Difference between revisions of "YLR178C"
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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=' | + | '''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='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><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='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| | + | {{SGDpaper|S000119473}} PMID 17076703</ref> |
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Revision as of 13:05, 31 March 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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Contents
Community Commentary
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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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- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ submitted by Viktor Boer on 2003-07-25
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