| UniProt ID | CDC23_YEAST | |
|---|---|---|
| UniProt AC | P16522 | |
| Protein Name | Anaphase-promoting complex subunit CDC23 | |
| Gene Name | CDC23 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 626 | |
| Subcellular Localization | Nucleus. Chromosome, centromere, kinetochore. Associated with the kinetochore. | |
| Protein Description | Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.. | |
| Protein Sequence | MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM | |
| 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 |
|---|---|---|---|---|---|
| 52 | Phosphorylation | EAIDVDQTHSLADES HHCCCCCCCCCCCCC | 14.68 | 21440633 | |
| 54 | Phosphorylation | IDVDQTHSLADESPL CCCCCCCCCCCCCCC | 28.74 | 21440633 | |
| 59 | Phosphorylation | THSLADESPLRNKQG CCCCCCCCCCCCCCC | 29.76 | 21440633 | |
| 117 | Acetylation | DVTNPYLKFLKLYSK CCCCHHHHHHHHHHH | 42.69 | 24489116 | |
| 159 | Phosphorylation | ANKDGDGSGNEDINQ CCCCCCCCCCCCCCH | 43.09 | 23749301 | |
| 368 | Phosphorylation | YRLNDLETYSNILYV CCCCHHHHHHHHHHH | 39.28 | 25882841 | |
| 370 | Phosphorylation | LNDLETYSNILYVMQ CCHHHHHHHHHHHHH | 25.47 | 28889911 | |
| 374 | Phosphorylation | ETYSNILYVMQKNSK HHHHHHHHHHHHCCH | 7.06 | 25882841 | |
| 493 | Phosphorylation | YYFQKACTLKPWDRR HHHHHHHCCCCCCHH | 42.55 | 22369663 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 59 | S | Phosphorylation | Kinase | CDC28 | P00546 | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDC23_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 CDC23_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 SER-59, AND MASSSPECTROMETRY. | |
| "Phosphorylation by Cdc28 activates the Cdc20-dependent activity ofthe anaphase-promoting complex."; Rudner A.D., Murray A.W.; J. Cell Biol. 149:1377-1390(2000). Cited for: FUNCTION, AND PHOSPHORYLATION AT SER-59. | |
