Difference between revisions of "YBR109C"
SGDwikiBot (talk | contribs) (Automated import of articles) |
SGDwikiBot (talk | contribs) (Automated import of articles) |
||
(10 intermediate revisions by 2 users not shown) | |||
Line 4: | Line 4: | ||
{|{{Prettytable}} align = 'right' width = '200px' | {|{{Prettytable}} align = 'right' width = '200px' | ||
|- | |- | ||
− | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000313 YBR109C] |
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''CMD1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''CMD1 '' | ||
Line 13: | Line 13: | ||
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
− | |nowrap| Chr II: | + | |nowrap| Chr II:458362..457919 |
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000000313 | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000000313 | ||
|} | |} | ||
<br> | <br> | ||
− | '''Description of YBR109C:''' Calmodulin; Ca++ binding protein that regulates Ca++ independent processes (mitosis, bud growth, actin organization, endocytosis, etc.) and Ca++ dependent processes (stress-activated pathways), targets include Nuf1p, Myo2p and calcineurin<ref name=' | + | '''Description of YBR109C:''' Calmodulin; Ca++ binding protein that regulates Ca++ independent processes (mitosis, bud growth, actin organization, endocytosis, etc.) and Ca++ dependent processes (stress-activated pathways), targets include Nuf1p, Myo2p and calcineurin<ref name='S000066251'>Cyert MS (2001) Genetic analysis of calmodulin and its targets in Saccharomyces cerevisiae. Annu Rev Genet 35:647-72 {{SGDpaper|S000066251}} PMID 11700296</ref><ref name='S000046694'>Davis TN, et al. (1986) Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 47(3):423-31 {{SGDpaper|S000046694}} PMID 3533275</ref><ref name='S000071160'>Desrivieres S, et al. (2002) Calmodulin controls organization of the actin cytoskeleton via regulation of phosphatidylinositol (4,5)-bisphosphate synthesis in Saccharomyces cerevisiae. Biochem J 366(Pt 3):945-51 {{SGDpaper|S000071160}} PMID 12079494</ref><ref name='S000041618'>Kubler E, et al. (1994) Calcium-independent calmodulin requirement for endocytosis in yeast. EMBO J 13(23):5539-46 {{SGDpaper|S000041618}} PMID 7988551</ref><ref name='S000047941'>Ohya Y and Botstein D (1994) Diverse essential functions revealed by complementing yeast calmodulin mutants. Science 263(5149):963-6 {{SGDpaper|S000047941}} PMID 8310294</ref><ref name='S000062321'>Peters C and Mayer A (1998) Ca2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion. Nature 396(6711):575-80 {{SGDpaper|S000062321}} PMID 9859992</ref><ref name='S000080958'>Starai VJ, et al. (2005) Ion regulation of homotypic vacuole fusion in Saccharomyces cerevisiae. J Biol Chem 280(17):16754-62 {{SGDpaper|S000080958}} PMID 15737991</ref><ref name='S000062307'>Starovasnik MA, et al. (1993) Similarities and differences between yeast and vertebrate calmodulin: an examination of the calcium-binding and structural properties of calmodulin from the yeast Saccharomyces cerevisiae. Biochemistry 32(13):3261-70 |
− | {{SGDpaper| | + | {{SGDpaper|S000062307}} PMID 8461293</ref> |
<br> | <br> | ||
<br> | <br> | ||
Line 29: | Line 29: | ||
==Community Commentary== | ==Community Commentary== | ||
{{CommentaryHelp}} | {{CommentaryHelp}} | ||
− | + | Summary of Davis lab calmodulin alleles: | |
+ | <br>cmd1-1: temperature-sensitive defect in mitosis with very minor defect in bud growth. | ||
+ | <ref> Davis, T. N. (1992). A temperature-sensitive calmodulin mutant loses viability during mitosis. J. Cell Biol., 118:607-617.</ref> | ||
+ | <br> cmd1-3: temperature-sensitive defect in mitosis and complete defect in all Ca<sup>2+</sup>-dependent functions (unpublished and <ref>Geiser, J. R., D. van Tuinen, S. E. Brockerhoff, M. M. Neff, T. N. Davis. (1991). Can calmodulin function without binding calcium? Cell, 65, 949-959.</ref>) | ||
+ | <br>cmd1-6: no defect in mitosis, complete defect in all Ca<sup>2+</sup>-dependent functions (unpublished and <ref>Geiser, J. R., D. van Tuinen, S. E. Brockerhoff, M. M. Neff, T. N. Davis. (1991). Can calmodulin function without binding calcium? Cell, 65, 949-959.</ref>) | ||
+ | <br>cmd1-8: temperature-sensitive defect in bud growth (mild and only apparent at 38C) (unpublished) | ||
Line 42: | Line 47: | ||
+ | <protect> | ||
+ | |||
+ | ==References== | ||
+ | <!-- REFERENCES ARE AUTOMATICALLY GENERATED. PLEASE DON'T EDIT THIS SECTION--> | ||
+ | {{RefHelp}} | ||
+ | </protect> | ||
<protect> | <protect> | ||
==References== | ==References== |
Latest revision as of 07:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
Systematic name | YBR109C |
Gene name | CMD1 |
Aliases | CaM |
Feature type | ORF, Verified |
Coordinates | Chr II:458362..457919 |
Primary SGDID | S000000313 |
Description of YBR109C: Calmodulin; Ca++ binding protein that regulates Ca++ independent processes (mitosis, bud growth, actin organization, endocytosis, etc.) and Ca++ dependent processes (stress-activated pathways), targets include Nuf1p, Myo2p and calcineurin[1][2][3][4][5][6][7][8]
</protect>
Community Commentary
About Community Commentary. Please share your knowledge!
Summary of Davis lab calmodulin alleles:
cmd1-1: temperature-sensitive defect in mitosis with very minor defect in bud growth.
[9]
cmd1-3: temperature-sensitive defect in mitosis and complete defect in all Ca2+-dependent functions (unpublished and [10])
cmd1-6: no defect in mitosis, complete defect in all Ca2+-dependent functions (unpublished and [11])
cmd1-8: temperature-sensitive defect in bud growth (mild and only apparent at 38C) (unpublished)
<protect>
References
See Help:References on how to add references
- ↑ Cyert MS (2001) Genetic analysis of calmodulin and its targets in Saccharomyces cerevisiae. Annu Rev Genet 35:647-72 SGD PMID 11700296
- ↑ Davis TN, et al. (1986) Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 47(3):423-31 SGD PMID 3533275
- ↑ Desrivieres S, et al. (2002) Calmodulin controls organization of the actin cytoskeleton via regulation of phosphatidylinositol (4,5)-bisphosphate synthesis in Saccharomyces cerevisiae. Biochem J 366(Pt 3):945-51 SGD PMID 12079494
- ↑ Kubler E, et al. (1994) Calcium-independent calmodulin requirement for endocytosis in yeast. EMBO J 13(23):5539-46 SGD PMID 7988551
- ↑ Ohya Y and Botstein D (1994) Diverse essential functions revealed by complementing yeast calmodulin mutants. Science 263(5149):963-6 SGD PMID 8310294
- ↑ Peters C and Mayer A (1998) Ca2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion. Nature 396(6711):575-80 SGD PMID 9859992
- ↑ Starai VJ, et al. (2005) Ion regulation of homotypic vacuole fusion in Saccharomyces cerevisiae. J Biol Chem 280(17):16754-62 SGD PMID 15737991
- ↑ Starovasnik MA, et al. (1993) Similarities and differences between yeast and vertebrate calmodulin: an examination of the calcium-binding and structural properties of calmodulin from the yeast Saccharomyces cerevisiae. Biochemistry 32(13):3261-70 SGD PMID 8461293
- ↑ Davis, T. N. (1992). A temperature-sensitive calmodulin mutant loses viability during mitosis. J. Cell Biol., 118:607-617.
- ↑ Geiser, J. R., D. van Tuinen, S. E. Brockerhoff, M. M. Neff, T. N. Davis. (1991). Can calmodulin function without binding calcium? Cell, 65, 949-959.
- ↑ Geiser, J. R., D. van Tuinen, S. E. Brockerhoff, M. M. Neff, T. N. Davis. (1991). Can calmodulin function without binding calcium? Cell, 65, 949-959.
See Help:Categories on how to add the wiki page for this gene to a Category </protect> <protect>
References
See Help:References on how to add references
See Help:Categories on how to add the wiki page for this gene to a Category </protect>