Difference between revisions of "YLR178C"

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'''Description of YLR178C:''' Carboxypeptidase Y inhibitor, function requires acetylation by the NatB N-terminal acetyltransferase; phosphatidylethanolamine-binding protein involved in protein kinase A signaling pathway<ref name='S000077123'>Caesar R and Blomberg A (2004) The stress-induced Tfs1p requires NatB-mediated acetylation to inhibit carboxypeptidase Y and to regulate the protein kinase A pathway. J Biol Chem 279(37):38532-43 {{SGDpaper|S000077123}} PMID 15229224</ref><ref name='S000039310'>Bruun AW, et al. (1998) A high-affinity inhibitor of yeast carboxypeptidase Y is encoded by TFS1 and shows homology to a family of lipid binding proteins. Biochemistry 37(10):3351-7
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'''Description of YLR178C:''' Carboxypeptidase Y inhibitor, has affinity for anionic phospholipids; targeted to vacuolar membranes during stationary phase; function requires acetylation by NatB N-terminal acetyltransferase; involved in protein kinase A signaling pathway<ref name='S000119473'>Mima J, et al. (2006) Specific membrane binding of the carboxypeptidase Y inhibitor I(C), a phosphatidylethanolamine-binding protein family member. FEBS J 273(23):5374-83 {{SGDpaper|S000119473}} PMID 17076703</ref><ref name='S000077123'>Caesar R and Blomberg A (2004) The stress-induced Tfs1p requires NatB-mediated acetylation to inhibit carboxypeptidase Y and to regulate the protein kinase A pathway. J Biol Chem 279(37):38532-43 {{SGDpaper|S000077123}} PMID 15229224</ref><ref name='S000039310'>Bruun AW, et al. (1998) A high-affinity inhibitor of yeast carboxypeptidase Y is encoded by TFS1 and shows homology to a family of lipid binding proteins. Biochemistry 37(10):3351-7
 
  {{SGDpaper|S000039310}} PMID 9521655</ref>
 
  {{SGDpaper|S000039310}} PMID 9521655</ref>
 
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Revision as of 06:21, 26 February 2009

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Systematic name YLR178C
Gene name TFS1
Aliases DKA1
Feature type ORF, Verified
Coordinates Chr XII:513823..513164
Primary SGDID S000004168


Description of YLR178C: Carboxypeptidase Y inhibitor, has affinity for anionic phospholipids; targeted to vacuolar membranes during stationary phase; function requires acetylation by NatB N-terminal acetyltransferase; involved in protein kinase A signaling pathway[1][2][3]




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DNA and RNA Details

Other DNA and RNA Details

Other Topic: expression

Specifically lower expression in sulfur limited chemostat cultures versus sulfur excess. [4] [5]





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References

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  1. Mima J, et al. (2006) Specific membrane binding of the carboxypeptidase Y inhibitor I(C), a phosphatidylethanolamine-binding protein family member. FEBS J 273(23):5374-83 SGD PMID 17076703
  2. Caesar R and Blomberg A (2004) The stress-induced Tfs1p requires NatB-mediated acetylation to inhibit carboxypeptidase Y and to regulate the protein kinase A pathway. J Biol Chem 279(37):38532-43 SGD PMID 15229224
  3. Bruun AW, et al. (1998) A high-affinity inhibitor of yeast carboxypeptidase Y is encoded by TFS1 and shows homology to a family of lipid binding proteins. Biochemistry 37(10):3351-7 SGD PMID 9521655
  4. 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 SGD PMID 12414795
  5. submitted by Viktor Boer on 2003-07-25

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