EIF3B

EIF3B

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2KRB, 2NLW, 5K1H

Identifiers

EIF3B, EIF3-ETA, EIF3-P110, EIF3-P116, EIF3S9, PRT1, eukaryotic translation initiation factor 3 subunit B

External IDs

OMIM: 603917; MGI: 106478; HomoloGene: 2780; GeneCards: EIF3B; OMA:EIF3B - orthologs

Gene location (Human)

Chr.	Chromosome 7 (human)^[1]

Band	7p22.3	Start	2,354,086 bp^[1]
Band	7p22.3	End	2,380,745 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 5 (mouse)^[2]

Band	5 G2\|5 78.97 cM	Start	140,405,083 bp^[2]
Band	5 G2\|5 78.97 cM	End	140,429,115 bp^[2]

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

body of pancreas

skin of abdomen

skin of leg

muscle layer of sigmoid colon

stromal cell of endometrium

left uterine tube

gastrocnemius muscle

ventricular zone

right ovary

smooth muscle tissue

Top expressed in

epiblast

spermatid

ventricular zone

yolk sac

lip

otic vesicle

lactiferous gland

somite

morula

morula

More reference expression data


More reference expression data

Gene ontology
Molecular function	molecular adaptor activity translation initiation factor binding protein binding translation initiation factor activity nucleic acid binding RNA binding
Cellular component	cytosol eukaryotic translation initiation factor 3 complex eukaryotic translation initiation factor 3 complex, eIF3m extracellular exosome cytoplasm eukaryotic 43S preinitiation complex eukaryotic 48S preinitiation complex synapse
Biological process	translational initiation IRES-dependent viral translational initiation protein biosynthesis viral translational termination-reinitiation regulation of translational initiation formation of cytoplasmic translation initiation complex cytoplasmic translational initiation
Sources:Amigo / QuickGO

Species

Human

Mouse


8662


27979


ENSG00000106263


ENSMUSG00000056076


P55884


Q8JZQ9

RefSeq (mRNA)

NM_001037283 NM_003751 NM_001362791 NM_001362792 NM_001362793
NM_182712


NM_133916

RefSeq (protein)


NP_001032360 NP_003742 NP_001349720 NP_001349721 NP_001349722


NP_598677

Location (UCSC)

Chr 7: 2.35 – 2.38 Mb

Chr 5: 140.41 – 140.43 Mb

PubMed search

^[3]

^[4]

View/Edit Human

View/Edit Mouse

Eukaryotic translation initiation factor 3 subunit B (eIF3b) is a protein that in humans is encoded by the EIF3B gene.^[5]^[6]

Interactions

EIF3B has been shown to interact with P70-S6 Kinase 1^[7] and EIF3A.^[5]^[8]^[9]^[10]

See also

Eukaryotic initiation factor 3 (eIF3)

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000106263 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000056076 – 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 Méthot N, Rom E, Olsen H, Sonenberg N (February 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.
^ "Entrez Gene: EIF3S9 eukaryotic translation initiation factor 3, subunit 9 eta, 116kDa".
^ Holz MK, Ballif BA, Gygi SP, Blenis J (November 2005). "mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events". Cell. 123 (4): 569–80. doi:10.1016/j.cell.2005.10.024. PMID 16286006. S2CID 11118504.
^ 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.
^ Harris TE, Chi A, Shabanowitz J, Hunt DF, Rhoads RE, Lawrence JC (April 2006). "mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin". EMBO J. 25 (8): 1659–68. doi:10.1038/sj.emboj.7601047. PMC 1440840. PMID 16541103.
^ Block KL, Vornlocher HP, Hershey JW (November 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.

Further reading

Kirken RA, Rui H, Evans GA, Farrar WL (1993). "Characterization of an interleukin-2 (IL-2)-induced tyrosine phosphorylated 116-kDa protein associated with the IL-2 receptor beta-subunit". J. Biol. Chem. 268 (30): 22765–70. doi:10.1016/S0021-9258(18)41592-X. PMID 7693677.
Bonaldo MF, Lennon G, Soares MB (1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
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.
Chaudhuri J, Chakrabarti A, Maitra U (1997). "Biochemical characterization of mammalian translation initiation factor 3 (eIF3). Molecular cloning reveals that p110 subunit is the mammalian homologue of Saccharomyces cerevisiae protein Prt1". J. Biol. Chem. 272 (49): 30975–83. doi:10.1074/jbc.272.49.30975. PMID 9388245.
Block KL, Vornlocher HP, Hershey JW (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.
Sanger Centre, The; Washington University Genome Sequencing Cente, The (1998). "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. doi:10.1101/gr.8.11.1097. PMID 9847074.
Lin L, Holbro T, Alonso G, Gerosa D, Burger MM (2001). "Molecular interaction between human tumor marker protein p150, the largest subunit of eIF3, and intermediate filament protein K7". J. Cell. Biochem. 80 (4): 483–90. doi:10.1002/1097-4644(20010315)80:4<483::AID-JCB1002>3.0.CO;2-B. PMID 11169732. S2CID 35848129.
Asano K, Shalev A, Phan L, Nielsen K, Clayton J, Valásek L, Donahue TF, Hinnebusch AG (2001). "Multiple roles for the C-terminal domain of eIF5 in translation initiation complex assembly and GTPase activation". EMBO J. 20 (9): 2326–37. doi:10.1093/emboj/20.9.2326. PMC 125443. PMID 11331597.
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.
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.
Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
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.
ElAntak L, Tzakos AG, Locker N, Lukavsky PJ (2007). "Structure of eIF3b RNA recognition motif and its interaction with eIF3j: structural insights into the recruitment of eIF3b to the 40 S ribosomal subunit" (PDF). J. Biol. Chem. 282 (11): 8165–74. doi:10.1074/jbc.M610860200. PMID 17190833. S2CID 2313046.

v t e PDB gallery
2nlw: Solution structure of the RRM domain of human eukaryotic initiation factor 3b

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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