| UniProt ID | COFI_YEAST | |
|---|---|---|
| UniProt AC | Q03048 | |
| Protein Name | Cofilin | |
| Gene Name | COF1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 143 | |
| Subcellular Localization | Cytoplasm . Cytoplasm, cytoskeleton . Nucleus matrix . Throughout the cytoplasm (but not on the cytoplasmic cables) and major component of the cortical actin cytoskeleton. | |
| Protein Description | Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton. In effect, yeast cofilin increases the rate of actin polymerization by making new ends available for actin subunit addition. Such a protein complex is important for the polarized growth of yeast cells.. | |
| Protein Sequence | MSRSGVAVADESLTAFNDLKLGKKYKFILFGLNDAKTEIVVKETSTDPSYDAFLEKLPENDCLYAIYDFEYEINGNEGKRSKIVFFTWSPDTAPVRSKMVYASSKDALRRALNGVSTDVQGTDFSEVSYDSVLERVSRGAGSH | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSRSGVAVA ------CCCCCEEEC | 34.84 | 22369663 | |
| 4 | Phosphorylation | ----MSRSGVAVADE ----CCCCCEEECCC | 30.25 | 22369663 | |
| 12 | Phosphorylation | GVAVADESLTAFNDL CEEECCCCCHHHCCC | 31.41 | 22369663 | |
| 14 | Phosphorylation | AVADESLTAFNDLKL EECCCCCHHHCCCCC | 38.18 | 22369663 | |
| 20 | Acetylation | LTAFNDLKLGKKYKF CHHHCCCCCCCEEEE | 59.04 | 24489116 | |
| 20 | Ubiquitination | LTAFNDLKLGKKYKF CHHHCCCCCCCEEEE | 59.04 | 24961812 | |
| 20 | Succinylation | LTAFNDLKLGKKYKF CHHHCCCCCCCEEEE | 59.04 | 23954790 | |
| 26 | Acetylation | LKLGKKYKFILFGLN CCCCCEEEEEEEECC | 34.50 | 24489116 | |
| 37 | Phosphorylation | FGLNDAKTEIVVKET EECCCCCCEEEEEEC | 32.44 | 22369663 | |
| 81 | Phosphorylation | NGNEGKRSKIVFFTW CCCCCCEEEEEEEEE | 30.16 | 21440633 | |
| 82 | Acetylation | GNEGKRSKIVFFTWS CCCCCEEEEEEEEEC | 47.09 | 24489116 | |
| 87 | Phosphorylation | RSKIVFFTWSPDTAP EEEEEEEEECCCCCC | 17.36 | 22369663 | |
| 89 | Phosphorylation | KIVFFTWSPDTAPVR EEEEEEECCCCCCCC | 15.16 | 22369663 | |
| 92 | Phosphorylation | FFTWSPDTAPVRSKM EEEECCCCCCCCCCE | 35.92 | 21440633 | |
| 97 | Phosphorylation | PDTAPVRSKMVYASS CCCCCCCCCEEEECC | 25.90 | 21440633 | |
| 105 | Acetylation | KMVYASSKDALRRAL CEEEECCHHHHHHHH | 44.52 | 24489116 | |
| 105 | Succinylation | KMVYASSKDALRRAL CEEEECCHHHHHHHH | 44.52 | 23954790 | |
| 116 | Phosphorylation | RRALNGVSTDVQGTD HHHHCCCCCCCCCCC | 21.93 | 19823750 | |
| 117 | Phosphorylation | RALNGVSTDVQGTDF HHHCCCCCCCCCCCC | 37.47 | 19823750 | |
| 122 | Phosphorylation | VSTDVQGTDFSEVSY CCCCCCCCCCCCCCH | 19.44 | 19823750 | |
| 125 | Phosphorylation | DVQGTDFSEVSYDSV CCCCCCCCCCCHHHH | 39.64 | 19823750 | |
| 128 | Phosphorylation | GTDFSEVSYDSVLER CCCCCCCCHHHHHHH | 21.12 | 19823750 | |
| 129 | Phosphorylation | TDFSEVSYDSVLERV CCCCCCCHHHHHHHH | 19.88 | 19823750 | |
| 131 | Phosphorylation | FSEVSYDSVLERVSR CCCCCHHHHHHHHHC | 21.99 | 19823750 | |
| 137 | Phosphorylation | DSVLERVSRGAGSH- HHHHHHHHCCCCCC- | 31.08 | 19823750 | |
| 142 | Phosphorylation | RVSRGAGSH------ HHHCCCCCC------ | 26.03 | 19823750 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of COFI_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of COFI_YEAST !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of COFI_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND MASSSPECTROMETRY. | |
