| UniProt ID | COPD_YEAST | |
|---|---|---|
| UniProt AC | P43621 | |
| Protein Name | Coatomer subunit delta | |
| Gene Name | RET2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 546 | |
| 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 side o |
|
| 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 (By similarity).. | |
| Protein Sequence | MVVLAASITTRQGKPLLSRQFKDLSKDRVLELLSNFQNLVSEISSDHTFVEDKHVRYVYRPFDNYYIILITNRQSNIIKDLATLNLFSQTINSYLSSFQDQEIFHNAFEILSSFDEIVSMGGYKENLSFTQVQTYLSMESHEERIQEIIERNKEIEATEERKRRAKEIARKEHERKHGFMSSNGDYDGANRFMGSKDPNVTNAINSYYSHASPAAQQSYLQSSHAAAAEVAPVASPMATSQRAGHSATGGMKLGGGAGRRAGAAPRPSAISSASSGTPPPPEEDVPENNGILISIKEVINAEFSRDGTIHSSELKGVLELRINDHDLSHSNLKLADSIDVRDKSFQFKTHPNIDKQSFLSTKLISLRDKSKAFPANDQSLGVLRWRKVAPAEDDSLIPLTLTTWVSPSESQQGFDVIIEYESVLETELADVIFTIPVFPQEPVDINTESSTCSDAEVVNMDQEMGTSIKISKIAANDAGALAFTIEAPYEDALYPMTVSFQESTRDKLAKSFTGMAIQSVVMANDHDQELPYDVITSLKSDEYLVQ | |
| 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 |
|---|---|---|---|---|---|
| 10 | Phosphorylation | VLAASITTRQGKPLL EEEEEEECCCCCCCC | 21.23 | 17563356 | |
| 14 | Ubiquitination | SITTRQGKPLLSRQF EEECCCCCCCCCHHH | 24.93 | 23749301 | |
| 53 | Ubiquitination | DHTFVEDKHVRYVYR CCCCCCCCCEEEEEE | 30.41 | 23749301 | |
| 153 | Acetylation | QEIIERNKEIEATEE HHHHHHHHHHHHHHH | 67.31 | 22865919 | |
| 153 | Ubiquitination | QEIIERNKEIEATEE HHHHHHHHHHHHHHH | 67.31 | 23749301 | |
| 176 | Acetylation | ARKEHERKHGFMSSN HHHHHHHHHCCCCCC | 45.13 | 22865919 | |
| 181 | Phosphorylation | ERKHGFMSSNGDYDG HHHHCCCCCCCCCCH | 20.56 | 28889911 | |
| 182 | Phosphorylation | RKHGFMSSNGDYDGA HHHCCCCCCCCCCHH | 32.80 | 28889911 | |
| 201 | Phosphorylation | GSKDPNVTNAINSYY CCCCCCHHHHHHHHH | 26.10 | 30377154 | |
| 212 | Phosphorylation | NSYYSHASPAAQQSY HHHHCCCCHHHHHHH | 15.06 | 27738172 | |
| 218 | Phosphorylation | ASPAAQQSYLQSSHA CCHHHHHHHHHHHHH | 18.74 | 30377154 | |
| 235 | Phosphorylation | AEVAPVASPMATSQR HHHHCCCCCCCCCCC | 18.55 | 30377154 | |
| 246 | Phosphorylation | TSQRAGHSATGGMKL CCCCCCCCCCCCCCC | 26.97 | 28889911 | |
| 248 | Phosphorylation | QRAGHSATGGMKLGG CCCCCCCCCCCCCCC | 36.96 | 28889911 | |
| 252 | Acetylation | HSATGGMKLGGGAGR CCCCCCCCCCCCCCC | 47.45 | 25381059 | |
| 268 | Phosphorylation | AGAAPRPSAISSASS CCCCCCCHHHCCCCC | 39.24 | 22369663 | |
| 271 | Phosphorylation | APRPSAISSASSGTP CCCCHHHCCCCCCCC | 21.40 | 22369663 | |
| 272 | Phosphorylation | PRPSAISSASSGTPP CCCHHHCCCCCCCCC | 26.51 | 22369663 | |
| 274 | Phosphorylation | PSAISSASSGTPPPP CHHHCCCCCCCCCCC | 31.11 | 22369663 | |
| 275 | Phosphorylation | SAISSASSGTPPPPE HHHCCCCCCCCCCCH | 46.53 | 22369663 | |
| 277 | Phosphorylation | ISSASSGTPPPPEED HCCCCCCCCCCCHHH | 34.27 | 22369663 | |
| 294 | Phosphorylation | ENNGILISIKEVINA CCCCEEEEHHHHHCC | 24.94 | 22369663 | |
| 328 | Phosphorylation | RINDHDLSHSNLKLA EECCCCCCCCCCCCC | 30.81 | 29734811 | |
| 333 | Ubiquitination | DLSHSNLKLADSIDV CCCCCCCCCCCCCCC | 45.97 | 24961812 | |
| 333 | Acetylation | DLSHSNLKLADSIDV CCCCCCCCCCCCCCC | 45.97 | 24489116 | |
| 337 | Phosphorylation | SNLKLADSIDVRDKS CCCCCCCCCCCCCCC | 18.32 | 21440633 | |
| 344 | Phosphorylation | SIDVRDKSFQFKTHP CCCCCCCCEECCCCC | 28.68 | 21440633 | |
| 348 | Acetylation | RDKSFQFKTHPNIDK CCCCEECCCCCCCCH | 34.83 | 24489116 | |
| 355 | Acetylation | KTHPNIDKQSFLSTK CCCCCCCHHHHHHHH | 44.00 | 24489116 |
| 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 COPD_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of COPD_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 COPD_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-268; SER-272 ANDTHR-277, 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 THR-10 AND THR-277, AND MASSSPECTROMETRY. | |
