| UniProt ID | CDC20_YEAST | |
|---|---|---|
| UniProt AC | P26309 | |
| Protein Name | APC/C activator protein CDC20 | |
| Gene Name | CDC20 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 610 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Activator protein that regulates the ubiquitin ligase activity and substrate specificity of the anaphase promoting complex/cyclosome (APC/C). At the metaphase-to-anaphase transition, recognizes and binds proteins containing a D-box including the B-type cyclins CLB2 and CLB5, HSL1 and securin PDS1, and recruits them in a C-box-dependent manner to the APC/C for ubiquitination and subsequent proteolysis. Required for sister chromatid separation and disassembly of the mitotic spindle. Target of the spindle checkpoint pathway through participation in the mitotic checkpoint complex (MCC) and the MAD2-CDC20 subcomplex. MCC and presumably the MAD2-CDC20 subcomplex inhibit the ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) by preventing its activation by CDC20 until proper attachment of all chromosomes to the spindle.. | |
| Protein Sequence | MPESSRDKGNAAISGNRSVLSIASPTKLNILSSDWSRNQGKVSKNSLKRSSSLNIRNSKRPSLQASANSIYSRPKITIGAPPLIRRDSSFFKDEFDAKKDKATFSAYSSRSYPTIGSESVVSQTSLSQPTTSREVDEQFTVAADRYIPILQGASQNKVDPETLHEALPPPNASPISHLRAQTKIVFKQNVAEACGLDMNKRILQYMPEPPKCSSLRQKSYIMKKRTHYSYQQEQKIPDLIKLRKINTNPERILDAPGFQDDFYLNLLSWSKKNVLAIALDTALYLWNATTGDVSLLTDFENTTICSVTWSDDDCHISIGKEDGNTEIWDVETMSLIRTMRSGLGVRIGSLSWLDTLIATGSRSGEIQINDVRIKQHIVSTWAEHTGEVCGLSYKSDGLQLASGGNDNTVMIWDTRTSLPQFSKKTHTAAVKALSWCPYSPNILASGGGQTDKHIHFWNSITGARVGSINTGSQVSSLHWGQSHTSTNGGMMNKEIVATGGNPENAISVYNYETKFKVAEVVHAHEARICCSQLSPDGTTLATVGGDENLKFYKIFDPRCTGRSREDGLMDGMLGLIGKEGCRTNDKENRSKNSSEIHTRRPSSTSQYLIR | |
| 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 |
|---|---|---|---|---|---|
| 21 | Phosphorylation | SGNRSVLSIASPTKL CCCCEEEECCCCCEE | 17.60 | 21440633 | |
| 24 | Phosphorylation | RSVLSIASPTKLNIL CEEEECCCCCEEEEC | 31.28 | 21551504 | |
| 52 | Phosphorylation | NSLKRSSSLNIRNSK HHHHCCCCCCCCCCC | 27.04 | 14743219 | |
| 59 | Ubiquitination | SLNIRNSKRPSLQAS CCCCCCCCCCCHHHH | 72.39 | 17644757 | |
| 75 | Ubiquitination | NSIYSRPKITIGAPP CCHHCCCCCEECCCC | 51.91 | 17644757 | |
| 88 | Phosphorylation | PPLIRRDSSFFKDEF CCCCCCCCHHCCCCC | 27.51 | 14743219 | |
| 89 | Phosphorylation | PLIRRDSSFFKDEFD CCCCCCCHHCCCCCC | 38.70 | 21440633 | |
| 127 | Phosphorylation | VVSQTSLSQPTTSRE CCCCCCCCCCCCCCC | 33.60 | 27017623 | |
| 146 | Phosphorylation | FTVAADRYIPILQGA HHHHHHHHHHHHCCC | 16.17 | 28889911 | |
| 173 | Phosphorylation | ALPPPNASPISHLRA HCCCCCCCCCHHHHH | 29.43 | 21440633 | |
| 176 | Phosphorylation | PPNASPISHLRAQTK CCCCCCCHHHHHCCE | 21.61 | 27017623 | |
| 182 | Phosphorylation | ISHLRAQTKIVFKQN CHHHHHCCEEEEECC | 23.04 | 21551504 | |
| 241 | Acetylation | QKIPDLIKLRKINTN CCCCCHHHHHCCCCC | 49.92 | 24489116 | |
| 247 | Phosphorylation | IKLRKINTNPERILD HHHHCCCCCHHHHHC | 56.47 | 28889911 | |
| 431 | Ubiquitination | KTHTAAVKALSWCPY CCCHHHHHHHHCCCC | 38.59 | 17644757 | |
| 452 | Ubiquitination | SGGGQTDKHIHFWNS CCCCCCCCCCEEECC | 48.09 | 17644757 | |
| 493 | Ubiquitination | TNGGMMNKEIVATGG CCCCCCCCEEEEECC | 30.81 | 17644757 | |
| 514 | Ubiquitination | SVYNYETKFKVAEVV EEEECCCCEEEEEEE | 31.11 | 17644757 | |
| 516 | Ubiquitination | YNYETKFKVAEVVHA EECCCCEEEEEEEEH | 41.93 | 17644757 | |
| 550 | Ubiquitination | VGGDENLKFYKIFDP ECCCCCEEEEEECCC | 59.22 | 17644757 | |
| 603 | Phosphorylation | IHTRRPSSTSQYLIR CCCCCCCCCHHHCCC | 34.46 | 27017623 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDC20_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 CDC20_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 TYR-146, AND MASSSPECTROMETRY. | |
