GBP2

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
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RefSeq (mRNA)

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RefSeq (protein)

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Interferon-induced guanylate-binding protein 2 is a protein that in humans is encoded by the GBP2 gene.[1][2]

Function

Interferons are cytokines that have antiviral effects and inhibit tumor cell proliferation. They induce a large number of genes in their target cells, including those coding for the guanylate-binding proteins (GBPs). GBPs are characterized by their ability to specifically bind guanine nucleotides (GMP, GDP, and GTP). The protein encoded by this gene is a GTPase that converts GTP to GDP and GMP.[2]

References

  1. Cheng YS, Patterson CE, Staeheli P (Sep 1991). "Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus motif and bind GMP in addition to GDP and GTP". Mol Cell Biol. 11 (9): 4717–25. PMC 361367. PMID 1715024.
  2. 2.0 2.1 "Entrez Gene: GBP2 guanylate binding protein 2, interferon-inducible".

Further reading

  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Neun R, Richter MF, Staeheli P, Schwemmle M (1996). "GTPase properties of the interferon-induced human guanylate-binding protein 2". FEBS Lett. 390 (1): 69–72. doi:10.1016/0014-5793(96)00628-X. PMID 8706832.
  • Nitsche EM, Moquin A, Adams PS, et al. (1996). "Differential display RT PCR of total RNA from human foreskin fibroblasts for investigation of androgen-dependent gene expression". Am. J. Med. Genet. 63 (1): 231–8. doi:10.1002/(SICI)1096-8628(19960503)63:1<231::AID-AJMG40>3.0.CO;2-M. PMID 8723115.
  • Vestal DJ, Gorbacheva VY, Sen GC (2001). "Different subcellular localizations for the related interferon-induced GTPases, MuGBP-1 and MuGBP-2: implications for different functions?". J. Interferon Cytokine Res. 20 (11): 991–1000. doi:10.1089/10799900050198435. PMID 11096456.
  • Lukasiewicz R, Velazquez-Dones A, Huynh N, et al. (2007). "Structurally unique yeast and mammalian serine-arginine protein kinases catalyze evolutionarily conserved phosphorylation reactions". J. Biol. Chem. 282 (32): 23036–43. doi:10.1074/jbc.M611305200. PMID 17517895.