Difference between revisions of "YHR013C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YHR013C YHR013C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001055 YHR013C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''ARD1 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''ARD1 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|nowrap| Chr VIII:131440..130724
 
|nowrap| Chr VIII:131440..130724
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000001055
 
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'''Description of {{PAGENAME}}:''' Subunit of the N-terminal acetyltransferase NatA (Nat1p, Ard1p, Nat5p); N-terminally acetylates many proteins, which influences multiple processes such as the cell cycle, heat-shock resistance, mating, sporulation, and telomeric silencing<ref name='S000074487'>Gautschi M, et al. (2003) The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol Cell Biol 23(20):7403-14 {{SGDpaper|S000074487}} PMID 14517307</ref><ref name='S000073836'>Polevoda B and Sherman F (2003) Composition and function of the eukaryotic N-terminal acetyltransferase subunits. Biochem Biophys Res Commun 308(1):1-11 {{SGDpaper|S000073836}} PMID 12890471</ref><ref name='S000044111'>Mullen JR, et al. (1989) Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast. EMBO J 8(7):2067-75 {{SGDpaper|S000044111}} PMID 2551674</ref><ref name='S000042046'>Park EC and Szostak JW (1992) ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J 11(6):2087-93
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'''Description of YHR013C:''' Subunit of the N-terminal acetyltransferase NatA (Nat1p, Ard1p, Nat5p); N-terminally acetylates many proteins, which influences multiple processes such as the cell cycle, heat-shock resistance, mating, sporulation, and telomeric silencing<ref name='S000074487'>Gautschi M, et al. (2003) The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol Cell Biol 23(20):7403-14 {{SGDpaper|S000074487}} PMID 14517307</ref><ref name='S000073836'>Polevoda B and Sherman F (2003) Composition and function of the eukaryotic N-terminal acetyltransferase subunits. Biochem Biophys Res Commun 308(1):1-11 {{SGDpaper|S000073836}} PMID 12890471</ref><ref name='S000044111'>Mullen JR, et al. (1989) Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast. EMBO J 8(7):2067-75 {{SGDpaper|S000044111}} PMID 2551674</ref><ref name='S000042046'>Park EC and Szostak JW (1992) ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J 11(6):2087-93
 
  {{SGDpaper|S000042046}} PMID 1600941</ref>
 
  {{SGDpaper|S000042046}} PMID 1600941</ref>
 
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J Biol Chem 278(5):3265-74</ref>
 
J Biol Chem 278(5):3265-74</ref>
 
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Revision as of 07:45, 27 February 2007

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Systematic name YHR013C
Gene name ARD1
Aliases
Feature type ORF, Verified
Coordinates Chr VIII:131440..130724
Primary SGDID S000001055


Description of YHR013C: Subunit of the N-terminal acetyltransferase NatA (Nat1p, Ard1p, Nat5p); N-terminally acetylates many proteins, which influences multiple processes such as the cell cycle, heat-shock resistance, mating, sporulation, and telomeric silencing[1][2][3][4]




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communication correction

Mutations in ARD1 lead to inability to respond to alpha-factor, inability to enter stationary phase, and inability to sporulate [5] [6]





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References

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  1. Gautschi M, et al. (2003) The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol Cell Biol 23(20):7403-14 SGD PMID 14517307
  2. Polevoda B and Sherman F (2003) Composition and function of the eukaryotic N-terminal acetyltransferase subunits. Biochem Biophys Res Commun 308(1):1-11 SGD PMID 12890471
  3. Mullen JR, et al. (1989) Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast. EMBO J 8(7):2067-75 SGD PMID 2551674
  4. Park EC and Szostak JW (1992) ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J 11(6):2087-93 SGD PMID 1600941
  5. Whiteway M and Szostak JW (1985) The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathways. Cell 43(2 Pt 1):483-92 SGD PMID 3907857
  6. submitted by Juanita Martinez on 2004-09-22

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