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

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Gene Review: 

UGGT2  -  UDP-glucose glycoprotein...

Homo sapiens

Synonyms: FLJ10873, FLJ11485, HUGT2, MGC117360, MGC150689, ...
 
 
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High impact information on UGCGL2

  • In this report we demonstrate that HUGT2 is localized to the ER in a manner that overlaps the distribution of HUGT1 [1].
  • HUGT1 and HUGT2 mRNAs are broadly expressed in multiple tissues and differ slightly in their tissue distribution [2].
  • Conjugases such as UDP- glucuronosyltransferases with substrates 3-OH benzo(a)pyrene (UGT1) and 4-hydroxybiphenyl (UGT2) and glutathione S-transferase (GST) with substrate 1-chloro-2,4-dinitrobenzene were higher by 72, 69, and 33% in RF and 28, 38, and 24% in rRF groups, respectively [3].
 

Biological context of UGCGL2

  • The results indicate that the amino-terminal 80% of HUGT1 is required for activation of the catalytic domain, whereas the homologous portion of HUGT2 cannot provide this function [1].
  • The HUGT1 and HUGT2 cDNAs were expressed by transient transfection in COS-1 monkey cells to obtain similar levels of protein localized to the ER [2].

References

  1. The noncatalytic portion of human UDP-glucose: glycoprotein glucosyltransferase I confers UDP-glucose binding and transferase function to the catalytic domain. Arnold, S.M., Kaufman, R.J. J. Biol. Chem. (2003) [Pubmed]
  2. Two homologues encoding human UDP-glucose:glycoprotein glucosyltransferase differ in mRNA expression and enzymatic activity. Arnold, S.M., Fessler, L.I., Fessler, J.H., Kaufman, R.J. Biochemistry (2000) [Pubmed]
  3. Malnutrition sequela on the drug metabolizing enzymes in male Holtzman rats. Reen, R.K., Melo, G.E., Moraes-Santos, T. J. Nutr. Biochem. (1999) [Pubmed]
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