Difference between revisions of "YDR093W"
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| + | Specifically higher expression in carbon limited chemostat cultures versus carbon excess. | ||
| + | <ref>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</ref> | ||
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Revision as of 13:02, 21 February 2007
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| Systematic name | YDR093W |
| Gene name | DNF2 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:631279..636117 |
Description of YDR093W: Aminophospholipid translocase (flippase) that localizes primarily to the plasma membrane; contributes to endocytosis, protein transport and cell polarity; type 4 P-type ATPase[1][2][3][4]
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Protein Details
Protein Modification
Modification(s): Phosphorylation
Identified as an efficient substrate of Clb2-Cdk1-as1 in a screen of a proteomic GST-fusion library. [5] [6]
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References
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- ↑ Catty P, et al. (1997) The complete inventory of the yeast Saccharomyces cerevisiae P-type transport ATPases. FEBS Lett 409(3):325-32 SGD PMID 9224683
- ↑ Iwamoto K, et al. (2004) Local exposure of phosphatidylethanolamine on the yeast plasma membrane is implicated in cell polarity. Genes Cells 9(10):891-903 SGD PMID 15461661
- ↑ Pomorski T, et al. (2003) Drs2p-related P-type ATPases Dnf1p and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis. Mol Biol Cell 14(3):1240-54 SGD PMID 12631737
- ↑ Hua Z, et al. (2002) An essential subfamily of Drs2p-related P-type ATPases is required for protein trafficking between Golgi complex and endosomal/vacuolar system. Mol Biol Cell 13(9):3162-77 SGD PMID 12221123
- ↑ Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 SGD PMID 14574415
- ↑ submitted by Jeff Ubersax on 2004-01-21
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