| UniProt ID | COPB_YEAST | |
|---|---|---|
| UniProt AC | P41810 | |
| Protein Name | Coatomer subunit beta | |
| Gene Name | SEC26 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 973 | |
| Subcellular Localization |
Cytoplasm. Golgi apparatus membrane Peripheral membrane protein Cytoplasmic side . Cytoplasmic vesicle, COPI-coated vesicle membrane Peripheral membrane protein Cytoplasmic side. The coatomer is cytoplasmic or polymerized on the cytoplasmic sid |
|
| Protein Description | The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Required for mitochondrial morphology.. | |
| Protein Sequence | MTSLSSQPAYTLVFDPSPSMETYSSTDFQKALEKGSDEQKIDTMKSILVTMLEGNPMPELLMHIIRFVMPSKNKELKKLLYFYWEIVPKLAEDGKLRHEMILVCNAIQHDLQHPNEYIRGNTLRFLTKLREAELLEQMVPSVLACLEYRHAYVRKYAILAVFSIFKVSEHLLPDAKEIINSFIVAETDPICKRNAFIGLAELDRENALHYLENNIADIENLDPLLQAVFVQFIRQDANRTPALKAQYIELLMELLSTTTSDEVIFETALALTVLSANPNVLVPAVNKLIDLAVKVSDNNIKLIVLDRIQDINANNVGALEELTLDILRVLNAEDLDVRSKALDISMDLATSRNAEDVVQLLKKELQTTVNNPDQDKAMQYRQLLIKTIRTVAVNFVEMAASVVSLLLDFIGDLNSVAASGIIAFIKEVIEKYPQLRANILENMVQTLDKVRSAKAYRGALWIMGEYAEGESEIQHCWKHIRNSVGEVPILQSEIKKLTQNQEHTEENEVDATAKPTGPVILPDGTYATESAFDVKTSQKSVTDEERDSRPPIRRFVLSGDFYTAAILANTIIKLVLKFENVSKNKTVINALKAEALLILVSIVRVGQSSLVEKKIDEDSLERVMTSISILLDEVNPEEKKEEVKLLEVAFLDTTKSSFKRQIEIAKKNKHKRALKDSCKNIEPIDTPISFRQFAGVDSTNVQKDSIEEDLQLAMKGDAIHATSSSSISKLKKIVPLCGFSDPVYAEACITNNQFDVVLDVLLVNQTKETLKNLHVQFATLGDLKIIDTPQKTNVIPHGFHKFTVTVKVSSADTGVIFGNIIYDGAHGEDARYVILNDVHVDIMDYIKPATADDEHFRTMWNAFEWENKISVKSQLPTLHAYLRELVKGTNMGILTPSESLGEDDCRFLSCNLYAKSSFGEDALANLCIEKDSKTNDVIGYVRIRSKGQGLALSLGDRVALIAKKTNKLALTHV | |
| 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 |
|---|---|---|---|---|---|
| 40 | Ubiquitination | EKGSDEQKIDTMKSI HCCCHHHHHHHHHHH | 40.27 | 23749301 | |
| 95 | 2-Hydroxyisobutyrylation | PKLAEDGKLRHEMIL HHHHHCCCCCCEEEH | 55.45 | - | |
| 181 | Phosphorylation | DAKEIINSFIVAETD CHHHHHHHHHHCCCC | 13.12 | 21440633 | |
| 192 | Ubiquitination | AETDPICKRNAFIGL CCCCHHHCCCCEEEC | 49.78 | 24961812 | |
| 345 | Phosphorylation | RSKALDISMDLATSR HHHHHHHHHHHHHCC | 13.10 | 28889911 | |
| 351 | Phosphorylation | ISMDLATSRNAEDVV HHHHHHHCCCHHHHH | 20.24 | 28889911 | |
| 362 | Acetylation | EDVVQLLKKELQTTV HHHHHHHHHHHHHHC | 53.44 | 24489116 | |
| 363 | Ubiquitination | DVVQLLKKELQTTVN HHHHHHHHHHHHHCC | 64.72 | 23749301 | |
| 376 | Ubiquitination | VNNPDQDKAMQYRQL CCCCCHHHHHHHHHH | 39.87 | 23749301 | |
| 376 | Acetylation | VNNPDQDKAMQYRQL CCCCCHHHHHHHHHH | 39.87 | 24489116 | |
| 386 | Acetylation | QYRQLLIKTIRTVAV HHHHHHHHHHHHHHH | 37.56 | 24489116 | |
| 449 | Acetylation | NMVQTLDKVRSAKAY HHHHHHHHHHHCHHH | 42.53 | 24489116 | |
| 483 | Phosphorylation | CWKHIRNSVGEVPIL HHHHHHHCCCCHHHH | 22.96 | 24961812 | |
| 495 | Ubiquitination | PILQSEIKKLTQNQE HHHHHHHHHHHCCCC | 37.36 | 15699485 | |
| 496 | Ubiquitination | ILQSEIKKLTQNQEH HHHHHHHHHHCCCCC | 63.53 | 15699485 | |
| 540 | Phosphorylation | DVKTSQKSVTDEERD CCCCCCCCCCCCHHC | 23.70 | 17563356 | |
| 542 | Phosphorylation | KTSQKSVTDEERDSR CCCCCCCCCCHHCCC | 44.79 | 30377154 | |
| 577 | Acetylation | TIIKLVLKFENVSKN HHHHHHHHCCCCCCC | 43.06 | 24489116 | |
| 613 | Ubiquitination | GQSSLVEKKIDEDSL CCHHHHHCCCCHHHH | 47.77 | 23749301 | |
| 614 | Ubiquitination | QSSLVEKKIDEDSLE CHHHHHCCCCHHHHH | 41.71 | 21427232 | |
| 675 | Acetylation | NKHKRALKDSCKNIE CHHHHHHHHHCCCCC | 46.76 | 25381059 | |
| 679 | Ubiquitination | RALKDSCKNIEPIDT HHHHHHCCCCCCCCC | 65.98 | 23749301 | |
| 686 | Phosphorylation | KNIEPIDTPISFRQF CCCCCCCCCCCHHHH | 24.20 | 27214570 | |
| 791 | Ubiquitination | KIIDTPQKTNVIPHG EEECCCCCCCCCCCC | 43.18 | 17644757 | |
| 801 | Ubiquitination | VIPHGFHKFTVTVKV CCCCCCEEEEEEEEE | 40.23 | 17644757 | |
| 868 | Ubiquitination | NAFEWENKISVKSQL HHHCCCCCCCHHHHC | 25.50 | 23749301 | |
| 872 | Ubiquitination | WENKISVKSQLPTLH CCCCCCHHHHCCHHH | 26.20 | 17644757 | |
| 887 | Ubiquitination | AYLRELVKGTNMGIL HHHHHHHCCCCCEEE | 73.05 | 23749301 | |
| 895 | Phosphorylation | GTNMGILTPSESLGE CCCCEEECCCHHCCC | 23.89 | 28889911 | |
| 946 | Ubiquitination | GYVRIRSKGQGLALS EEEEEEECCCCEEEE | 45.46 | 23749301 | |
| 967 | Acetylation | LIAKKTNKLALTHV- HEEHHHCCCCCCCC- | 40.13 | 22865919 |
| 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 COPB_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of COPB_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 COPB_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-181; SER-540 ANDTHR-895, AND MASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND MASSSPECTROMETRY. | |
