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Gene Review

ASNS  -  asparagine synthetase (glutamine-hydrolyzing)

Homo sapiens

Synonyms: ASNSD, Cell cycle control protein TS11, Glutamine-dependent asparagine synthetase, TS11
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Disease relevance of ASNS


High impact information on ASNS


Chemical compound and disease context of ASNS


Biological context of ASNS


Anatomical context of ASNS


Associations of ASNS with chemical compounds


Regulatory relationships of ASNS

  • Based on sequence analysis, one of the predicted truncated proteins (ATF3deltaZip3) is likely incapable of binding DNA; and yet, exogenous expression of the cDNA enhanced starvation-induced or ATF4-activated ASNS transcription, possibly by sequestering corepressor proteins [14].

Other interactions of ASNS

  • Overexpression studies established that ATF4, ATF3-FL, and C/EBPbeta-LAP could coordinately modulate the transcription from the human ASNS promoter [11].
  • Collectively, the results provide evidence for a potential role of multiple predicted ATF3 isoforms in the transcriptional regulation of the ASNS gene in response to nutrient deprivation [14].
  • Significantly, that potentiation was >700-fold in the multidrug-resistant derivative OVCAR-8/ADR, showing that the causal relationship between ASNS expression and l-ASP activity survives development of classical multidrug resistance [3].
  • Additionally, a processed pseudogene for asparagine synthetase was found about 6 kb upstream of the GNAL gene [18].
  • We report the transactivation of two genes, asparagine synthetase and human telomerase reverse transcriptase [19].

Analytical, diagnostic and therapeutic context of ASNS


  1. Regulation of asparagine synthetase gene transcription by the basic region leucine zipper transcription factors ATF5 and CHOP. Al Sarraj, J., Vinson, C., Thiel, G. Biol. Chem. (2005) [Pubmed]
  2. Asparagine synthetase chemotherapy. Richards, N.G., Kilberg, M.S. Annu. Rev. Biochem. (2006) [Pubmed]
  3. Asparagine synthetase as a causal, predictive biomarker for L-asparaginase activity in ovarian cancer cells. Lorenzi, P.L., Reinhold, W.C., Rudelius, M., Gunsior, M., Shankavaram, U., Bussey, K.J., Scherf, U., Eichler, G.S., Martin, S.E., Chin, K., Gray, J.W., Kohn, E.C., Horak, I.D., Von Hoff, D.D., Raffeld, M., Goldsmith, P.K., Caplen, N.J., Weinstein, J.N. Mol. Cancer Ther. (2006) [Pubmed]
  4. Sexual dimorphism in body composition, weight status and growth in prepubertal school chiildren from rural areas of eastern Austria. Kirchengast, S., Steiner, V. Collegium antropologicum. (2001) [Pubmed]
  5. Isolation of human cDNAs for asparagine synthetase and expression in Jensen rat sarcoma cells. Andrulis, I.L., Chen, J., Ray, P.N. Mol. Cell. Biol. (1987) [Pubmed]
  6. Channeling of substrates and intermediates in enzyme-catalyzed reactions. Huang, X., Holden, H.M., Raushel, F.M. Annu. Rev. Biochem. (2001) [Pubmed]
  7. Dark-induced and organ-specific expression of two asparagine synthetase genes in Pisum sativum. Tsai, F.Y., Coruzzi, G.M. EMBO J. (1990) [Pubmed]
  8. Nitrogen assimilation in alfalfa: isolation and characterization of an asparagine synthetase gene showing enhanced expression in root nodules and dark-adapted leaves. Shi, L., Twary, S.N., Yoshioka, H., Gregerson, R.G., Miller, S.S., Samac, D.A., Gantt, J.S., Unkefer, P.J., Vance, C.P. Plant Cell (1997) [Pubmed]
  9. A role for asparaginyl-tRNA in the regulation of asparagine synthetase in a mammalian cell line. Arfin, S.M., Simpson, D.R., Chiang, C.S., Andrulis, I.L., Hatfield, G.W. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
  10. Alignment of the Transcription Start Site Coincides with Increased Transcriptional Activity from the Human Asparagine Synthetase Gene Following Amino Acid Deprivation of HepG2 Cells. Chen, H., Kilberg, M.S. J. Nutr. (2006) [Pubmed]
  11. Amino acid deprivation induces the transcription rate of the human asparagine synthetase gene through a timed program of expression and promoter binding of nutrient-responsive basic region/leucine zipper transcription factors as well as localized histone acetylation. Chen, H., Pan, Y.X., Dudenhausen, E.E., Kilberg, M.S. J. Biol. Chem. (2004) [Pubmed]
  12. Amino-acid limitation induces transcription from the human C/EBPbeta gene via an enhancer activity located downstream of the protein coding sequence. Chen, C., Dudenhausen, E., Chen, H., Pan, Y.X., Gjymishka, A., Kilberg, M.S. Biochem. J. (2005) [Pubmed]
  13. Cis- and trans-acting elements involved in amino acid regulation of asparagine synthetase gene expression. Guerrini, L., Gong, S.S., Mangasarian, K., Basilico, C. Mol. Cell. Biol. (1993) [Pubmed]
  14. Amino acid deprivation and endoplasmic reticulum stress induce expression of multiple activating transcription factor-3 mRNA species that, when overexpressed in HepG2 cells, modulate transcription by the human asparagine synthetase promoter. Pan, Y., Chen, H., Siu, F., Kilberg, M.S. J. Biol. Chem. (2003) [Pubmed]
  15. Refined localization of the asparagine synthetase gene (ASNS) to chromosome 7, region q21.3, and characterization of the somatic cell hybrid line 4AF/106/KO15. Heng, H.H., Shi, X.M., Scherer, S.W., Andrulis, I.L., Tsui, L.C. Cytogenet. Cell Genet. (1994) [Pubmed]
  16. Expression of human asparagine synthetase in Escherichia coli. Van Heeke, G., Schuster, S.M. J. Biol. Chem. (1989) [Pubmed]
  17. The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity. Van Heeke, G., Schuster, S.M. J. Biol. Chem. (1989) [Pubmed]
  18. Sequence and genomic organization of the human G-protein Golfalpha gene (GNAL) on chromosome 18p11, a susceptibility region for bipolar disorder and schizophrenia. Vuoristo, J.T., Berrettini, W.H., Overhauser, J., Prockop, D.J., Ferraro, T.N., Ala-Kokko, L. Mol. Psychiatry (2000) [Pubmed]
  19. Tumor-derived p53 mutants induce oncogenesis by transactivating growth-promoting genes. Scian, M.J., Stagliano, K.E., Deb, D., Ellis, M.A., Carchman, E.H., Das, A., Valerie, K., Deb, S.P., Deb, S. Oncogene (2004) [Pubmed]
  20. Accurate detection of asparagine synthetase (ASNS) using quantitative real-time PCR (qRT-PCR), without requiring DNaseI treatment. Hurteau, G.J., Broome, J.D., Brock, G.J. Leukemia (2005) [Pubmed]
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