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Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

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EEF1A1

Introduction

Eukaryotic translation elongation factor 1 alpha 1, also known as EEF1A1, is a human gene.

This gene encodes an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible for the enzymatic delivery of aminoacyl tRNAs to the ribosome. This isoform (alpha 1) is expressed in brain, placenta, lung, liver, kidney, and pancreas, and the other isoform (alpha 2) is expressed in brain, heart and skeletal muscle. This isoform is identified as an autoantigen in 66% of patients with Felty syndrome. This gene has been found to have multiple copies on many chromosomes, some of which, if not all, represent different pseudogenes.[1]

References

References

  1. ↑ “Entrez Gene: EEF1A1 eukaryotic translation elongation factor 1 alpha 1”.
Further reading

Further reading

  • Madsen HO, Poulsen K, Dahl O; et al. (1990). “Retropseudogenes constitute the major part of the human elongation factor 1 alpha gene family”. Nucleic Acids Res. 18 (6): 1513–6. PMID 2183196.
  • Bec G, Kerjan P, Zha XD, Waller JP (1990). “Valyl-tRNA synthetase from rabbit liver. I. Purification as a heterotypic complex in association with elongation factor 1”. J. Biol. Chem. 264 (35): 21131–7. PMID 2556394.
  • Uetsuki T, Naito A, Nagata S, Kaziro Y (1989). “Isolation and characterization of the human chromosomal gene for polypeptide chain elongation factor-1 alpha”. J. Biol. Chem. 264 (10): 5791–8. PMID 2564392.
  • Whiteheart SW, Shenbagamurthi P, Chen L; et al. (1989). “Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha”. J. Biol. Chem. 264 (24): 14334–41. PMID 2569467.
  • Motorin YuA , Wolfson AD, Orlovsky AF, Gladilin KL (1988). “Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor”. FEBS Lett. 238 (2): 262–4. PMID 3169261.
  • Ann DK, Wu MM, Huang T; et al. (1988). “Retinol-regulated gene expression in human tracheobronchial epithelial cells. Enhanced expression of elongation factor EF-1 alpha”. J. Biol. Chem. 263 (8): 3546–9. PMID 3346208.
  • Brands JH, Maassen JA, van Hemert FJ; et al. (1986). “The primary structure of the alpha subunit of human elongation factor 1. Structural aspects of guanine-nucleotide-binding sites”. Eur. J. Biochem. 155 (1): 167–71. PMID 3512269.
  • Opdenakker G, Cabeza-Arvelaiz Y, Fiten P; et al. (1987). “Human elongation factor 1 alpha: a polymorphic and conserved multigene family with multiple chromosomal localizations”. Hum. Genet. 75 (4): 339–44. PMID 3570288.
  • Rao TR, Slobin LI (1986). “Structure of the amino-terminal end of mammalian elongation factor Tu”. Nucleic Acids Res. 14 (5): 2409. PMID 3960725.
  • Carvalho MD, Carvalho JF, Merrick WC (1984). “Biological characterization of various forms of elongation factor 1 from rabbit reticulocytes”. Arch. Biochem. Biophys. 234 (2): 603–11. PMID 6568109.
  • Shen R, Su ZZ, Olsson CA, Fisher PB (1995). “Identification of the human prostatic carcinoma oncogene PTI-1 by rapid expression cloning and differential RNA display”. Proc. Natl. Acad. Sci. U.S.A. 92 (15): 6778–82. PMID 7542776.
  • Reed VS, Wastney ME, Yang DC (1995). “Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1 alpha”. J. Biol. Chem. 269 (52): 32932–6. PMID 7806521.
  • Kielbassa K, Müller HJ, Meyer HE; et al. (1995). “Protein kinase C delta-specific phosphorylation of the elongation factor eEF-alpha and an eEF-1 alpha peptide at threonine 431”. J. Biol. Chem. 270 (11): 6156–62. PMID 7890750.
  • 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. PMID 8125298.
  • Wu-Baer F, Lane WS, Gaynor RB (1996). “Identification of a group of cellular cofactors that stimulate the binding of RNA polymerase II and TRP-185 to human immunodeficiency virus 1 TAR RNA”. J. Biol. Chem. 271 (8): 4201–8. PMID 8626763.
  • Sanders J, Brandsma M, Janssen GM; et al. (1996). “Immunofluorescence studies of human fibroblasts demonstrate the presence of the complex of elongation factor-1 beta gamma delta in the endoplasmic reticulum”. J. Cell. Sci. 109 ( Pt 5): 1113–7. PMID 8743958.
  • Lund A, Knudsen SM, Vissing H; et al. (1997). “Assignment of human elongation factor 1alpha genes: EEF1A maps to chromosome 6q14 and EEF1A2 to 20q13.3”. Genomics. 36 (2): 359–61. doi:10.1006/geno.1996.0475. PMID 8812466.
  • Welle S, Thornton C, Bhatt K, Krym M (1997). “Expression of elongation factor-1 alpha and S1 in young and old human skeletal muscle”. J. Gerontol. A Biol. Sci. Med. Sci. 52 (5): B235–9. PMID 9310071.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). “Construction and characterization of a full length-enriched and a 5′-end-enriched cDNA library”. Gene. 200 (1–2): 149–56. PMID 9373149.
  • Sheu GT, Traugh JA (1998). “Recombinant subunits of mammalian elongation factor 1 expressed in Escherichia coli. Subunit interactions, elongation activity, and phosphorylation by protein kinase CKII”. J. Biol. Chem. 272 (52): 33290–7. PMID 9407120.

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