Difference between revisions of "YDR305C"
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− | '''Description of YDR305C:''' Dinucleoside triphosphate hydrolase; has similarity to the tumor suppressor FHIT and belongs to the histidine triad (HIT) superfamily of nucleotide-binding proteins<ref name=' | + | '''Description of YDR305C:''' Dinucleoside triphosphate hydrolase; has similarity to the tumor suppressor FHIT and belongs to the histidine triad (HIT) superfamily of nucleotide-binding proteins<ref name='S000069891'>Rubio-Texeira M, et al. (2002) Control of dinucleoside polyphosphates by the FHIT-homologous HNT2 gene, adenine biosynthesis and heat shock in Saccharomyces cerevisiae. BMC Mol Biol 3:7 {{SGDpaper|S000069891}} PMID 12028594</ref><ref name='S000063530'>Chen J, et al. (1998) Control of 5',5'-dinucleoside triphosphate catabolism by APH1, a Saccharomyces cerevisiae analog of human FHIT. J Bacteriol 180(9):2345-9 {{SGDpaper|S000063530}} PMID 9573184</ref><ref name='S000063528'>Brevet A, et al. (1991) Isolation and characterization of a dinucleoside triphosphatase from Saccharomyces cerevisiae. J Bacteriol 173(17):5275-9 |
− | {{SGDpaper| | + | {{SGDpaper|S000063528}} PMID 1653209</ref> |
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Revision as of 13:05, 16 January 2009
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Systematic name | YDR305C |
Gene name | HNT2 |
Aliases | APH1 |
Feature type | ORF, Verified |
Coordinates | Chr IV:1073485..1072743 |
Primary SGDID | S000002713 |
Description of YDR305C: Dinucleoside triphosphate hydrolase; has similarity to the tumor suppressor FHIT and belongs to the histidine triad (HIT) superfamily of nucleotide-binding proteins[1][2][3]
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Contents
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References
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- ↑ Rubio-Texeira M, et al. (2002) Control of dinucleoside polyphosphates by the FHIT-homologous HNT2 gene, adenine biosynthesis and heat shock in Saccharomyces cerevisiae. BMC Mol Biol 3:7 SGD PMID 12028594
- ↑ Chen J, et al. (1998) Control of 5',5'-dinucleoside triphosphate catabolism by APH1, a Saccharomyces cerevisiae analog of human FHIT. J Bacteriol 180(9):2345-9 SGD PMID 9573184
- ↑ Brevet A, et al. (1991) Isolation and characterization of a dinucleoside triphosphatase from Saccharomyces cerevisiae. J Bacteriol 173(17):5275-9 SGD PMID 1653209
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