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=' | + | '''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 |
− | {{SGDpaper| | + | {{SGDpaper|S000073475}} PMID 11942625</ref> |
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Revision as of 13:05, 31 March 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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- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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 2004-01-27
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