EIF2B1 EIF2B2 EIF2B3 EIF2B4 EIF2B5 EIF-2 kinase

eIF3	EIF3A B C D F G H I J K M S6

eIF4	EIF4A2 A3 B E1 E2 G1 G2 G3 H

eIF5	EIF5A A2 B

eIF6	EIF6

Elongation factor

Prokaryotic	EF-Tu EF-Ts EF-G

Archaeal	aEF-1, aEF-2

Eukaryotic	EEF-1 EEF1A1 EEF1A2 EEF1A3 EEF1B1 EEF1B2 EEF1B3 EEF1B4 EEF1D EEF1E1 EEF1G EEF2

Release factor

Other

Other concepts

Index of genetics

Description	Gene expression DNA replication cycle recombination repair binding proteins Transcription factors regulators nucleic acids RNA RNA binding proteins ribonucleoproteins repeated sequence modification Translation ribosome modification nexins Proteins domains Structure primary secondary tertiary quaternary

Disease	Replication and repair Transcription factor Transcription Translation

EIF3G

Interactions

References

Further reading