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Gene Review

FBXL12  -  F-box and leucine-rich repeat protein 12

Gallus gallus

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Disease relevance of FBXL12

  • Thus, a replication-deficient lacZ recombinant human adenovirus, which naturally does not infect avian cells, allowed highly efficient and specific gene transfer to the liver of ducks in vivo when complexed with N-acetylglucosamine, a ligand for the chicken hepatic lectin [1].

High impact information on FBXL12


Biological context of FBXL12


Anatomical context of FBXL12


Associations of FBXL12 with chemical compounds


Analytical, diagnostic and therapeutic context of FBXL12

  • To measure intracellular EGFR sorting, we developed a novel cell fractionation assay toward which cells were co-transfected for chicken hepatic lectin, a receptor for agialoglycoproteins [15].
  • The subunit structure of soluble goat hepatic lectin was studied by determining molecular weight under nondenaturing conditions by gel filtration and denaturing conditions by SDS PAGE [16].


  1. Ligand-mediated retargeting of recombinant adenovirus for gene transfer in vivo. Thoma, C., Wieland, S., Moradpour, D., von Weizsäcker, F., Offensperger, S., Madon, J., Blum, H.E., Offensperger, W.B. Gene Ther. (2000) [Pubmed]
  2. Molecular structure of human lymphocyte receptor for immunoglobulin E. Kikutani, H., Inui, S., Sato, R., Barsumian, E.L., Owaki, H., Yamasaki, K., Kaisho, T., Uchibayashi, N., Hardy, R.R., Hirano, T. Cell (1986) [Pubmed]
  3. Human lymphocyte Fc receptor for IgE: sequence homology of its cloned cDNA with animal lectins. Ikuta, K., Takami, M., Kim, C.W., Honjo, T., Miyoshi, T., Tagaya, Y., Kawabe, T., Yodoi, J. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  4. Cloning and sequence analysis of a partial cDNA for chicken cartilage proteoglycan core protein. Sai, S., Tanaka, T., Kosher, R.A., Tanzer, M.L. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  5. Evolutionary conservation of intron position in a subfamily of genes encoding carbohydrate-recognition domains. Bezouska, K., Crichlow, G.V., Rose, J.M., Taylor, M.E., Drickamer, K. J. Biol. Chem. (1991) [Pubmed]
  6. Functional and physical molecular size of the chicken hepatic lectin determined by radiation inactivation and sedimentation equilibrium analysis. Steer, C.J., Osborne, J.C., Kempner, E.S. J. Biol. Chem. (1990) [Pubmed]
  7. Complete amino acid sequence of a membrane receptor for glycoproteins. Sequence of the chicken hepatic lectin. Drickamer, K. J. Biol. Chem. (1981) [Pubmed]
  8. The binding site of chicken hepatic lectin. Sikder, S.K., Kabat, E.A., Steer, C.J., Ashwell, G. J. Biol. Chem. (1983) [Pubmed]
  9. Phosphorylation of a membrane receptor for glycoproteins. Possible transmembrane orientation of the chicken hepatic lectin. Drickamer, K., Mamon, J.F. J. Biol. Chem. (1982) [Pubmed]
  10. Partial structure of the gene for chicken cartilage proteoglycan core protein. Tanaka, T., Har-el, R., Tanzer, M.L. J. Biol. Chem. (1988) [Pubmed]
  11. The chicken receptor for endocytosis of glycoproteins contains a cluster of N-acetylglucosamine-binding sites. Loeb, J.A., Drickamer, K. J. Biol. Chem. (1987) [Pubmed]
  12. Purification and cDNA cloning of a novel factor produced by a human T-cell hybridoma: sequence homology with animal lectins. Yoshimatsu, K., Ohya, Y., Shikata, Y., Seto, T., Hasegawa, Y., Tanaka, I., Kawamura, T., Kitoh, K., Toyoshima, S., Osawa, T. Mol. Immunol. (1992) [Pubmed]
  13. Endocytosis of N-acetylglucosamine-containing glycoproteins by rat fibroblasts expressing a single species of chicken liver glycoprotein receptor. Mellow, T.E., Halberg, D., Drickamer, K. J. Biol. Chem. (1988) [Pubmed]
  14. The partial amino acid sequence of bovine cartilage proteoglycan, deduced from a cDNA clone, contains numerous Ser-Gly sequences arranged in homologous repeats. Oldberg, A., Antonsson, P., Heinegård, D. Biochem. J. (1987) [Pubmed]
  15. Sorting of ligand-activated epidermal growth factor receptor to lysosomes requires its actin-binding domain. Stoorvogel, W., Kerstens, S., Fritzsche, I., den Hartigh, J.C., Oud, R., van der Heyden, M.A., Voortman, J., van Bergen en Henegouwen, P.M. J. Biol. Chem. (2004) [Pubmed]
  16. Subunit structure of Ca++ dependent soluble goat hepatic lectin: evidence that it has antigenic structural relationship with soluble 14K lectin family. Ali, N., Ola, S., Bhat, R. Biochem. Mol. Biol. Int. (1996) [Pubmed]
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