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Gene Review

KARS  -  lysyl-tRNA synthetase

Homo sapiens

Synonyms: CMTRIB, DFNB89, KARS1, KARS2, KIAA0070, ...
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Disease relevance of KARS


High impact information on KARS


Biological context of KARS


Anatomical context of KARS


Associations of KARS with chemical compounds

  • Even though eukaryotic lysine tRNAs also encode G73, the motif 2 loop sequence of lysyl-tRNA synthetase differs at multiple positions from that of the aspartate enzyme [2].
  • In confirmation of this idea, we found that newly synthesized LysRS is associated with Gag after a 10-min pulse with [(35)S]cysteine/methionine [11].
  • Using data recently obtained from the emerging genome projects, our analysis points to the extant forms of lysyl-tRNA synthetase being preceded in evolution by the establishment of the identity of lysine tRNA [13].
  • Here we describe the systematic substitution of the 13 lysine or arginine residues located within the general RNA-binding domain of hamster LysRS made of 70 residues [14].
  • Gag alone is sufficient for packaging of LysRS, and these two proteins have been shown to interact in vitro using glutathione S-transferase pull-down assays [8].

Other interactions of KARS

  • Significant sequence similarities between KARS and ADAT1 are apparent within their substrate interaction domains [15].
  • In addition to its contribution to the translation process, LysRS also takes part in the regulation of MITF and USF2 target genes [12].
  • This same organization is conserved at the human Rap1-KARS locus [16].
  • By using the yeast two-hybrid system, Lys-tRNA synthetase (LysRS) was identified as a Vpr-interacting protein [7].
  • Assignment of two human autoantigen genes-isoleucyl-tRNA synthetase locates to 9q21 and lysyl-tRNA synthetase locates to 16q23-q24 [17].

Analytical, diagnostic and therapeutic context of KARS

  • Gel chromatography studies further support the formation of a Gag/LysRS heterodimer [8].
  • Functional dissection of the eukaryotic-specific tRNA-interacting factor of lysyl-tRNA synthetase [14].
  • OBJECTIVES: To determine the seroprevalence of diphtheria in 767 children aged 0-6 years and to identify the relationship between diphtheria seroprevalence and several sociodemographic characteristics of the study subjects in the Erzurum, Erzincan and Kars cities situated in Eastern Turkey [18].


  1. The interaction between HIV-1 Gag and human lysyl-tRNA synthetase during viral assembly. Javanbakht, H., Halwani, R., Cen, S., Saadatmand, J., Musier-Forsyth, K., Gottlinger, H., Kleiman, L. J. Biol. Chem. (2003) [Pubmed]
  2. Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant. Shiba, K., Stello, T., Motegi, H., Noda, T., Musier-Forsyth, K., Schimmel, P. J. Biol. Chem. (1997) [Pubmed]
  3. Incorporation of lysyl-tRNA synthetase into human immunodeficiency virus type 1. Cen, S., Khorchid, A., Javanbakht, H., Gabor, J., Stello, T., Shiba, K., Musier-Forsyth, K., Kleiman, L. J. Virol. (2001) [Pubmed]
  4. A euryarchaeal lysyl-tRNA synthetase: resemblance to class I synthetases. Ibba, M., Morgan, S., Curnow, A.W., Pridmore, D.R., Vothknecht, U.C., Gardner, W., Lin, W., Woese, C.R., Söll, D. Science (1997) [Pubmed]
  5. Reaction of anti-OJ autoantibodies with components of the multi-enzyme complex of aminoacyl-tRNA synthetases in addition to isoleucyl-tRNA synthetase. Targoff, I.N., Trieu, E.P., Miller, F.W. J. Clin. Invest. (1993) [Pubmed]
  6. Human lysyl-tRNA synthetase is secreted to trigger proinflammatory response. Park, S.G., Kim, H.J., Min, Y.H., Choi, E.C., Shin, Y.K., Park, B.J., Lee, S.W., Kim, S. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  7. Human immunodeficiency virus type 1 (HIV-1) viral protein R (Vpr) interacts with Lys-tRNA synthetase: implications for priming of HIV-1 reverse transcription. Stark, L.A., Hay, R.T. J. Virol. (1998) [Pubmed]
  8. In vitro characterization of the interaction between HIV-1 Gag and human lysyl-tRNA synthetase. Kovaleski, B.J., Kennedy, R., Hong, M.K., Datta, S.A., Kleiman, L., Rein, A., Musier-Forsyth, K. J. Biol. Chem. (2006) [Pubmed]
  9. The N-terminal domain of mammalian Lysyl-tRNA synthetase is a functional tRNA-binding domain. Francin, M., Kaminska, M., Kerjan, P., Mirande, M. J. Biol. Chem. (2002) [Pubmed]
  10. Inhibition of cellular HIV-1 protease activity by lysyl-tRNA synthetase. Guo, F., Gabor, J., Cen, S., Hu, K., Mouland, A.J., Kleiman, L. J. Biol. Chem. (2005) [Pubmed]
  11. Cellular distribution of Lysyl-tRNA synthetase and its interaction with Gag during human immunodeficiency virus type 1 assembly. Halwani, R., Cen, S., Javanbakht, H., Saadatmand, J., Kim, S., Shiba, K., Kleiman, L. J. Virol. (2004) [Pubmed]
  12. Translation and Transcription: the Dual Functionality of LysRS in Mast Cells. Yannay-Cohen, N., Razin, E. Mol. Cells (2006) [Pubmed]
  13. Genetic code origins: tRNAs older than their synthetases? Ribas de Pouplana, L., Turner, R.J., Steer, B.A., Schimmel, P. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  14. Functional dissection of the eukaryotic-specific tRNA-interacting factor of lysyl-tRNA synthetase. Francin, M., Mirande, M. J. Biol. Chem. (2003) [Pubmed]
  15. Genomic clustering of tRNA-specific adenosine deaminase ADAT1 and two tRNA synthetases. Maas, S., Kim, Y.G., Rich, A. Mamm. Genome (2001) [Pubmed]
  16. The telomeric protein Rap1 is conserved in vertebrates and is expressed from a bidirectional promoter positioned between the Rap1 and KARS genes. Tan, M., Wei, C., Price, C.M. Gene (2003) [Pubmed]
  17. Assignment of two human autoantigen genes-isoleucyl-tRNA synthetase locates to 9q21 and lysyl-tRNA synthetase locates to 16q23-q24. Nichols, R.C., Blinder, J., Pai, S.I., Ge, Q., Targoff, I.N., Plotz, P.H., Liu, P. Genomics (1996) [Pubmed]
  18. Diphtheria seroprevalence in children living in the eastern Turkey. Altinkaynak, S., Ertekin, V., Arik, A., Guraksin, A. East African medical journal. (2003) [Pubmed]
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