| UniProt ID | CDK1_YEAST | |
|---|---|---|
| UniProt AC | P00546 | |
| Protein Name | Cyclin-dependent kinase 1 | |
| Gene Name | CDC28 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 298 | |
| Subcellular Localization | ||
| Protein Description | This protein is essential for the completion of the start, the controlling event, in the cell cycle. More than 200 substrates have been identified.. | |
| Protein Sequence | MSGELANYKRLEKVGEGTYGVVYKALDLRPGQGQRVVALKKIRLESEDEGVPSTAIREISLLKELKDDNIVRLYDIVHSDAHKLYLVFEFLDLDLKRYMEGIPKDQPLGADIVKKFMMQLCKGIAYCHSHRILHRDLKPQNLLINKDGNLKLGDFGLARAFGVPLRAYTHEIVTLWYRAPEVLLGGKQYSTGVDTWSIGCIFAEMCNRKPIFSGDSEIDQIFKIFRVLGTPNEAIWPDIVYLPDFKPSFPQWRRKDLSQVVPSLDPRGIDLLDKLLAYDPINRISARRAAIHPYFQES | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSGELANYK ------CCCCCCCCC | 40.76 | 22814378 | |
| 18 | Phosphorylation | LEKVGEGTYGVVYKA HHCCCCCCCEEEEEE | 16.89 | 22890988 | |
| 19 | Phosphorylation | EKVGEGTYGVVYKAL HCCCCCCCEEEEEEE | 20.84 | 8253069 | |
| 23 | Phosphorylation | EGTYGVVYKALDLRP CCCCEEEEEEEECCC | 6.53 | 22890988 | |
| 24 | Acetylation | GTYGVVYKALDLRPG CCCEEEEEEEECCCC | 30.75 | 24489116 | |
| 46 | Phosphorylation | LKKIRLESEDEGVPS EEEEECCCCCCCCCH | 55.74 | 21440633 | |
| 54 | Phosphorylation | EDEGVPSTAIREISL CCCCCCHHHHHHHHH | 21.75 | 27017623 | |
| 138 | Acetylation | RILHRDLKPQNLLIN CEECCCCCCCCEEEC | 49.17 | 24489116 | |
| 138 | Ubiquitination | RILHRDLKPQNLLIN CEECCCCCCCCEEEC | 49.17 | 24961812 | |
| 146 | Acetylation | PQNLLINKDGNLKLG CCCEEECCCCCCCCC | 61.08 | 24489116 | |
| 168 | Phosphorylation | FGVPLRAYTHEIVTL HCCCCCCEECCEEEE | 11.38 | 22890988 | |
| 169 | Phosphorylation | GVPLRAYTHEIVTLW CCCCCCEECCEEEEE | 16.43 | 22369663 | |
| 174 | Phosphorylation | AYTHEIVTLWYRAPE CEECCEEEEEEECCC | 19.75 | 22369663 | |
| 190 | Phosphorylation | LLGGKQYSTGVDTWS ECCCEECCCCCCCCH | 19.05 | 28889911 | |
| 191 | Phosphorylation | LGGKQYSTGVDTWSI CCCEECCCCCCCCHH | 35.97 | 28889911 | |
| 255 | Ubiquitination | SFPQWRRKDLSQVVP CCCHHHHCCHHHHCC | 55.22 | 22817900 | |
| 298 | Phosphorylation | IHPYFQES------- HCHHHCCC------- | 34.44 | 21440633 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 46 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDK1_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 CDK1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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 TYR-19, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19 AND THR-169, AND MASSSPECTROMETRY. | |
