Difference between revisions of "YDL125C"
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+ | Specifically higher expression in carbon limited chemostat cultures versus carbon excess. | ||
+ | <ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur. | ||
+ | J Biol Chem 278(5):3265-74</ref> | ||
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Revision as of 13:02, 21 February 2007
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Systematic name | YDL125C |
Gene name | HNT1 |
Aliases | |
Feature type | ORF, Verified |
Coordinates | Chr IV:239606..239019 |
Description of YDL125C: Adenosine 5'-monophosphoramidase; interacts physically and genetically with Kin28p, a CDK and TFIIK subunit, and genetically with CAK1; member of the histidine triad (HIT) superfamily of nucleotide-binding proteins and similar to Hint[1][2][3][4]
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References
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- ↑ Bieganowski P, et al. (2002) Adenosine monophosphoramidase activity of Hint and Hnt1 supports function of Kin28, Ccl1, and Tfb3. J Biol Chem 277(13):10852-60 SGD PMID 11805111
- ↑ Korsisaari N and Makela TP (2000) Interactions of Cdk7 and Kin28 with Hint/PKCI-1 and Hnt1 histidine triad proteins. J Biol Chem 275(45):34837-40 SGD PMID 10958787
- ↑ Brenner C, et al. (1997) Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins. Nat Struct Biol 4(3):231-8 SGD PMID 9164465
- ↑ Seraphin B (1992) The HIT protein family: a new family of proteins present in prokaryotes, yeast and mammals. DNA Seq 3(3):177-9 SGD PMID 1472710
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