EIF3D

Protein-coding gene in the species Homo sapiens
EIF3D
Identifiers
AliasesEIF3D, EIF3S7, eIF3-p66, eIF3-zeta, eukaryotic translation initiation factor 3 subunit D
External IDsOMIM: 603915; MGI: 1933181; HomoloGene: 2782; GeneCards: EIF3D; OMA:EIF3D - orthologs
Gene location (Human)
Chromosome 22 (human)
Chr.Chromosome 22 (human)[1]
Chromosome 22 (human)
Genomic location for EIF3D
Genomic location for EIF3D
Band22q12.3Start36,510,855 bp[1]
End36,529,184 bp[1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[2]
Chromosome 15 (mouse)
Genomic location for EIF3D
Genomic location for EIF3D
Band15|15 E1Start77,843,198 bp[2]
End77,855,013 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • body of pancreas

  • left ovary

  • skin of abdomen

  • skin of leg

  • epithelium of nasopharynx

  • parotid gland

  • right uterine tube

  • right ovary

  • spleen

  • body of stomach
Top expressed in
  • epiblast

  • mandibular prominence

  • somite

  • abdominal wall

  • maxillary prominence

  • fetal liver hematopoietic progenitor cell

  • human fetus

  • efferent ductule

  • endothelial cell of lymphatic vessel

  • ventricular zone
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein binding
  • translation initiation factor activity
  • RNA binding
  • mRNA cap binding
Cellular component
  • cytoplasm
  • cytosol
  • eukaryotic translation initiation factor 3 complex, eIF3m
  • membrane
  • eukaryotic translation initiation factor 3 complex
  • eukaryotic 43S preinitiation complex
  • eukaryotic 48S preinitiation complex
Biological process
  • formation of cytoplasmic translation initiation complex
  • viral translational termination-reinitiation
  • translational initiation
  • protein biosynthesis
  • IRES-dependent viral translational initiation
  • cap-dependent translational initiation
  • positive regulation of translation
  • positive regulation of mRNA binding
  • cytoplasmic translational initiation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8664

55944

Ensembl

ENSG00000100353

ENSMUSG00000016554

UniProt

O15371

O70194

RefSeq (mRNA)

NM_003753

NM_018749

RefSeq (protein)

NP_003744

NP_061219

Location (UCSC)Chr 22: 36.51 – 36.53 MbChr 15: 77.84 – 77.86 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Eukaryotic translation initiation factor 3 subunit D (eIF3d) is a protein that in humans is encoded by the EIF3D gene.[5][6]

Function

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.[6]

Interactions

EIF3D has been shown to interact with PHLDA1[7] and EIF3A.[8][9][10]

EIF3D has also been shown to interact with c-Jun mRNA via a non-canonical mechanism. Instead of the EIF4G protein acting as a cap-binding protein to mediate translation, EIF3D has been shown to be a cap binding protein for certain mRNAs such as c-Jun which has structures at the 5' UTR inhibiting binding of EIF4G and promoting binding of EIF3D.[11] EIF3D as a cap binding protein has been thought of as critical to regulating gene expression under cell stress such as during glucose deprivation. For translation of c-Jun under glucose starved conditions, the cap binding activity of EIF3D increased by 10-fold.[12][13]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000100353 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000016554 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Asano K, Vornlocher HP, Richter-Cook NJ, Merrick WC, Hinnebusch AG, Hershey JW (October 1997). "Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly". The Journal of Biological Chemistry. 272 (43): 27042–27052. doi:10.1074/jbc.272.43.27042. PMID 9341143.
  6. ^ a b "Entrez Gene: EIF3S7 eukaryotic translation initiation factor 3, subunit 7 zeta, 66/67kDa".
  7. ^ 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". Cellular Signalling. 13 (5): 345–352. doi:10.1016/S0898-6568(01)00141-3. PMID 11369516.
  8. ^ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  9. ^ 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". European Journal of Biochemistry. 270 (20): 4133–4139. doi:10.1046/j.1432-1033.2003.03807.x. PMID 14519125.
  10. ^ Block KL, Vornlocher HP, Hershey JW (November 1998). "Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3". The Journal of Biological Chemistry. 273 (48): 31901–31908. doi:10.1074/jbc.273.48.31901. PMID 9822659.
  11. ^ Lee AS, Kranzusch PJ, Doudna JA, Cate JH (August 2016). "eIF3d is an mRNA cap-binding protein that is required for specialized translation initiation". Nature. 536 (7614): 96–99. Bibcode:2016Natur.536...96L. doi:10.1038/nature18954. PMC 5003174. PMID 27462815.
  12. ^ Jia L, Qian SB (January 2021). "A Versatile eIF3d in Translational Control of Stress Adaptation". Molecular Cell. 81 (1): 10–12. doi:10.1016/j.molcel.2020.12.016. PMID 33417853. S2CID 231303797.
  13. ^ Lamper AM, Fleming RH, Ladd KM, Lee AS (November 2020). "A phosphorylation-regulated eIF3d translation switch mediates cellular adaptation to metabolic stress". Science. 370 (6518): 853–856. Bibcode:2020Sci...370..853L. doi:10.1126/science.abb0993. PMID 33184215. S2CID 226308112.

Further reading

  • Asano K, Kinzy TG, Merrick WC, Hershey JW (January 1997). "Conservation and diversity of eukaryotic translation initiation factor eIF3". The Journal of Biological Chemistry. 272 (2): 1101–1109. doi:10.1074/jbc.272.2.1101. PMID 8995409.
  • Méthot N, Rom E, Olsen H, Sonenberg N (January 1997). "The human homologue of the yeast Prt1 protein is an integral part of the eukaryotic initiation factor 3 complex and interacts with p170". The Journal of Biological Chemistry. 272 (2): 1110–1116. doi:10.1074/jbc.272.2.1110. PMID 8995410.
  • Block KL, Vornlocher HP, Hershey JW (November 1998). "Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3". The Journal of Biological Chemistry. 273 (48): 31901–31908. doi:10.1074/jbc.273.48.31901. PMID 9822659.
  • Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, et al. (December 1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–495. Bibcode:1999Natur.402..489D. doi:10.1038/990031. PMID 10591208.
  • Asano K, Shalev A, Phan L, Nielsen K, Clayton J, Valásek L, et al. (May 2001). "Multiple roles for the C-terminal domain of eIF5 in translation initiation complex assembly and GTPase activation". The EMBO Journal. 20 (9): 2326–2337. doi:10.1093/emboj/20.9.2326. PMC 125443. PMID 11331597.
  • 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". Cellular Signalling. 13 (5): 345–352. doi:10.1016/S0898-6568(01)00141-3. PMID 11369516.
  • Morris-Desbois C, Réty S, Ferro M, Garin J, Jalinot P (December 2001). "The human protein HSPC021 interacts with Int-6 and is associated with eukaryotic translation initiation factor 3". The Journal of Biological Chemistry. 276 (49): 45988–45995. doi:10.1074/jbc.M104966200. PMID 11590142.
  • 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". European Journal of Biochemistry. 270 (20): 4133–4139. doi:10.1046/j.1432-1033.2003.03807.x. PMID 14519125.
  • Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, et al. (2004). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biology. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
  • Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, et al. (January 2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nature Biotechnology. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
  • Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  • v
  • t
  • e
Proteins
Initiation factor
Bacterial
Mitochondrial
Archaeal
  • aIF1
  • aIF2
  • aIF5
  • aIF6
Eukaryotic
eIF1
eIF2
eIF3
eIF4
eIF5
eIF6
Elongation factor
Bacterial/​Mitochondrial
Archaeal/​Eukaryotic
Release factor
Ribosomal Proteins
Cytoplasmic
60S subunit
40S subunit
Mitochondrial
39S subunit
28S subunit
Other concepts
Stub icon

This article on a gene on human chromosome 22 is a stub. You can help Wikipedia by expanding it.

  • v
  • t
  • e