Difference between revisions of "YMR174C"
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| − | '''Description of YMR174C:''' Cytoplasmic proteinase A (Pep4p) inhibitor, dependent on Pbs2p and Hog1p protein kinases for osmotic induction; intrinsically unstructured, N-terminal half becomes ordered in the active site of proteinase A upon contact<ref name=' | + | '''Description of YMR174C:''' Cytoplasmic proteinase A (Pep4p) inhibitor, dependent on Pbs2p and Hog1p protein kinases for osmotic induction; intrinsically unstructured, N-terminal half becomes ordered in the active site of proteinase A upon contact<ref name='S000040158'>Miralles VJ and Serrano R (1995) A genomic locus in Saccharomyces cerevisiae with four genes up-regulated by osmotic stress. Mol Microbiol 17(4):653-62 {{SGDpaper|S000040158}} PMID 8801420</ref><ref name='S000064297'>Phylip LH, et al. (2001) The potency and specificity of the interaction between the IA3 inhibitor and its target aspartic proteinase from Saccharomyces cerevisiae. J Biol Chem 276(3):2023-30 {{SGDpaper|S000064297}} PMID 11042188</ref><ref name='S000072383'>Beck I, et al. (1980) The intracellular proteinases and their inhibitors in yeast. A mutant with altered regulation of proteinase A inhibitor activity. J Biol Chem 255(10):4821-8 {{SGDpaper|S000072383}} PMID 6989820</ref><ref name='S000072389'>Badasso MO, et al. (2000) Purification, co-crystallization and preliminary X--ray analysis of the natural aspartic proteinase inhibitor IA3 complexed with saccharopepsin from Saccharomyces cerevisiae. Acta Crystallogr D Biol Crystallogr 56(Pt 7):915-7 |
| − | {{SGDpaper| | + | {{SGDpaper|S000072389}} PMID 10930843</ref> |
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Revision as of 13:05, 31 March 2009
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| Systematic name | YMR174C |
| Gene name | PAI3 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XIII:610364..610158 |
| Primary SGDID | S000004786 |
Description of YMR174C: Cytoplasmic proteinase A (Pep4p) inhibitor, dependent on Pbs2p and Hog1p protein kinases for osmotic induction; intrinsically unstructured, N-terminal half becomes ordered in the active site of proteinase A upon contact[1][2][3][4]
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Contents
Community Commentary
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DNA and RNA Details
Other DNA and RNA Details
Other Topic: expression
Specifically higher expression in carbon limited chemostat cultures versus carbon excess. [5] [6]
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References
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- ↑ Miralles VJ and Serrano R (1995) A genomic locus in Saccharomyces cerevisiae with four genes up-regulated by osmotic stress. Mol Microbiol 17(4):653-62 SGD PMID 8801420
- ↑ Phylip LH, et al. (2001) The potency and specificity of the interaction between the IA3 inhibitor and its target aspartic proteinase from Saccharomyces cerevisiae. J Biol Chem 276(3):2023-30 SGD PMID 11042188
- ↑ Beck I, et al. (1980) The intracellular proteinases and their inhibitors in yeast. A mutant with altered regulation of proteinase A inhibitor activity. J Biol Chem 255(10):4821-8 SGD PMID 6989820
- ↑ Badasso MO, et al. (2000) Purification, co-crystallization and preliminary X--ray analysis of the natural aspartic proteinase inhibitor IA3 complexed with saccharopepsin from Saccharomyces cerevisiae. Acta Crystallogr D Biol Crystallogr 56(Pt 7):915-7 SGD PMID 10930843
- ↑ 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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