| UniProt ID | CLC1_YEAST | |
|---|---|---|
| UniProt AC | P17891 | |
| Protein Name | Clathrin light chain | |
| Gene Name | CLC1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 233 | |
| Subcellular Localization |
Cytoplasmic vesicle membrane Peripheral membrane protein Cytoplasmic side. Membrane, coated pit Peripheral membrane protein Cytoplasmic side. Cytoplasmic face of coated pits and vesicles. |
|
| Protein Description | Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. In yeast, it is involved in the retention of proteins in an intracellular membrane compartment, presumably the trans-Golgi. The yeast light chain is important for cell growth. The light chain may help to properly orient the assembly/ disassembly of the clathrin coats.. | |
| Protein Sequence | MSEKFPPLEDQNIDFTPNDKKDDDTDFLKREAEILGDEFKTEQDDILETEASPAKDDDEIRDFEEQFPDINSANGAVSSDQNGSATVSSGNDNGEADDDFSTFEGANQSTESVKEDRSEVVDQWKQRRAVEIHEKDLKDEELKKELQDEAIKHIDDFYDSYNKKKEQQLEDAAKEAEAFLKKRDEFFGQDNTTWDRALQLINQDDADIIGGRDRSKLKEILLRLKGNAKAPGA | |
| 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 |
|---|---|---|---|---|---|
| 16 | Phosphorylation | EDQNIDFTPNDKKDD CCCCCCCCCCCCCCC | 19.89 | 28889911 | |
| 21 | Ubiquitination | DFTPNDKKDDDTDFL CCCCCCCCCCCCHHH | 70.07 | 24961812 | |
| 29 | Ubiquitination | DDDTDFLKREAEILG CCCCHHHHHHHHHHC | 48.46 | 24961812 | |
| 41 | Phosphorylation | ILGDEFKTEQDDILE HHCHHHCCCCCCHHH | 44.17 | 22369663 | |
| 49 | Phosphorylation | EQDDILETEASPAKD CCCCHHHCCCCCCCC | 33.15 | 22369663 | |
| 52 | Phosphorylation | DILETEASPAKDDDE CHHHCCCCCCCCHHH | 21.11 | 22369663 | |
| 125 | Ubiquitination | SEVVDQWKQRRAVEI HHHHHHHHHHHHHHH | 28.44 | 22817900 | |
| 125 | 2-Hydroxyisobutyrylation | SEVVDQWKQRRAVEI HHHHHHHHHHHHHHH | 28.44 | - | |
| 135 | Succinylation | RAVEIHEKDLKDEEL HHHHHHHHHCCHHHH | 54.95 | 23954790 | |
| 138 | Acetylation | EIHEKDLKDEELKKE HHHHHHCCHHHHHHH | 73.55 | 22865919 | |
| 152 | Acetylation | ELQDEAIKHIDDFYD HHHHHHHHHHHHHHH | 41.37 | 24489116 | |
| 160 | Phosphorylation | HIDDFYDSYNKKKEQ HHHHHHHHHHHHHHH | 21.16 | 21440633 | |
| 165 | Ubiquitination | YDSYNKKKEQQLEDA HHHHHHHHHHHHHHH | 63.47 | 23749301 | |
| 174 | Acetylation | QQLEDAAKEAEAFLK HHHHHHHHHHHHHHH | 60.21 | 24489116 | |
| 229 | Ubiquitination | LRLKGNAKAPGA--- HHHHCCCCCCCC--- | 60.14 | 23749301 |
| 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 CLC1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CLC1_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 CLC1_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-52, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49 AND SER-52, AND MASSSPECTROMETRY. | |
