Difference between revisions of "YKL129C"

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'''Description of YKL129C:''' One of two type I myosins; localizes to actin cortical patches; deletion of MYO3 has little effect on growth, but myo3 myo5 double deletion causes severe defects in growth and actin cytoskeleton organization<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='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='S000073475'>Tanaka K and Matsui Y (2001) Functions of unconventional myosins in the yeast Saccharomyces cerevisiae. Cell Struct Funct 26(6):671-5
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'''Description of YKL129C:''' One of two type I myosins; localizes to actin cortical patches; deletion of MYO3 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
  {{SGDpaper|S000073475}} PMID 11942625</ref>
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  {{SGDpaper|S000039647}} PMID 8614799</ref>
 
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Revision as of 14:05, 16 January 2009

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Systematic name YKL129C
Gene name MYO3
Aliases
Feature type ORF, Verified
Coordinates Chr XI:200163..196348
Primary SGDID S000001612


Description of YKL129C: One of two type I myosins; localizes to actin cortical patches; deletion of MYO3 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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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. [4] [5]





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References

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  1. 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
  2. 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
  3. 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
  4. Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 SGD PMID 14574415
  5. submitted by Jeff Ubersax on 2004-01-27

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