EIF4B

EIF4B

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1WI8, 2J76

Identifiers

EIF4B, EIF-4B, PRO1843, eukaryotic translation initiation factor 4B

External IDs

OMIM: 603928; MGI: 95304; HomoloGene: 83162; GeneCards: EIF4B; OMA:EIF4B - orthologs

Gene location (Human)

Chr.	Chromosome 12 (human)^[1]

Band	12q13.13	Start	53,006,282 bp^[1]
Band	12q13.13	End	53,042,215 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 15 (mouse)^[2]

Band	15\|15 F2	Start	101,982,208 bp^[2]
Band	15\|15 F2	End	102,005,608 bp^[2]

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

Achilles tendon

ganglionic eminence

left ovary

epithelium of colon

islet of Langerhans

stromal cell of endometrium

body of pancreas

right ovary

ventricular zone

monocyte

Top expressed in

tail of embryo

lacrimal gland

genital tubercle

epiblast

ankle

ventricular zone

somite

mandibular prominence

left lung lobe

vas deferens

More reference expression data


More reference expression data

Gene ontology
Molecular function	protein binding nucleic acid binding ribosomal small subunit binding helicase activity RNA strand-exchange activity RNA strand annealing activity RNA binding translation initiation factor activity
Cellular component	cytosol eukaryotic translation initiation factor 4F complex polysome
Biological process	nuclear-transcribed mRNA poly(A) tail shortening regulation of translational initiation formation of translation preinitiation complex eukaryotic translation initiation factor 4F complex assembly protein biosynthesis translational initiation cytoplasmic translation
Sources:Amigo / QuickGO

Species

Human

Mouse


1975


75705


ENSG00000063046


ENSMUSG00000058655


P23588


Q8BGD9

RefSeq (mRNA)


NM_001300821 NM_001417 NM_018507 NM_001330654


NM_145625

RefSeq (protein)


NP_001287750 NP_001317583 NP_001408


NP_663600

Location (UCSC)

Chr 12: 53.01 – 53.04 Mb

Chr 15: 101.98 – 102.01 Mb

PubMed search

^[3]

^[4]

View/Edit Human

View/Edit Mouse

Eukaryotic translation initiation factor 4B is a protein that in humans is encoded by the EIF4B gene.^[5]

Interactions

eIF4B has been shown to interact with and stimulate the activity of eIF4A and bind to the eIF3 complex through the eIF3A subunit.^[6] This interaction results in the recruitment of the eukaryotic small ribosomal subunit (40S) to the mRNA which will in turn set the stage for the later steps leading to elongation.

See also

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000063046 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000058655 – 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.
^ "Entrez Gene: EIF4B eukaryotic translation initiation factor 4B".
^ Merrick WC (Oct 2015). "eIF4F: a retrospective". The Journal of Biological Chemistry. 290 (40): 24091–9. doi:10.1074/jbc.R115.675280. PMC 4591800. PMID 26324716.

Further reading

van Heugten HA, Kasperaitis MA, Thomas AA, Voorma HO (1991). "Evidence that eukaryotic initiation factor (eIF) 2 is a cap-binding protein that stimulates cap recognition by eIF-4B and eIF-4F". J. Biol. Chem. 266 (11): 7279–84. doi:10.1016/S0021-9258(20)89641-0. PMID 2016328.
Milburn SC, Hershey JW, Davies MV, Kelleher K, Kaufman RJ (1990). "Cloning and expression of eukaryotic initiation factor 4B cDNA: sequence determination identifies a common RNA recognition motif". EMBO J. 9 (9): 2783–90. doi:10.1002/j.1460-2075.1990.tb07466.x. PMC 551988. PMID 2390971.
Howe JG, Hershey JW (1984). "Translational initiation factor and ribosome association with the cytoskeletal framework fraction from HeLa cells". Cell. 37 (1): 85–93. doi:10.1016/0092-8674(84)90303-9. PMID 6722878.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Méthot N, Pause A, Hershey JW, Sonenberg N (1994). "The translation initiation factor eIF-4B contains an RNA-binding region that is distinct and independent from its ribonucleoprotein consensus sequence". Mol. Cell. Biol. 14 (4): 2307–16. doi:10.1128/mcb.14.4.2307. PMC 358597. PMID 8139536.
Naranda T, Strong WB, Menaya J, Fabbri BJ, Hershey JW (1994). "Two structural domains of initiation factor eIF-4B are involved in binding to RNA". J. Biol. Chem. 269 (20): 14465–72. doi:10.1016/S0021-9258(17)36646-2. PMID 8182051.
Méthot N, Song MS, Sonenberg N (1996). "A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3". Mol. Cell. Biol. 16 (10): 5328–34. doi:10.1128/MCB.16.10.5328. PMC 231531. PMID 8816444.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Richter NJ, Rogers GW, Hensold JO, Merrick WC (1999). "Further biochemical and kinetic characterization of human eukaryotic initiation factor 4H". J. Biol. Chem. 274 (50): 35415–24. doi:10.1074/jbc.274.50.35415. PMID 10585411.
Bushell M, Wood W, Clemens MJ, Morley SJ (2000). "Changes in integrity and association of eukaryotic protein synthesis initiation factors during apoptosis". Eur. J. Biochem. 267 (4): 1083–91. doi:10.1046/j.1432-1327.2000.01101.x. PMID 10672017.
Bushell M, Wood W, Carpenter G, Pain VM, Morley SJ, Clemens MJ (2001). "Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavages". J. Biol. Chem. 276 (26): 23922–8. doi:10.1074/jbc.M100384200. PMID 11274152.
Fleming K, Ghuman J, Yuan X, Simpson P, Szendröi A, Matthews S, Curry S (2003). "Solution structure and RNA interactions of the RNA recognition motif from eukaryotic translation initiation factor 4B". Biochemistry. 42 (30): 8966–75. doi:10.1021/bi034506g. PMID 12885229.
Raught B, Peiretti F, Gingras AC, Livingstone M, Shahbazian D, Mayeur GL, Polakiewicz RD, Sonenberg N, Hershey JW (2004). "Phosphorylation of eucaryotic translation initiation factor 4B Ser422 is modulated by S6 kinases". EMBO J. 23 (8): 1761–9. doi:10.1038/sj.emboj.7600193. PMC 394247. PMID 15071500.
Doepker RC, Hsu WL, Saffran HA, Smiley JR (2004). "Herpes simplex virus virion host shutoff protein is stimulated by translation initiation factors eIF4B and eIF4H". J. Virol. 78 (9): 4684–99. doi:10.1128/JVI.78.9.4684-4699.2004. PMC 387725. PMID 15078951.
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.
Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
Shahbazian D, Roux PP, Mieulet V, Cohen MS, Raught B, Taunton J, Hershey JW, Blenis J, Pende M, Sonenberg N (2006). "The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity". EMBO J. 25 (12): 2781–91. doi:10.1038/sj.emboj.7601166. PMC 1500846. PMID 16763566.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.

v t e PDB gallery
1wi8: Solution structure of the RNA binding domain of eukaryotic initiation factor 4B

Protein biosynthesis: translation (bacterial, archaeal, eukaryotic)

Proteins

Initiation factor

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

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

Ribosomal Proteins

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

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

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