| UniProt ID | UBC3_YEAST | |
|---|---|---|
| UniProt AC | P14682 | |
| Protein Name | Ubiquitin-conjugating enzyme E2-34 kDa | |
| Gene Name | CDC34 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 295 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Catalyzes the covalent attachment of ubiquitin to other proteins. Capable, in vitro, to ubiquitinate histone H2A.; Mediates the initiation of DNA replication (transition of G1 to S phase in cell cycle). Essential component of the E3 ubiquitin ligase complex SCF (SKP1-CUL1-F-box protein), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Involved in the regulation of methionine biosynthesis genes and in the degradation of CDC6 together with CDC4 and CDC53.. | |
| Protein Sequence | MSSRKSTASSLLLRQYRELTDPKKAIPSFHIELEDDSNIFTWNIGVMVLNEDSIYHGGFFKAQMRFPEDFPFSPPQFRFTPAIYHPNVYRDGRLCISILHQSGDPMTDEPDAETWSPVQTVESVLISIVSLLEDPNINSPANVDAAVDYRKNPEQYKQRVKMEVERSKQDIPKGFIMPTSESAYISQSKLDEPESNKDMADNFWYDSDLDDDENGSVILQDDDYDDGNNHIPFEDDDVYNYNDNDDDDERIEFEDDDDDDDDSIDNDSVMDRKQPHKAEDESEDVEDVERVSKKI | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MSSRKSTASS -----CCCHHHHHHH | 42.29 | 30377154 | |
| 5 | Ubiquitination | ---MSSRKSTASSLL ---CCCHHHHHHHHH | 54.85 | 17644757 | |
| 7 | Phosphorylation | -MSSRKSTASSLLLR -CCCHHHHHHHHHHH | 33.33 | 21440633 | |
| 9 | Phosphorylation | SSRKSTASSLLLRQY CCHHHHHHHHHHHHH | 22.93 | 30377154 | |
| 10 | Phosphorylation | SRKSTASSLLLRQYR CHHHHHHHHHHHHHH | 22.14 | 28889911 | |
| 151 | Ubiquitination | DAAVDYRKNPEQYKQ CHHCCCCCCHHHHHH | 71.30 | 23749301 | |
| 157 | Ubiquitination | RKNPEQYKQRVKMEV CCCHHHHHHHHHHHH | 31.18 | 23749301 | |
| 161 | Ubiquitination | EQYKQRVKMEVERSK HHHHHHHHHHHHHHC | 31.37 | 23749301 | |
| 168 | Ubiquitination | KMEVERSKQDIPKGF HHHHHHHCCCCCCCC | 59.20 | 23749301 | |
| 179 | Phosphorylation | PKGFIMPTSESAYIS CCCCCCCCCHHHEEC | 27.96 | 29136822 | |
| 180 | Phosphorylation | KGFIMPTSESAYISQ CCCCCCCCHHHEECH | 24.55 | 21440633 | |
| 182 | Phosphorylation | FIMPTSESAYISQSK CCCCCCHHHEECHHH | 26.58 | 29136822 | |
| 184 | Phosphorylation | MPTSESAYISQSKLD CCCCHHHEECHHHCC | 15.47 | 29136822 | |
| 186 | Phosphorylation | TSESAYISQSKLDEP CCHHHEECHHHCCCC | 18.74 | 21551504 | |
| 188 | Phosphorylation | ESAYISQSKLDEPES HHHEECHHHCCCCCC | 28.53 | 29136822 | |
| 189 | Ubiquitination | SAYISQSKLDEPESN HHEECHHHCCCCCCC | 52.93 | 23749301 | |
| 189 | Acetylation | SAYISQSKLDEPESN HHEECHHHCCCCCCC | 52.93 | 24489116 | |
| 195 | Phosphorylation | SKLDEPESNKDMADN HHCCCCCCCCCCCCC | 60.95 | 25521595 | |
| 207 | Phosphorylation | ADNFWYDSDLDDDEN CCCCCCCCCCCCCCC | 25.11 | 17461777 | |
| 216 | Phosphorylation | LDDDENGSVILQDDD CCCCCCCCEEEECCC | 19.98 | 28889911 | |
| 263 | Phosphorylation | DDDDDDDSIDNDSVM CCCCCCCCCCCCCHH | 38.54 | 24930733 | |
| 268 | Phosphorylation | DDSIDNDSVMDRKQP CCCCCCCCHHCCCCC | 26.12 | 24930733 | |
| 282 | Phosphorylation | PHKAEDESEDVEDVE CCCCCCCCCCHHHHH | 51.96 | 25533186 | |
| 292 | Phosphorylation | VEDVERVSKKI---- HHHHHHHHHCC---- | 34.16 | 28889911 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 282 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UBC3_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 UBC3_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-10; SER-182; SER-186;SER-188 AND SER-292, AND MASS SPECTROMETRY. | |
