Difference between revisions of "YHR013C"
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| − | '''Description of YHR013C:''' Subunit of | + | '''Description of YHR013C:''' Subunit of N-terminal acetyltransferase NatA (Nat1p, Ard1p, Nat5p); acetylates many proteins and thus affects telomeric silencing, cell cycle, heat-shock resistance, mating, and sporulation; human Ard1p levels are elevated in cancer cells<ref name='S000129704'>Yu M, et al. (2009) Immunohistochemical analysis of human arrest-defective-1 expressed in cancers in vivo. Oncol Rep 21(4):909-15 {{SGDpaper|S000129704}} PMID 19287988</ref><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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Revision as of 13:05, 30 March 2009
Share your knowledge...Edit this entry! <protect>
| Systematic name | YHR013C |
| Gene name | ARD1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr VIII:131440..130724 |
| Primary SGDID | S000001055 |
Description of YHR013C: Subunit of N-terminal acetyltransferase NatA (Nat1p, Ard1p, Nat5p); acetylates many proteins and thus affects telomeric silencing, cell cycle, heat-shock resistance, mating, and sporulation; human Ard1p levels are elevated in cancer cells[1][2][3][4][5]
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Community Commentary
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Other
communication correction
Mutations in ARD1 lead to inability to respond to alpha-factor, inability to enter stationary phase, and inability to sporulate [6] [7]
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References
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- ↑ Yu M, et al. (2009) Immunohistochemical analysis of human arrest-defective-1 expressed in cancers in vivo. Oncol Rep 21(4):909-15 SGD PMID 19287988
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ submitted by Juanita Martinez on 2004-09-22
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