YNL058C
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| Systematic name | YNL058C |
| Gene name | |
| Aliases | |
| Feature type | ORF, Uncharacterized |
| Coordinates | Chr XIV:516713..515763 |
| Primary SGDID | S000005003 |
Description of YNL058C: Putative protein of unknown function; green fluorescent protein (GFP)-fusion protein localizes to the vacuole; YNL058C is not an essential gene[1][2][3]
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Contents
Community Commentary
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UW Stout/D2O SP22
The Knock Out Yeast Strain YNL058C (A6) was unaffected by the 35% dilution of D2O. This also shows in the optical density results being about 0.4-0.5 OD 600.
UW-Stout/UV Light SP22
As part of the University of Wisconsin Stout Orphan Gene Project this gene was tested under a UV Light using this protocol.
RESULTS
INTERPERTATION
In the graph and photos above, exposing this gene to 600 seconds of 400 Watt UV Light killed approximately 85% of yeast cell cultures, compared to its control counterpart, which was the same gene and amount of cells, just was not exposed to UV Light.
Transmembrane Domain GxxxG
The transmembrane domain of Ynl058cp shows homology with the SKG6/AXL2 alpha-helix transmembrane domain (IPR014805). In particular, this domain contains GaviG. The presence of a overlapping GxxxG motif [4] strongly indicates that Ynl058c dimerises.
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. [3] [5]
This gene is part of the UW-Stout Orphan Gene Project. Learn more here.
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References
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- ↑ Giaever G, et al. (2002) Functional profiling of the Saccharomyces cerevisiae genome. Nature 418(6896):387-91 SGD PMID 12140549
- ↑ Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 SGD PMID 14562095
- ↑ 3.0 3.1 Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64
SGD PMID 14574415 Cite error: Invalid
<ref>tag; name "S000074306" defined multiple times with different content - ↑ Senes A, Engel DE and DeGrado WF (2004) Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs. Curr Opin Struct Biol. 2004 14(4):465-79. PMID 15313242
- ↑ submitted by Jeff Ubersax on 2004-01-29
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