Difference between revisions of "YDL125C"

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'''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<ref name='S000069835'>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 {{SGDpaper|S000069835}} PMID 11805111</ref><ref name='S000059617'>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 {{SGDpaper|S000059617}} PMID 10958787</ref><ref name='S000058119'>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 {{SGDpaper|S000058119}} PMID 9164465</ref><ref name='S000056528'>Seraphin B (1992) The HIT protein family: a new family of proteins present in prokaryotes, yeast and mammals. DNA Seq 3(3):177-9
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'''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<ref name='S000056528'>Seraphin B (1992) The HIT protein family: a new family of proteins present in prokaryotes, yeast and mammals. DNA Seq 3(3):177-9 {{SGDpaper|S000056528}} PMID 1472710</ref><ref name='S000058119'>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 {{SGDpaper|S000058119}} PMID 9164465</ref><ref name='S000059617'>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 {{SGDpaper|S000059617}} PMID 10958787</ref><ref name='S000069835'>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
  {{SGDpaper|S000056528}} PMID 1472710</ref>
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  {{SGDpaper|S000069835}} PMID 11805111</ref>
 
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Revision as of 14:05, 31 March 2009

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Systematic name YDL125C
Gene name HNT1
Aliases
Feature type ORF, Verified
Coordinates Chr IV:239606..239019
Primary SGDID S000002283


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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  1. 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
  2. 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
  3. 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
  4. 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

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