| UniProt ID | CDC27_YEAST | |
|---|---|---|
| UniProt AC | P38042 | |
| Protein Name | Anaphase-promoting complex subunit CDC27 | |
| Gene Name | CDC27 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 758 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| 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 | MAVNPELAPFTLSRGIPSFDDQALSTIIQLQDCIQQAIQQLNYSTAEFLAELLYAECSILDKSSVYWSDAVYLYALSLFLNKSYHTAFQISKEFKEYHLGIAYIFGRCALQLSQGVNEAILTLLSIINVFSSNSSNTRINMVLNSNLVHIPDLATLNCLLGNLYMKLDHSKEGAFYHSEALAINPYLWESYEAICKMRATVDLKRVFFDIAGKKSNSHNNNAASSFPSTSLSHFEPRSQPSLYSKTNKNGNNNINNNVNTLFQSSNSPPSTSASSFSSIQHFSRSQQQQANTSIRTCQNKNTQTPKNPAINSKTSSALPNNISMNLVSPSSKQPTISSLAKVYNRNKLLTTPPSKLLNNDRNHQNNNNNNNNNNNNNNNNNNNNNNNNIINKTTFKTPRNLYSSTGRLTTSKKNPRSLIISNSILTSDYSITLPEIMYNFALILRSSSQYNSFKAIRLFESQIPSHIKDTMPWCLVQLGKLHFEIINYDMSLKYFNRLKDLQPARVKDMEIFSTLLWHLHDKVKSSNLANGLMDTMPNKPETWCCIGNLLSLQKDHDAAIKAFEKATQLDPNFAYAYTLQGHEHSSNDSSDSAKTCYRKALACDPQHYNAYYGLGTSAMKLGQYEEALLYFEKARSINPVNVVLICCCGGSLEKLGYKEKALQYYELACHLQPTSSLSKYKMGQLLYSMTRYNVALQTFEELVKLVPDDATAHYLLGQTYRIVGRKKDAIKELTVAMNLDPKGNQVIIDELQKCHMQE | |
| 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 |
|---|---|---|---|---|---|
| 84 | Phosphorylation | SLFLNKSYHTAFQIS HHHHCCCHHHHHHHC | 12.56 | 28889911 | |
| 91 | Phosphorylation | YHTAFQISKEFKEYH HHHHHHHCHHHHHHH | 18.49 | 28889911 | |
| 260 | Phosphorylation | NINNNVNTLFQSSNS CCCHHHHHHHHCCCC | 25.35 | 30377154 | |
| 265 | Phosphorylation | VNTLFQSSNSPPSTS HHHHHHCCCCCCCCC | 30.46 | 30377154 | |
| 267 | Phosphorylation | TLFQSSNSPPSTSAS HHHHCCCCCCCCCHH | 39.89 | 28889911 | |
| 270 | Phosphorylation | QSSNSPPSTSASSFS HCCCCCCCCCHHHHH | 38.08 | 30377154 | |
| 274 | Phosphorylation | SPPSTSASSFSSIQH CCCCCCHHHHHHHHH | 31.51 | 30377154 | |
| 275 | Phosphorylation | PPSTSASSFSSIQHF CCCCCHHHHHHHHHH | 28.94 | 30377154 | |
| 277 | Phosphorylation | STSASSFSSIQHFSR CCCHHHHHHHHHHCH | 28.60 | 30377154 | |
| 292 | Phosphorylation | SQQQQANTSIRTCQN HHHHHHHHHHHHHCC | 28.66 | 30377154 | |
| 302 | Phosphorylation | RTCQNKNTQTPKNPA HHHCCCCCCCCCCCC | 35.11 | 23749301 | |
| 304 | Phosphorylation | CQNKNTQTPKNPAIN HCCCCCCCCCCCCCC | 33.90 | 23749301 | |
| 312 | Phosphorylation | PKNPAINSKTSSALP CCCCCCCCCCCCCCC | 31.06 | 21551504 | |
| 328 | Phosphorylation | NISMNLVSPSSKQPT CEEECCCCCCCCCCC | 23.41 | 21440633 | |
| 331 | Phosphorylation | MNLVSPSSKQPTISS ECCCCCCCCCCCHHH | 38.40 | 27017623 | |
| 350 | Phosphorylation | YNRNKLLTTPPSKLL HCCCCCCCCCHHHHC | 47.93 | 28889911 | |
| 351 | Phosphorylation | NRNKLLTTPPSKLLN CCCCCCCCCHHHHCC | 32.92 | 20377248 | |
| 354 | Phosphorylation | KLLTTPPSKLLNNDR CCCCCCHHHHCCCCC | 36.82 | 27214570 | |
| 397 | Phosphorylation | INKTTFKTPRNLYSS CCCCCCCCCCCHHHC | 24.24 | 23749301 | |
| 411 | Phosphorylation | STGRLTTSKKNPRSL CCCCCCCCCCCCCEE | 36.08 | 28889911 |
| 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 CDC27_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDC27_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 CDC27_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-354, AND MASSSPECTROMETRY. | |
