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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

IGKV1D-13  -  immunoglobulin kappa variable 1D-13

Homo sapiens

Synonyms: IGKV1D13, L18
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Disease relevance of IGKV1D-13


High impact information on IGKV1D-13

  • Analysis of sequence covariation using the entire RNase P RNA data set reveals elements of tertiary structure in the RNA; the third nucleotides (underlined) of the GNRA tetraloops L14 and L18 are seen to interact with adjacent Watson-Crick base pairs in helix P8, forming A:G/C or G:A/U base triples [4].
  • Overexpression of L18 may promote protein synthesis and cell growth in certain cancerous tissue through inhibition of PKR activity [1].
  • Overexpression of L18 by transient DNA transfection reduced eIF-2alpha phosphorylation and stimulated translation of a reporter gene in vivo [1].
  • Muramyl dipeptide (MDP)-Lys (L18), a synthetic MDP analogue derived from bacterial cell walls, has been reported to be a potent immunoadjuvant that enhances protective immunity against pathogens and tumors by stimulating immune-competent cells, such as monocytes and macrophages [5].
  • Of the other proteins, S3 and S7 from the small subunit and proteins L6, L18, L19 and L35 from the large subunit were predominantly phosphorylated by the cyclic AMP-dependent enzyme [6].

Chemical compound and disease context of IGKV1D-13


Biological context of IGKV1D-13


Anatomical context of IGKV1D-13

  • Ribosomes from H. marismortui, however, released an RNA.protein complex containing a single protein (L18) that is homologous to the single protein found in the eukaryotic 5S ribonucleoprotein complexes [8].

Associations of IGKV1D-13 with chemical compounds

  • Furthermore, it was found that omission of veratryl alcohol addition to the culture did not affect the levels of the L18-related transcripts in carbon-limited cultures [9].

Analytical, diagnostic and therapeutic context of IGKV1D-13

  • N-terminal sequence analyses of the halophilic 5S RNA-binding proteins suggest that the L18 protein primary structure is highly conserved, with only the H. marismortui protein having a sequence difference in at least the first twenty amino acids [8].


  1. Double-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18. Kumar, K.U., Srivastava, S.P., Kaufman, R.J. Mol. Cell. Biol. (1999) [Pubmed]
  2. Intrapleural therapy with MDP-Lys (L18), a synthetic derivative of muramyl dipeptide, against malignant pleurisy associated with lung cancer. Yanagawa, H., Haku, T., Takeuchi, E., Suzuki, Y., Nokihara, H., Sone, S. Lung Cancer (2000) [Pubmed]
  3. Restorative effect of MDP-Lys (L18) on leukopenia of cancer patient treated with radiotherapy. Okawa, T., Kikuchi, Y., Watarai, J., Dokiya, T., Tanaka, T., Saito, Y., Hirokawa, Y., Takegawa, Y., Hata, K. Nippon Igaku Hoshasen Gakkai zasshi. Nippon acta radiologica. (1988) [Pubmed]
  4. Comparative analysis of ribonuclease P RNA using gene sequences from natural microbial populations reveals tertiary structural elements. Brown, J.W., Nolan, J.M., Haas, E.S., Rubio, M.A., Major, F., Pace, N.R. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  5. Muramyl dipeptide-Lys stimulates the function of human dendritic cells. Todate, A., Suda, T., Kuwata, H., Chida, K., Nakamura, H. J. Leukoc. Biol. (2001) [Pubmed]
  6. Comparison of phosphorylation of ribosomal proteins from HeLa and Krebs II ascites-tumour cells by cyclic AMP-dependent and cyclic GMP-dependent protein kinases. Issinger, O.G., Beier, H., Speichermann, N., Flokerzi, V., Hofmann, F. Biochem. J. (1980) [Pubmed]
  7. Nucleotide and deduced amino acid sequence of human ribosomal protein L18. Puder, M., Barnard, G.F., Staniunas, R.J., Steele, G.D., Chen, L.B. Biochim. Biophys. Acta (1993) [Pubmed]
  8. Comparative analysis of the protein components from 5S rRNA.protein complexes of halophilic archaebacteria. McDougall, J., Wittmann-Liebold, B. Eur. J. Biochem. (1994) [Pubmed]
  9. Methods to investigate the expression of lignin peroxidase genes by the white rot fungus Phanerochaete chrysosporium. Reiser, J., Walther, I.S., Fraefel, C., Fiechter, A. Appl. Environ. Microbiol. (1993) [Pubmed]
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