Difference between revisions of "YOR209C"

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'''Description of YOR209C:''' Nicotinate phosphoribosyltransferase, acts in the salvage pathway of NAD+ biosynthesis; required for silencing at rDNA and telomeres and has a role in silencing at mating-type loci; localized to the nucleus<ref name='S000048730'>Smith JS, et al. (2000) A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family. Proc Natl Acad Sci U S A 97(12):6658-63 {{SGDpaper|S000048730}} PMID 10841563</ref><ref name='S000070049'>Anderson RM, et al. (2002) Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels. J Biol Chem 277(21):18881-90
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'''Description of YOR209C:''' Nicotinate phosphoribosyltransferase, acts in the salvage pathway of NAD+ biosynthesis; required for silencing at rDNA and telomeres and has a role in silencing at mating-type loci; localized to the nucleus<ref name='S000070049'>Anderson RM, et al. (2002) Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels. J Biol Chem 277(21):18881-90 {{SGDpaper|S000070049}} PMID 11884393</ref><ref name='S000048730'>Smith JS, et al. (2000) A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family. Proc Natl Acad Sci U S A 97(12):6658-63
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Revision as of 14:05, 25 February 2010

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Systematic name YOR209C
Gene name NPT1
Aliases
Feature type ORF, Verified
Coordinates Chr XV:737727..736438
Primary SGDID S000005735


Description of YOR209C: Nicotinate phosphoribosyltransferase, acts in the salvage pathway of NAD+ biosynthesis; required for silencing at rDNA and telomeres and has a role in silencing at mating-type loci; localized to the nucleus[1][2]




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References

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  1. Anderson RM, et al. (2002) Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels. J Biol Chem 277(21):18881-90 SGD PMID 11884393
  2. Smith JS, et al. (2000) A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family. Proc Natl Acad Sci U S A 97(12):6658-63 SGD PMID 10841563

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