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

Consensus Sequence

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Disease relevance of Consensus Sequence


High impact information on Consensus Sequence


Chemical compound and disease context of Consensus Sequence


Biological context of Consensus Sequence


Anatomical context of Consensus Sequence


Associations of Consensus Sequence with chemical compounds

  • All of the mutations that reduce competition involve base changes that decrease homology to a eucaryotic tRNA consensus sequence in the highly conserved D and T psi regions [26].
  • NF-kappaB specifically recognizes kappaB DNA elements with a consensus sequence of 5'-GGGRNYYYCC-3' (R is an unspecified purine; Y is an unspecified pyrimidine; and N is any nucleotide) [27].
  • The third histidine (His 102) forms part of a consensus sequence, shared not only by the members of the astacin family, but also by otherwise sequentially unrelated proteinases, such as vertebrate collagenases [28].
  • Conversion of the consensus sequence surrounding serine 1506 to one more favorable for cA-PK enhanced modulation of sodium currents by cA-PK [29].
  • No consensus sequence for a tyrosine kinase was present in the cytoplasmic domain [30].

Gene context of Consensus Sequence


Analytical, diagnostic and therapeutic context of Consensus Sequence


  1. Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III. Affholter, J.A., Fried, V.A., Roth, R.A. Science (1988) [Pubmed]
  2. Random peptide libraries: a source of specific protein binding molecules. Devlin, J.J., Panganiban, L.C., Devlin, P.E. Science (1990) [Pubmed]
  3. A plant viral coat protein RNA binding consensus sequence contains a crucial arginine. Ansel-McKinney, P., Scott, S.W., Swanson, M., Ge, X., Gehrke, L. EMBO J. (1996) [Pubmed]
  4. Hypoxia stimulates insulin-like growth factor binding protein 1 (IGFBP-1) gene expression in HepG2 cells: a possible model for IGFBP-1 expression in fetal hypoxia. Tazuke, S.I., Mazure, N.M., Sugawara, J., Carland, G., Faessen, G.H., Suen, L.F., Irwin, J.C., Powell, D.R., Giaccia, A.J., Giudice, L.C. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  5. Mutations causing hemophilia B: direct estimate of the underlying rates of spontaneous germ-line transitions, transversions, and deletions in a human gene. Koeberl, D.D., Bottema, C.D., Ketterling, R.P., Bridge, P.J., Lillicrap, D.P., Sommer, S.S. Am. J. Hum. Genet. (1990) [Pubmed]
  6. Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer. Deo, R.C., Groft, C.M., Rajashankar, K.R., Burley, S.K. Cell (2002) [Pubmed]
  7. The Arabidopsis NPR1 gene that controls systemic acquired resistance encodes a novel protein containing ankyrin repeats. Cao, H., Glazebrook, J., Clarke, J.D., Volko, S., Dong, X. Cell (1997) [Pubmed]
  8. tRNA ligase is required for regulated mRNA splicing in the unfolded protein response. Sidrauski, C., Cox, J.S., Walter, P. Cell (1996) [Pubmed]
  9. A novel gene, Translin, encodes a recombination hotspot binding protein associated with chromosomal translocations. Aoki, K., Suzuki, K., Sugano, T., Tasaka, T., Nakahara, K., Kuge, O., Omori, A., Kasai, M. Nat. Genet. (1995) [Pubmed]
  10. Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Miyashita, T., Reed, J.C. Cell (1995) [Pubmed]
  11. trans activation of gene expression by v-myb. Ibanez, C.E., Lipsick, J.S. Mol. Cell. Biol. (1990) [Pubmed]
  12. Simultaneous expression of salivary and pancreatic amylase genes in cultured mouse hepatoma cells. Darlington, G.J., Tsai, C.C., Samuelson, L.C., Gumucio, D.L., Meisler, M.H. Mol. Cell. Biol. (1986) [Pubmed]
  13. Preferential transcription of rabbit Aldh1a1 in the cornea: implication of hypoxia-related pathways. Hough, R.B., Piatigorsky, J. Mol. Cell. Biol. (2004) [Pubmed]
  14. MAK3 encodes an N-acetyltransferase whose modification of the L-A gag NH2 terminus is necessary for virus particle assembly. Tercero, J.C., Wickner, R.B. J. Biol. Chem. (1992) [Pubmed]
  15. Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites. Poulin, R., Lu, L., Ackermann, B., Bey, P., Pegg, A.E. J. Biol. Chem. (1992) [Pubmed]
  16. The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide. Connolly, T., Gilmore, R. Cell (1989) [Pubmed]
  17. Negative regulation of mitosis by wee1+, a gene encoding a protein kinase homolog. Russell, P., Nurse, P. Cell (1987) [Pubmed]
  18. Self-splicing of group II introns in vitro: lariat formation and 3' splice site selection in mutant RNAs. Schmelzer, C., Müller, M.W. Cell (1987) [Pubmed]
  19. Erythroid transcription factor GATA-1 is abundantly transcribed in mouse testis. Ito, E., Toki, T., Ishihara, H., Ohtani, H., Gu, L., Yokoyama, M., Engel, J.D., Yamamoto, M. Nature (1993) [Pubmed]
  20. The elav gene product of Drosophila, required in neurons, has three RNP consensus motifs. Robinow, S., Campos, A.R., Yao, K.M., White, K. Science (1988) [Pubmed]
  21. Molecular characterization of abLIM, a novel actin-binding and double zinc finger protein. Roof, D.J., Hayes, A., Adamian, M., Chishti, A.H., Li, T. J. Cell Biol. (1997) [Pubmed]
  22. The fourth immunoglobulin-like domain of NCAM contains a carbohydrate recognition domain for oligomannosidic glycans implicated in association with L1 and neurite outgrowth. Horstkorte, R., Schachner, M., Magyar, J.P., Vorherr, T., Schmitz, B. J. Cell Biol. (1993) [Pubmed]
  23. IFN consensus sequence binding protein potentiates STAT1-dependent activation of IFNgamma-responsive promoters in macrophages. Contursi, C., Wang, I.M., Gabriele, L., Gadina, M., O'Shea, J., Morse, H.C., Ozato, K. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  24. Sculpting of the spliceosomal branch site recognition motif by a conserved pseudouridine. Newby, M.I., Greenbaum, N.L. Nat. Struct. Biol. (2002) [Pubmed]
  25. Sequence-specific DNA-binding proteins are components of a nuclear matrix-attachment site. Dworetzky, S.I., Wright, K.L., Fey, E.G., Penman, S., Lian, J.B., Stein, J.L., Stein, G.S. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  26. The promoter sequence of a yeast tRNAtyr gene. Allison, D.S., Goh, S.H., Hall, B.D. Cell (1983) [Pubmed]
  27. Crystal structure of p50/p65 heterodimer of transcription factor NF-kappaB bound to DNA. Chen, F.E., Huang, D.B., Chen, Y.Q., Ghosh, G. Nature (1998) [Pubmed]
  28. Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases. Bode, W., Gomis-Rüth, F.X., Huber, R., Zwilling, R., Stöcker, W. Nature (1992) [Pubmed]
  29. Convergent regulation of sodium channels by protein kinase C and cAMP-dependent protein kinase. Li, M., West, J.W., Numann, R., Murphy, B.J., Scheuer, T., Catterall, W.A. Science (1993) [Pubmed]
  30. Cloning of an interleukin-3 receptor gene: a member of a distinct receptor gene family. Itoh, N., Yonehara, S., Schreurs, J., Gorman, D.M., Maruyama, K., Ishii, A., Yahara, I., Arai, K., Miyajima, A. Science (1990) [Pubmed]
  31. Structural basis for self-association and receptor recognition of human TRAF2. Park, Y.C., Burkitt, V., Villa, A.R., Tong, L., Wu, H. Nature (1999) [Pubmed]
  32. The RNA component of telomerase is mutated in autosomal dominant dyskeratosis congenita. Vulliamy, T., Marrone, A., Goldman, F., Dearlove, A., Bessler, M., Mason, P.J., Dokal, I. Nature (2001) [Pubmed]
  33. Bent DNA at a yeast autonomously replicating sequence. Snyder, M., Buchman, A.R., Davis, R.W. Nature (1986) [Pubmed]
  34. Transcriptional regulation of a yeast HSP70 gene by heat shock factor and an upstream repression site-binding factor. Park, H.O., Craig, E.A. Genes Dev. (1991) [Pubmed]
  35. The interleukin 12 p40 gene promoter is primed by interferon gamma in monocytic cells. Ma, X., Chow, J.M., Gri, G., Carra, G., Gerosa, F., Wolf, S.F., Dzialo, R., Trinchieri, G. J. Exp. Med. (1996) [Pubmed]
  36. TLS/FUS, a pro-oncogene involved in multiple chromosomal translocations, is a novel regulator of BCR/ABL-mediated leukemogenesis. Perrotti, D., Bonatti, S., Trotta, R., Martinez, R., Skorski, T., Salomoni, P., Grassilli, E., Lozzo, R.V., Cooper, D.R., Calabretta, B. EMBO J. (1998) [Pubmed]
  37. Apolipoprotein E variation at the sequence haplotype level: implications for the origin and maintenance of a major human polymorphism. Fullerton, S.M., Clark, A.G., Weiss, K.M., Nickerson, D.A., Taylor, S.L., Stengârd, J.H., Salomaa, V., Vartiainen, E., Perola, M., Boerwinkle, E., Sing, C.F. Am. J. Hum. Genet. (2000) [Pubmed]
  38. The RNA-binding SAM domain of Smaug defines a new family of post-transcriptional regulators. Aviv, T., Lin, Z., Lau, S., Rendl, L.M., Sicheri, F., Smibert, C.A. Nat. Struct. Biol. (2003) [Pubmed]
  39. Clonal variability in beta-globin mRNA content in an interleukin-3-dependent bone marrow cell line transfected with the erythropoietin receptor before and after stimulation with erythropoietin. Ishiguro, K., Sartorelli, A.C. Blood (1997) [Pubmed]
  40. Characterization of recombinant amino-terminal NC4 domain of human collagen IX: interaction with glycosaminoglycans and cartilage oligomeric matrix protein. Pihlajamaa, T., Lankinen, H., Ylöstalo, J., Valmu, L., Jäälinoja, J., Zaucke, F., Spitznagel, L., Gösling, S., Puustinen, A., Mörgelin, M., Peränen, J., Maurer, P., Ala-Kokko, L., Kilpelaïnen, I. J. Biol. Chem. (2004) [Pubmed]
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