EEF1A2

Protein-coding gene in the species Homo sapiens
EEF1A2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4C0S, 3C5J

Identifiers
AliasesEEF1A2, EEF1AL, EF-1-alpha-2, EF1A, HS1, STN, STNL, EIEE33, MRD38, eukaryotic translation elongation factor 1 alpha 2, DEE33
External IDsOMIM: 602959; MGI: 1096317; HomoloGene: 121568; GeneCards: EEF1A2; OMA:EEF1A2 - orthologs
Gene location (Human)
Chromosome 20 (human)
Chr.Chromosome 20 (human)[1]
Chromosome 20 (human)
Genomic location for EEF1A2
Genomic location for EEF1A2
Band20q13.33Start63,488,013 bp[1]
End63,499,239 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for EEF1A2
Genomic location for EEF1A2
Band2 H4|2 103.6 cMStart180,789,446 bp[2]
End180,798,807 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • gastrocnemius muscle

  • apex of heart

  • muscle of thigh

  • paraflocculus of cerebellum

  • right hemisphere of cerebellum

  • frontal pole

  • thoracic diaphragm

  • Skeletal muscle tissue of rectus abdominis

  • Brodmann area 10

  • cerebellar vermis
Top expressed in
  • perirhinal cortex

  • entorhinal cortex

  • CA3 field

  • primary motor cortex

  • subiculum

  • superior colliculus

  • habenula

  • prefrontal cortex

  • pontine nuclei

  • triceps brachii muscle
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • nucleotide binding
  • GTP binding
  • translation factor activity, RNA binding
  • protein binding
  • protein kinase binding
  • GTPase activity
  • translation elongation factor activity
Cellular component
  • myelin sheath
  • neuronal cell body
  • cytoplasmic side of lysosomal membrane
  • nucleus
  • eukaryotic translation elongation factor 1 complex
  • cytoplasm
  • synapse
Biological process
  • positive regulation of apoptotic process
  • regulation of chaperone-mediated autophagy
  • translational elongation
  • positive regulation of lipid kinase activity
  • response to electrical stimulus
  • protein biosynthesis
  • response to inorganic substance
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

1917

13628

Ensembl

ENSG00000101210

ENSMUSG00000016349

UniProt

Q05639

P62631

RefSeq (mRNA)

NM_001958

NM_007906

RefSeq (protein)

NP_001949

NP_031932

Location (UCSC)Chr 20: 63.49 – 63.5 MbChr 2: 180.79 – 180.8 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Elongation factor 1-alpha 2 is a protein that in humans is encoded by the EEF1A2 gene.[5][6][7]

Function

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 2) is expressed in brain, heart and skeletal muscle, and the other isoform (alpha 1) is expressed in brain, placenta, lung, liver, kidney, and pancreas.

Clinical significance

This gene may be critical in the development of ovarian cancer.[7]

Regulation

EEF1A2 is a direct target of miRNA-663 and miRNA-744.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000101210 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000016349 – 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. ^ Knudsen SM, Frydenberg J, Clark BF, Leffers H (Sep 1993). "Tissue-dependent variation in the expression of elongation factor-1 alpha isoforms: isolation and characterisation of a cDNA encoding a novel variant of human elongation-factor 1 alpha". Eur J Biochem. 215 (3): 549–54. doi:10.1111/j.1432-1033.1993.tb18064.x. PMID 8354261.
  6. ^ Lund A, Knudsen SM, Vissing H, Clark B, Tommerup N (Jan 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.
  7. ^ a b "Entrez Gene: EEF1A2 eukaryotic translation elongation factor 1 alpha 2".
  8. ^ Vislovukh A, Kratassiouk G, Porto E, Gralievska N, Beldiman C, Pinna G, El'skaya A, Harel-Bellan A, Negrutskii B, Groisman I (11 June 2013). "Proto-oncogenic isoform A2 of eukaryotic translation elongation factor eEF1 is a target of miR-663 and miR-744". British Journal of Cancer. 108 (11): 2304–11. doi:10.1038/bjc.2013.243. PMC 3681015. PMID 23695020.

Further reading

  • Lee JM (2004). "The role of protein elongation factor eEF1A2 in ovarian cancer". Reprod. Biol. Endocrinol. 1: 69. doi:10.1186/1477-7827-1-69. PMC 239897. PMID 14588074.
  • Beh KJ (1976). "Immunoglobulin class specificity of non-agglutinating antibody produced in cattle following Brucella abortus 45/20 vaccination". Aust. Vet. J. 51 (10): 481–3. doi:10.1111/j.1751-0813.1975.tb02385.x. PMID 812466.
  • Lee S, Ann DK, Wang E (1994). "Cloning of human and mouse brain cDNAs coding for S1, the second member of the mammalian elongation factor-1 alpha gene family: analysis of a possible evolutionary pathway". Biochem. Biophys. Res. Commun. 203 (3): 1371–7. doi:10.1006/bbrc.1994.2336. PMID 7945283.
  • 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. doi:10.1074/jbc.271.8.4201. PMID 8626763.
  • Bischoff C, Kahns S, Lund A, Jørgensen HF, Praestegaard M, Clark BF, Leffers H (2001). "The human elongation factor 1 A-2 gene (EEF1A2): complete sequence and characterization of gene structure and promoter activity". Genomics. 68 (1): 63–70. doi:10.1006/geno.2000.6271. PMID 10950927.
  • McClatchy DB, Knudsen CR, Clark BF, Kahn RA, Hall RA, Levey AI (2002). "Novel interaction between the M4 muscarinic acetylcholine receptor and elongation factor 1A2". J. Biol. Chem. 277 (32): 29268–74. doi:10.1074/jbc.M203081200. PMID 12048193.
  • Anand N, Murthy S, Amann G, Wernick M, Porter LA, Cukier IH, Collins C, Gray JW, Diebold J, Demetrick DJ, Lee JM (2002). "Protein elongation factor EEF1A2 is a putative oncogene in ovarian cancer". Nat. Genet. 31 (3): 301–5. doi:10.1038/ng904. PMID 12053177. S2CID 37997742.
  • Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
  • 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.
  • Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
  • Byun HM, Suh D, Jeong Y, Wee HS, Kim JM, Kim WK, Ko JJ, Kim JS, Lee YB, Oh YK (2005). "Plasmid vectors harboring cellular promoters can induce prolonged gene expression in hematopoietic and mesenchymal progenitor cells". Biochem. Biophys. Res. Commun. 332 (2): 518–23. doi:10.1016/j.bbrc.2005.04.155. PMID 15893736.
  • Ahmed M, Forsberg J, Bergsten P (2005). "Protein profiling of human pancreatic islets by two-dimensional gel electrophoresis and mass spectrometry". J. Proteome Res. 4 (3): 931–40. doi:10.1021/pr050024a. PMID 15952740.
  • Tomlinson VA, Newbery HJ, Wray NR, Jackson J, Larionov A, Miller WR, Dixon JM, Abbott CM (2006). "Translation elongation factor eEF1A2 is a potential oncoprotein that is overexpressed in two-thirds of breast tumours". BMC Cancer. 5: 113. doi:10.1186/1471-2407-5-113. PMC 1236916. PMID 16156888.
  • Li R, Wang H, Bekele BN, Yin Z, Caraway NP, Katz RL, Stass SA, Jiang F (2006). "Identification of putative oncogenes in lung adenocarcinoma by a comprehensive functional genomic approach". Oncogene. 25 (18): 2628–35. doi:10.1038/sj.onc.1209289. PMID 16369491. S2CID 3101952.

External links

  • Overview of all the structural information available in the PDB for UniProt: Q05639 (Elongation factor 1-alpha 2) at the PDBe-KB.
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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


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