| UniProt ID | CDC16_YEAST | |
|---|---|---|
| UniProt AC | P09798 | |
| Protein Name | Anaphase-promoting complex subunit CDC16 | |
| Gene Name | CDC16 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 840 | |
| Subcellular Localization | 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 | MKFCLYCCHCYIVICGKATHYYKSSKATSNLKSSNRVLMRNPMSPSEQHSQHNSTLAASPFVSNVSAARTQQSLPTDAQNDRLQQPWNRTNTATSPYQSLANSPLIQKLQANIMTPHQPSANSNSNSNSITGNVVNDNNLLASMSKNSMFGSTIPSTLRKVSLQREYKDSVDGVVRDEDNDEDVHNNGDAAANANNDRESKLGHNGPLTTTTLTTTTTATQLDVSELSAIERLRLWRFDALMQHMYRTAEYIADKVYNISNDPDDAFWLGQVYYNNNQYVRAVELITRNNLDGVNILCRYLLGLSFVKLQRFDDALDVIGEYNPFSEDPSTTAANTMSNNGNNSNTSQPVTDGGIKMESSLCFLRGKIYFAQNNFNKARDAFREAILVDIKNFEAFEMLLSKNLLTPQEEWDLFDSLDFKEFGEDKEIMKNLYKINLSKYINTEDITKSNEILAKDYKLADNVDVVRSKVDICYTQCKFNECLELCETVLENDEFNTNILPAYIGCLYELSNKNKLFLLSHRLAETFPKSAITWFSVATYYMSLDRISEAQKYYSKSSILDPSFAAAWLGFAHTYALEGEQDQALTAYSTASRFFPGMHLPKLFLGMQFMAMNSLNLAESYFVLAYDICPNDPLVLNEMGVMYFKKNEFVKAKKYLKKALEVVKDLDPSSRTTISIQLNLGHTYRKLNENEIAIKCFRCVLEKNDKNSEIHCSLGYLYLKTKKLQKAIDHLHKSLYLKPNNSSATALLKNALELNVTLSLDASHPLIDKSNLMSQASKDKASLNKKRSSLTYDPVNMAKRLRTQKEIFDQNNKALRKGGHDSKTGSNNADDDFDADMELE | |
| 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 |
|---|---|---|---|---|---|
| 44 | Phosphorylation | VLMRNPMSPSEQHSQ EEECCCCCHHHHHHH | 26.91 | 28889911 | |
| 54 | Phosphorylation | EQHSQHNSTLAASPF HHHHHCCCCCCCCCC | 23.75 | 21082442 | |
| 59 | Phosphorylation | HNSTLAASPFVSNVS CCCCCCCCCCCCCCC | 17.17 | 28889911 | |
| 73 | Phosphorylation | SAARTQQSLPTDAQN CHHCHHCCCCCHHHC | 26.88 | 30377154 | |
| 92 | Phosphorylation | QPWNRTNTATSPYQS CCCCCCCCCCCHHHH | 30.60 | 23749301 | |
| 94 | Phosphorylation | WNRTNTATSPYQSLA CCCCCCCCCHHHHHC | 28.35 | 27017623 | |
| 95 | Phosphorylation | NRTNTATSPYQSLAN CCCCCCCCHHHHHCC | 21.10 | 23749301 | |
| 97 | Phosphorylation | TNTATSPYQSLANSP CCCCCCHHHHHCCCH | 15.53 | 27017623 | |
| 103 | Phosphorylation | PYQSLANSPLIQKLQ HHHHHCCCHHHHHHH | 18.57 | 23749301 | |
| 115 | Phosphorylation | KLQANIMTPHQPSAN HHHHHCCCCCCCCCC | 17.52 | 28889911 | |
| 148 | Phosphorylation | LASMSKNSMFGSTIP CHHHCCCCCCCCCCC | 21.16 | 24603354 | |
| 152 | Phosphorylation | SKNSMFGSTIPSTLR CCCCCCCCCCCHHHH | 16.34 | 28889911 | |
| 153 | Phosphorylation | KNSMFGSTIPSTLRK CCCCCCCCCCHHHHH | 36.97 | 27017623 | |
| 157 | Phosphorylation | FGSTIPSTLRKVSLQ CCCCCCHHHHHHHCC | 25.81 | 24603354 | |
| 162 | Phosphorylation | PSTLRKVSLQREYKD CHHHHHHHCCHHHHH | 23.09 | 21440633 | |
| 406 | Phosphorylation | LLSKNLLTPQEEWDL HHHCCCCCCHHHHHC | 26.54 | 28889911 | |
| 447 | Phosphorylation | YINTEDITKSNEILA CCCHHHCCCCCCHHH | 40.52 | 28889911 | |
| 757 | Phosphorylation | NALELNVTLSLDASH HHHHCCEEEEECCCC | 15.00 | 21440633 | |
| 770 | Phosphorylation | SHPLIDKSNLMSQAS CCCCCCHHHHCCHHH | 31.29 | 21440633 | |
| 778 | Acetylation | NLMSQASKDKASLNK HHCCHHHHCHHHHHH | 67.28 | 25381059 | |
| 788 | Phosphorylation | ASLNKKRSSLTYDPV HHHHHHHHCCCCCHH | 38.28 | 21440633 | |
| 789 | Phosphorylation | SLNKKRSSLTYDPVN HHHHHHHCCCCCHHH | 28.85 | 20377248 | |
| 791 | Phosphorylation | NKKRSSLTYDPVNMA HHHHHCCCCCHHHHH | 28.03 | 28889911 | |
| 792 | Phosphorylation | KKRSSLTYDPVNMAK HHHHCCCCCHHHHHH | 24.44 | 19779198 |
| 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 CDC16_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDC16_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 CDC16_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-789, AND MASSSPECTROMETRY. | |
