UniProt ID | CDC20_HUMAN | |
---|---|---|
UniProt AC | Q12834 | |
Protein Name | Cell division cycle protein 20 homolog | |
Gene Name | CDC20 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 499 | |
Subcellular Localization | Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle pole . | |
Protein Description | Required for full ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) and may confer substrate specificity upon the complex. Is regulated by MAD2L1: in metaphase the MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the CDC20-APC/C binary complex is active in degrading substrates. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces presynaptic differentiation.. | |
Protein Sequence | MAQFAFESDLHSLLQLDAPIPNAPPARWQRKAKEAAGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRYIPHRSAAQMEVASFLLSKENQPENSQTPTKKEHQKAWALNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGSSRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQMEQPGEYISSVAWIKEGNYLAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLSWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPDGRHLASGGNDNLVNVWPSAPGEGGWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAHSQVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTSRVLSLTMSPDGATVASAAADETLRLWRCFELDPARRREREKASAAKSSLIHQGIR | |
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 |
---|---|---|---|---|---|
31 | Ubiquitination | PPARWQRKAKEAAGP CCHHHHHHHHHHCCC | 49.03 | - | |
33 | Methylation | ARWQRKAKEAAGPAP HHHHHHHHHHCCCCC | 51.42 | - | |
41 | Phosphorylation | EAAGPAPSPMRAANR HHCCCCCCHHHHHHH | 33.17 | 19664994 | |
49 | Phosphorylation | PMRAANRSHSAGRTP HHHHHHHCCCCCCCC | 22.92 | 30576142 | |
51 | Phosphorylation | RAANRSHSAGRTPGR HHHHHCCCCCCCCCC | 33.39 | 30576142 | |
55 | Phosphorylation | RSHSAGRTPGRTPGK HCCCCCCCCCCCCCC | 29.22 | 25849741 | |
59 | Phosphorylation | AGRTPGRTPGKSSSK CCCCCCCCCCCCCCC | 42.16 | 25849741 | |
62 | Ubiquitination | TPGRTPGKSSSKVQT CCCCCCCCCCCCCCC | 48.66 | 21906983 | |
63 | Phosphorylation | PGRTPGKSSSKVQTT CCCCCCCCCCCCCCC | 45.84 | 30576142 | |
64 | Phosphorylation | GRTPGKSSSKVQTTP CCCCCCCCCCCCCCC | 37.35 | 18767875 | |
65 | Phosphorylation | RTPGKSSSKVQTTPS CCCCCCCCCCCCCCC | 43.89 | 29449344 | |
66 | Ubiquitination | TPGKSSSKVQTTPSK CCCCCCCCCCCCCCC | 40.07 | 21906983 | |
66 | Acetylation | TPGKSSSKVQTTPSK CCCCCCCCCCCCCCC | 40.07 | 22014574 | |
69 | Phosphorylation | KSSSKVQTTPSKPGG CCCCCCCCCCCCCCC | 43.60 | 30266825 | |
70 | Phosphorylation | SSSKVQTTPSKPGGD CCCCCCCCCCCCCCC | 14.42 | 29255136 | |
72 | Phosphorylation | SKVQTTPSKPGGDRY CCCCCCCCCCCCCCC | 49.76 | 22167270 | |
73 | Ubiquitination | KVQTTPSKPGGDRYI CCCCCCCCCCCCCCC | 49.22 | 21906983 | |
79 | Phosphorylation | SKPGGDRYIPHRSAA CCCCCCCCCCCCHHH | 24.44 | 23312004 | |
84 | Phosphorylation | DRYIPHRSAAQMEVA CCCCCCCHHHHHHHH | 25.56 | 27050516 | |
92 | Phosphorylation | AAQMEVASFLLSKEN HHHHHHHHHHHCCCC | 22.92 | 15525512 | |
96 | Phosphorylation | EVASFLLSKENQPEN HHHHHHHCCCCCCCC | 39.82 | 26074081 | |
97 | Ubiquitination | VASFLLSKENQPENS HHHHHHCCCCCCCCC | 61.73 | 21906983 | |
104 | Phosphorylation | KENQPENSQTPTKKE CCCCCCCCCCCCHHH | 33.50 | 23401153 | |
106 | Phosphorylation | NQPENSQTPTKKEHQ CCCCCCCCCCHHHHH | 32.52 | 22167270 | |
108 | Phosphorylation | PENSQTPTKKEHQKA CCCCCCCCHHHHHHH | 59.12 | 29255136 | |
109 | Sumoylation | ENSQTPTKKEHQKAW CCCCCCCHHHHHHHH | 58.32 | - | |
109 | Ubiquitination | ENSQTPTKKEHQKAW CCCCCCCHHHHHHHH | 58.32 | 21906983 | |
109 | Sumoylation | ENSQTPTKKEHQKAW CCCCCCCHHHHHHHH | 58.32 | - | |
110 | Ubiquitination | NSQTPTKKEHQKAWA CCCCCCHHHHHHHHH | 64.01 | 22817900 | |
114 | Ubiquitination | PTKKEHQKAWALNLN CCHHHHHHHHHHCCC | 48.04 | 21906983 | |
129 | Ubiquitination | GFDVEEAKILRLSGK CCCHHHHHHEEECCC | 45.62 | 21906983 | |
134 | Phosphorylation | EAKILRLSGKPQNAP HHHHEEECCCCCCCC | 38.03 | 28985074 | |
136 | Ubiquitination | KILRLSGKPQNAPEG HHEEECCCCCCCCCH | 39.80 | 23000965 | |
144 | Phosphorylation | PQNAPEGYQNRLKVL CCCCCCHHHHHHHHH | 10.84 | 28152594 | |
149 | Ubiquitination | EGYQNRLKVLYSQKA CHHHHHHHHHHCCCC | 27.27 | 22505724 | |
149 | Acetylation | EGYQNRLKVLYSQKA CHHHHHHHHHHCCCC | 27.27 | 25953088 | |
152 | Phosphorylation | QNRLKVLYSQKATPG HHHHHHHHCCCCCCC | 16.43 | 23312004 | |
153 | Phosphorylation | NRLKVLYSQKATPGS HHHHHHHCCCCCCCC | 22.50 | 15525512 | |
155 | Ubiquitination | LKVLYSQKATPGSSR HHHHHCCCCCCCCCC | 48.57 | 21906983 | |
157 | Phosphorylation | VLYSQKATPGSSRKT HHHCCCCCCCCCCCC | 34.91 | 15525512 | |
160 | Phosphorylation | SQKATPGSSRKTCRY CCCCCCCCCCCCCCC | 28.33 | 30576142 | |
161 | Phosphorylation | QKATPGSSRKTCRYI CCCCCCCCCCCCCCC | 43.65 | 15525512 | |
164 | Phosphorylation | TPGSSRKTCRYIPSL CCCCCCCCCCCCCCC | 10.91 | 29083192 | |
167 | Phosphorylation | SSRKTCRYIPSLPDR CCCCCCCCCCCCCCC | 21.23 | 29083192 | |
170 | Phosphorylation | KTCRYIPSLPDRILD CCCCCCCCCCCCCCC | 42.87 | 29083192 | |
174 | Methylation | YIPSLPDRILDAPEI CCCCCCCCCCCCHHH | 29.45 | - | |
259 | Ubiquitination | LWDVQQQKRLRNMTS EECHHHHHHHHHCCC | 49.41 | 21906983 | |
266 | Phosphorylation | KRLRNMTSHSARVGS HHHHHCCCCCCCCCC | 12.50 | 30576142 | |
268 | Phosphorylation | LRNMTSHSARVGSLS HHHCCCCCCCCCCEE | 19.96 | 26329039 | |
282 | Phosphorylation | SWNSYILSSGSRSGH ECCEEEECCCCCCCC | 24.08 | 30576142 | |
285 | Phosphorylation | SYILSSGSRSGHIHH EEEECCCCCCCCCEE | 25.81 | - | |
304 | Phosphorylation | VAEHHVATLSGHSQE EEEEEEEEECCCCCE | 21.99 | 26552605 | |
306 | Phosphorylation | EHHVATLSGHSQEVC EEEEEEECCCCCEEC | 30.06 | 26552605 | |
309 | Phosphorylation | VATLSGHSQEVCGLR EEEECCCCCEECCCE | 31.40 | 26552605 | |
435 | Ubiquitination | WKYPTMAKVAELKGH EECCCHHHHHHHCCC | 31.02 | 21906983 | |
440 | Ubiquitination | MAKVAELKGHTSRVL HHHHHHHCCCCEEEE | 39.90 | 21906983 | |
448 | Phosphorylation | GHTSRVLSLTMSPDG CCCEEEEEEEECCCC | 20.95 | 22817900 | |
457 | Phosphorylation | TMSPDGATVASAAAD EECCCCCHHHHHHHH | 23.33 | 22817900 | |
466 | Phosphorylation | ASAAADETLRLWRCF HHHHHHHHHHHHHHH | 20.09 | 22817900 | |
485 | Ubiquitination | ARRREREKASAAKSS HHHHHHHHHHHHHHH | 54.59 | 23000965 | |
487 | Phosphorylation | RREREKASAAKSSLI HHHHHHHHHHHHHHH | 39.57 | 28555341 | |
490 | Sumoylation | REKASAAKSSLIHQG HHHHHHHHHHHHHCC | 40.05 | - | |
490 | Ubiquitination | REKASAAKSSLIHQG HHHHHHHHHHHHHCC | 40.05 | 23000965 | |
490 | Sumoylation | REKASAAKSSLIHQG HHHHHHHHHHHHHCC | 40.05 | - | |
490 | Acetylation | REKASAAKSSLIHQG HHHHHHHHHHHHHCC | 40.05 | 25953088 | |
491 | Phosphorylation | EKASAAKSSLIHQGI HHHHHHHHHHHHCCC | 26.17 | 28555341 | |
492 | Phosphorylation | KASAAKSSLIHQGIR HHHHHHHHHHHCCCC | 30.54 | 28555341 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
41 | S | Phosphorylation | Kinase | BUB1 | O43683 | PSP |
72 | S | Phosphorylation | Kinase | BUB1 | O43683 | PSP |
92 | S | Phosphorylation | Kinase | BUB1 | O43683 | PSP |
153 | S | Phosphorylation | Kinase | BUB1 | O43683 | PSP |
157 | T | Phosphorylation | Kinase | BUB1 | O43683 | PSP |
161 | S | Phosphorylation | Kinase | BUB1 | O43683 | PSP |
170 | S | Phosphorylation | Kinase | PLK1 | P53350 | PSP |
- | K | Ubiquitination | E3 ubiquitin ligase | FZR1 | Q9UM11 | PMID:23091007 |
- | K | Ubiquitination | E3 ubiquitin ligase | SPOP | O43791 | PMID:27780719 |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
41 | S | Phosphorylation |
| 15525512 |
66 | K | Acetylation |
| 22014574 |
72 | S | Phosphorylation |
| 15525512 |
92 | S | Phosphorylation |
| 15525512 |
153 | S | Phosphorylation |
| 15525512 |
157 | T | Phosphorylation |
| 15525512 |
161 | S | Phosphorylation |
| 15525512 |
485 | K | ubiquitylation |
| 21926987 |
490 | K | ubiquitylation |
| 21926987 |
490 | K | ubiquitylation |
| 21926987 |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
485 | Ubiquitination | 479 (6) | R ⇒ Q;L | rs45461499 |
| 27114598 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND MASSSPECTROMETRY. | |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND MASSSPECTROMETRY. | |
"Phosphorylation of Cdc20 by Bub1 provides a catalytic mechanism forAPC/C inhibition by the spindle checkpoint."; Tang Z., Shu H., Oncel D., Chen S., Yu H.; Mol. Cell 16:387-397(2004). Cited for: PHOSPHORYLATION AT SER-41; SER-72; SER-92; SER-153; THR-157 ANDSER-161, MASS SPECTROMETRY, INTERACTION WITH BUB1B AND MAD2L1, ANDMUTAGENESIS OF SER-41; SER-72; SER-92; SER-153; THR-157 AND SER-161. | |
"Mitotic regulation of the human anaphase-promoting complex byphosphorylation."; Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J.,Peters J.-M.; EMBO J. 22:6598-6609(2003). Cited for: PHOSPHORYLATION AT THR-70 AND THR-106. | |
Ubiquitylation | |
Reference | PubMed |
"APC15 drives the turnover of MCC-CDC20 to make the spindle assemblycheckpoint responsive to kinetochore attachment."; Mansfeld J., Collin P., Collins M.O., Choudhary J.S., Pines J.; Nat. Cell Biol. 13:1234-1243(2011). Cited for: UBIQUITINATION AT LYS-485 AND LYS-490, AND MUTAGENESIS OF LYS-485 ANDLYS-490. |