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EIF3G

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

EIF3G

Available structures

PDB

Ortholog search:PDBe RCSB

List of PDB id codes
2CQ0,2MJC,5K0Y

Identifiers

Aliases

EIF3G, EIF3-P42, EIF3S4, eIF3-delta, eIF3-p44, eukaryotic translation initiation factor 3 subunit G

External IDs

OMIM:603913;MGI:1858258;HomoloGene:2784;GeneCards:EIF3G;OMA:EIF3G - orthologs

Gene location (Human)

Chr.	Chromosome 19 (human)^[1]

Band	19p13.2	Start	10,115,014bp^[1]
Band	19p13.2	End	10,119,918bp^[1]

Gene location (Mouse)

Chr.	Chromosome 9 (mouse)^[2]

Band	9\|9 A3	Start	20,805,645bp^[2]
Band	9\|9 A3	End	20,809,919bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

granulocyte

body of pancreas

left ovary

left testis

right testis

gastrocnemius muscle

right ovary

canal of the cervix

body of stomach

Achilles tendon

Top expressed in

primitive streak

mandibular prominence

Gonadal ridge

maxillary prominence

vas deferens

condyle

hair follicle

abdominal wall

epiblast

medullary collecting duct

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	protein binding translation initiation factor activity nucleic acid binding RNA binding
Cellular component	cytoplasm perinuclear region of cytoplasm eukaryotic translation initiation factor 3 complex nucleus cytosol eukaryotic 43S preinitiation complex eukaryotic 48S preinitiation complex
Biological process	translational initiation viral translational termination-reinitiation protein biosynthesis formation of cytoplasmic translation initiation complex cytoplasmic translational initiation
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


8666


53356

Ensembl


ENSG00000130811


ENSMUSG00000070319

UniProt


O75821


Q9Z1D1

RefSeq (mRNA)


NM_003755


NM_016876

RefSeq (protein)


NP_003746


NP_058572

Location (UCSC)

Chr 19: 10.12 – 10.12 Mb

Chr 9: 20.81 – 20.81 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Eukaryotic translation initiation factor 3 subunit G (eIF3g) is aprotein that in humans is encoded by theEIF3Ggene.^[5]^[6]

Interactions

[edit]

EIF3G has been shown tointeract withBand 4.1,^[7]EIF3C^[5]^[8] andEIF3A.^[5]^[9]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000130811 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000070319 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^^a ^b ^cBlock 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.
^"Entrez Gene: EIF3S4 eukaryotic translation initiation factor 3, subunit 4 delta, 44kDa".
^Hou CL, Tang Cj, 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.doi:10.1182/blood.V96.2.747.PMID 10887144.
^Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J,Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network".Nature.437 (7062):1173–8.Bibcode:2005Natur.437.1173R.doi:10.1038/nature04209.PMID 16189514.S2CID 4427026.
^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.

Hillier LD, Lennon G, Becker M, Bonaldo MF, Chiapelli B, Chissoe S, Dietrich N, DuBuque T, Favello A, Gish W, Hawkins M, Hultman M, Kucaba T, Lacy M, Le M, Le N, Mardis E, Moore B, Morris M, Parsons J, Prange C, Rifkin L, Rohlfing T, Schellenberg K, Bento Soares M, Tan F, Thierry-Meg J, Trevaskis E, Underwood K, Wohldman P, Waterston R, Wilson R, Marra M (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.
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.
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, Cohn MA, Cantley LC, Gygi SP (2004)."Large-scale characterization of HeLa cell nuclear phosphoproteins".Proc. Natl. Acad. Sci. U.S.A.101 (33):12130–5.Bibcode:2004PNAS..10112130B.doi:10.1073/pnas.0404720101.PMC 514446.PMID 15302935.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network".Nature.437 (7062):1173–8.Bibcode:2005Natur.437.1173R.doi:10.1038/nature04209.PMID 16189514.S2CID 4427026.
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.Bibcode:2005BBRC..338..771O.doi:10.1016/j.bbrc.2005.10.013.PMID 16243297.
Kim JT, Kim KD, Song EY, Lee HG, Kim JW, Kim JW, Chae SK, Kim E, Lee MS, Yang Y, Lim JS (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.Bibcode:2006FEBSL.580.6375K.doi:10.1016/j.febslet.2006.10.049.PMID 17094969.S2CID 32237993.
Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (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.

v t e PDB gallery
2cq0: solution structure of RNA binding domain in eukaryotic translation initiation factor 3 subunit 4

Protein biosynthesis:translation (bacterial,archaeal,eukaryotic)

Proteins

eIF1	eIF1 B SUI1 family eIF1A Y
eIF2	α kinase β γ eIF2A eIF2B 1 2 3 4 5 eIF2D
eIF3	A B C D E F G H I J K L M
eIF4	A 1 2 3 E1 2 3 G 1 2 3 B H
eIF5	EIF5 EIF5A 2 5B
eIF6	EIF6

Elongation factor

Bacterial/Mitochondrial	EF-Tu EF-Ts EF-G EF-4 EF-P TSFM GFM1 GFM2
Archaeal/Eukaryotic	a/eEF-1 A1 2 3 B P1 P2 P3 D E G a/eEF-2

Release factor

Class 1
- eRF1
Class 2/RF3
- GSPT1
- GSPT2

Ribosomal Proteins

Cytoplasmic

60S subunit	RPL3 RPL4 RPL5 RPL6 RPL7 RPL7A RPL8 RPL9 RPL10 RPL10A RPL10-like RPL11 RPL12 RPL13 RPL13A RPL14 RPL15 RPL17 RPL18 RPL18A RPL19 RPL21 RPL22 RPL23 RPL23A RPL24 RPL26 RPL27 RPL27A RPL28 RPL29 RPL30 RPL31 RPL32 RPL34 RPL35 RPL35A RPL36 RPL36A RPL37 RPL37A RPL38 RPL39 RPL40 RPL41 RPLP0 RPLP1 RPLP2 RRP15-like RSL24D1
40S subunit	RPSA RPS2 RPS3 RPS3A RPS4 (RPS4X,RPS4Y1,RPS4Y2) RPS5 RPS6 RPS7 RPS8 RPS9 RPS10 RPS11 RPS12 RPS13 RPS14 RPS15 RPS15A RPS16 RPS17 RPS18 RPS19 RPS20 RPS21 RPS23 RPS24 RPS25 RPS26 RPS27 RPS27A RPS28 RPS29 RPS30 RACK1

Mitochondrial

39S subunit	MRPL1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42
28S subunit	MRPS1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35

Other concepts

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