EIF3D

Eukaryotic translation initiation factor 3, subunit D

Identifiers

EIF3D; EIF3S7; MGC126526; MGC17258; eIF3-p66; eIF3-zeta

External IDs

OMIM: 603915 MGI: 1933181 HomoloGene: 2782 GeneCards: EIF3D Gene

Gene Ontology
Molecular function	• translation initiation factor activity • translation initiation factor activity • protein binding
Cellular component	• cytoplasm • cytosol • cytosol • eukaryotic translation initiation factor 3 complex
Biological process	• formation of translation initiation complex • translation • translational initiation • 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 22:
36.91 – 36.93 Mb

Chr 15:
77.79 – 77.8 Mb

PubMed search

[1]

[2]

Eukaryotic translation initiation factor 3 subunit D is a protein that in humans is encoded by the EIF3D gene.^[1]^[2]

Eukaryotic translation initiation factor-3 (eIF3), the largest of the eIFs, is a multiprotein complex composed of at least ten nonidentical subunits. The complex binds to the 40S ribosome and helps maintain the 40S and 60S ribosomal subunits in a dissociated state. It is also thought to play a role in the formation of the 40S initiation complex by interacting with the ternary complex of eIF2/GTP/methionyl-tRNA, and by promoting mRNA binding. The protein encoded by this gene is the major RNA binding subunit of the eIF3 complex.^[2]

Interactions

EIF3D has been shown to interact with PHLDA1^[3] and EIF3A.^[4]^[5]^[6]

References

^ Asano K, Vornlocher HP, Richter-Cook NJ, Merrick WC, Hinnebusch AG, Hershey JW (Nov 1997). "Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly". J Biol Chem 272 (43): 27042–52. doi:10.1074/jbc.272.43.27042. PMID 9341143.
^ ^a ^b "Entrez Gene: EIF3S7 eukaryotic translation initiation factor 3, subunit 7 zeta, 66/67kDa". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8664.
^ Hinz, T; Flindt S, Marx A, Janssen O, Kabelitz D (May. 2001). "Inhibition of protein synthesis by the T cell receptor-inducible human TDAG51 gene product". Cell. Signal. (England) 13 (5): 345–52. doi:10.1016/S0898-6568(01)00141-3. ISSN 0898-6568. PMID 11369516.
^ Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. (England) 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.
^ Mayeur, Greg L; Fraser Christopher S, Peiretti Franck, Block Karen L, Hershey John W B (Oct. 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.
^ Block, K L; Vornlocher H P, Hershey J W (Nov. 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.

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.
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.
Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22.". Nature 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125443.
Hinz T, Flindt S, Marx A, et al. (2001). "Inhibition of protein synthesis by the T cell receptor-inducible human TDAG51 gene product.". Cell. Signal. 13 (5): 345–52. doi:10.1016/S0898-6568(01)00141-3. PMID 11369516.
Morris-Desbois C, Réty S, Ferro M, et al. (2002). "The human protein HSPC021 interacts with Int-6 and is associated with eukaryotic translation initiation factor 3.". J. Biol. Chem. 276 (49): 45988–95. doi:10.1074/jbc.M104966200. PMID 11590142.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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.
Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome.". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=545604.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
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.
Ewing RM, Chu P, Elisma F, 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.

Protein biosynthesis: translation (prokaryotic, eukaryotic)

Ribosomal proteins

Initiation factor

Prokaryotic	PIF-1 · PIF-2 · PIF-3

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

Prokaryotic · Archaeal · Eukaryotic (ETF1)

Other

RPS1 · RPS2 · RPS3 · RPS4 · RPS5 · RPS6 · RPS7 · RPS8 · RPS9 · RPS10 · RPS11 · RPS12 · RPS13 · RPS14 · RPS15 · RPS16 · RPS17 · RPS18 · RPS19 · RPS20 · RPS21 · RPS22 · RPS23 · RPS24 · RPS25 · RPS26 · RPS27 · RPS28 · RPS29

Other concepts

Aminoacyl tRNA synthetase · Reading frame · Start codon · Stop codon · Shine-Dalgarno sequence/Kozak consensus sequence

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°)

EIF3D

Interactions

References

Further reading