EIF3B

From Wikipedia, the free encyclopedia

Eukaryotic translation initiation factor 3, subunit B

PDB rendering based on 2nlw.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2KRB, 2NLW

Identifiers

Symbols

EIF3B; EIF3-ETA; EIF3-P110; EIF3-P116; EIF3S9; PRT1

External IDs

OMIM: 603917 MGI: 106478 HomoloGene: 2780 GeneCards: EIF3B Gene

Gene Ontology
Molecular function	• nucleotide binding • translation initiation factor activity • protein binding • translation initiation factor binding • protein complex scaffold
Cellular component	• cytosol • eukaryotic translation initiation factor 3 complex
Biological process	• 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 7:
2.39 – 2.42 Mb

Chr 5:
140.42 – 140.44 Mb

PubMed search

Eukaryotic translation initiation factor 3 subunit B is a protein that in humans is encoded by the EIF3B gene.^[1]^[2]

Interactions

EIF3B has been shown to interact with P70-S6 Kinase 1^[3] and EIF3A.^[1]^[4]^[5]^[6]

References

↑ 1.0 1.1 Methot 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, Marina K; Ballif Bryan A, Gygi Steven P, Blenis John (November 2005). "mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events". Cell (United States) 123 (4): 569–80. doi:10.1016/j.cell.2005.10.024. ISSN 0092-8674. PMID 16286006. Cite uses deprecated parameters (help)
↑ Mayeur, Greg L; Fraser Christopher S, Peiretti Franck, Block Karen L, Hershey John W B (October 2003). "Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor elF3". Eur. J. Biochem. (Germany) 270 (20): 4133–9. doi:10.1046/j.1432-1033.2003.03807.x. ISSN 0014-2956. PMID 14519125. Cite uses deprecated parameters (help)
↑ Harris, Thurl E; Chi An, Shabanowitz Jeffrey, Hunt Donald F, Rhoads Robert E, Lawrence John C (April 2006). "mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin". EMBO J. (England) 25 (8): 1659–68. doi:10.1038/sj.emboj.7601047. ISSN 0261-4189. PMC 1440840. PMID 16541103. Cite uses deprecated parameters (help)
↑ Block, K L; Vornlocher H P, Hershey J W (November 1998). "Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3". J. Biol. Chem. (UNITED STATES) 273 (48): 31901–8. doi:10.1074/jbc.273.48.31901. ISSN 0021-9258. PMID 9822659. Cite uses deprecated parameters (help)

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. PMID 7693677.
Bonaldo MF, Lennon G, Soares MB (1997). "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 (1998). "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.
"Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. 1999. doi:10.1101/gr.8.11.1097. PMID 9847074.
Lin L, Holbro T, Alonso G et al. (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.
Asano K, Shalev A, Phan L et al. (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.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Scherer SW, Cheung J, MacDonald JR et al. (2003). "Human Chromosome 7: DNA Sequence and Biology". Science 300 (5620): 767–72. doi:10.1126/science.1083423. PMC 2882961. PMID 12690205.
Mayeur GL, Fraser CS, Peiretti F et al. (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 et al. (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.
Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Beausoleil SA, Jedrychowski M, Schwartz D 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.
Gerhard DS, Wagner L, Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Rush J, Moritz A, Lee KA et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
Olsen JV, Blagoev B, Gnad F et al. (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.
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". J. Biol. Chem. 282 (11): 8165–74. doi:10.1074/jbc.M610860200. PMID 17190833.

PDB gallery

2nlw: Solution structure of the RRM domain of human eukaryotic initiation factor 3b

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

see also disorders of translation and posttranslational modification
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

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EIF3B

Interactions

References

Further reading