Difference between revisions of "YMR109W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YMR109W YMR109W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004715 YMR109W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''MYO5 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''MYO5 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XIII:486586..490245
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|nowrap| Chr XIII:486587..490246
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000004715
 
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'''Description of {{PAGENAME}}:''' One of two type I myosins; contains proline-rich tail homology 2 (TH2) and SH3 domains; MYO5 deletion has little effect on growth, but myo3 myo5 double deletion causes severe defects in growth and actin cytoskeleton organization<ref name='S000073475'>Tanaka K and Matsui Y (2001) Functions of unconventional myosins in the yeast Saccharomyces cerevisiae. Cell Struct Funct 26(6):671-5 {{SGDpaper|S000073475}} PMID 11942625</ref><ref name='S000040780'>Anderson BL, et al. (1998) The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization. J Cell Biol 141(6):1357-70 {{SGDpaper|S000040780}} PMID 9628892</ref><ref name='S000039647'>Geli MI and Riezman H (1996) Role of type I myosins in receptor-mediated endocytosis in yeast. Science 272(5261):533-5
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'''Description of YMR109W:''' One of two type I myosins; contains proline-rich tail homology 2 (TH2) and SH3 domains; MYO5 deletion has little effect on growth, but myo3 myo5 double deletion causes severe defects in growth and actin cytoskeleton organization<ref name='S000040780'>Anderson BL, et al. (1998) The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization. J Cell Biol 141(6):1357-70 {{SGDpaper|S000040780}} PMID 9628892</ref><ref name='S000039647'>Geli MI and Riezman H (1996) Role of type I myosins in receptor-mediated endocytosis in yeast. Science 272(5261):533-5 {{SGDpaper|S000039647}} PMID 8614799</ref><ref name='S000073475'>Tanaka K and Matsui Y (2001) Functions of unconventional myosins in the yeast Saccharomyces cerevisiae. Cell Struct Funct 26(6):671-5
  {{SGDpaper|S000039647}} PMID 8614799</ref>
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  {{SGDpaper|S000073475}} PMID 11942625</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
{{CommentaryHelp}}
 
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<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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<!--
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<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.
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J Biol Chem 278(5):3265-74</ref>
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Latest revision as of 07:45, 23 January 2012

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Systematic name YMR109W
Gene name MYO5
Aliases
Feature type ORF, Verified
Coordinates Chr XIII:486587..490246
Primary SGDID S000004715


Description of YMR109W: One of two type I myosins; contains proline-rich tail homology 2 (TH2) and SH3 domains; MYO5 deletion has little effect on growth, but myo3 myo5 double deletion causes severe defects in growth and actin cytoskeleton organization[1][2][3]




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References

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  1. Anderson BL, et al. (1998) The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization. J Cell Biol 141(6):1357-70 SGD PMID 9628892
  2. Geli MI and Riezman H (1996) Role of type I myosins in receptor-mediated endocytosis in yeast. Science 272(5261):533-5 SGD PMID 8614799
  3. Tanaka K and Matsui Y (2001) Functions of unconventional myosins in the yeast Saccharomyces cerevisiae. Cell Struct Funct 26(6):671-5 SGD PMID 11942625

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