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Database: UniProt
Entry: Q12834
LinkDB: Q12834
Original site: Q12834 
ID   CDC20_HUMAN             Reviewed;         499 AA.
AC   Q12834; B2R6Z6; D3DPJ1; Q5JUY4; Q9BW56; Q9UQI9;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2003, sequence version 2.
DT   17-JUN-2020, entry version 200.
DE   RecName: Full=Cell division cycle protein 20 homolog;
DE   AltName: Full=p55CDC;
GN   Name=CDC20;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7513050; DOI=10.1128/mcb.14.5.3350;
RA   Weinstein J., Jacobsen F.W., Hsu-Chen J., Wu T., Baum L.G.;
RT   "A novel mammalian protein, p55CDC, present in dividing cells is associated
RT   with protein kinase activity and has homology to the Saccharomyces
RT   cerevisiae cell division cycle proteins Cdc20 and Cdc4.";
RL   Mol. Cell. Biol. 14:3350-3363(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH MAD2L1 AND
RP   APC/C.
RC   TISSUE=Liver, and Spleen;
RX   PubMed=9811605; DOI=10.1016/s0960-9822(07)00510-6;
RA   Kramer E.R., Gieffers C., Hoelzl G., Hengstschlaeger M., Peters J.-M.;
RT   "Activation of the human anaphase-promoting complex by proteins of the
RT   CDC20/Fizzy family.";
RL   Curr. Biol. 8:1207-1210(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-402 AND GLN-479.
RG   NIEHS SNPs program;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon, Colon adenocarcinoma, Lymph, Muscle, Ovary, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH APC/C.
RX   PubMed=9734353; DOI=10.1016/s1097-2765(00)80126-4;
RA   Fang G., Yu H., Kirschner M.W.;
RT   "Direct binding of CDC20 protein family members activates the anaphase-
RT   promoting complex in mitosis and G1.";
RL   Mol. Cell 2:163-171(1998).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH MAD2L1 AND APC/C.
RX   PubMed=9637688; DOI=10.1101/gad.12.12.1871;
RA   Fang G., Yu H., Kirschner M.W.;
RT   "The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary
RT   complex with the anaphase-promoting complex to control anaphase
RT   initiation.";
RL   Genes Dev. 12:1871-1883(1998).
RN   [11]
RP   PHOSPHORYLATION.
RX   PubMed=10459014; DOI=10.1083/jcb.146.4.791;
RA   Kotani S., Tanaka H., Yasuda H., Todokoro K.;
RT   "Regulation of APC activity by phosphorylation and regulatory factors.";
RL   J. Cell Biol. 146:791-800(1999).
RN   [12]
RP   INTERACTION WITH MAD2L2.
RX   PubMed=11459826; DOI=10.1101/gad.898701;
RA   Chen J., Fang G.;
RT   "MAD2B is an inhibitor of the anaphase-promoting complex.";
RL   Genes Dev. 15:1765-1770(2001).
RN   [13]
RP   PHOSPHORYLATION AT THR-70 AND THR-106.
RX   PubMed=14657031; DOI=10.1093/emboj/cdg627;
RA   Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J.,
RA   Peters J.-M.;
RT   "Mitotic regulation of the human anaphase-promoting complex by
RT   phosphorylation.";
RL   EMBO J. 22:6598-6609(2003).
RN   [14]
RP   PHOSPHORYLATION AT SER-41; SER-72; SER-92; SER-153; THR-157 AND SER-161,
RP   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH BUB1B AND MAD2L1, AND
RP   MUTAGENESIS OF SER-41; SER-72; SER-92; SER-153; THR-157 AND SER-161.
RX   PubMed=15525512; DOI=10.1016/j.molcel.2004.09.031;
RA   Tang Z., Shu H., Oncel D., Chen S., Yu H.;
RT   "Phosphorylation of Cdc20 by Bub1 provides a catalytic mechanism for APC/C
RT   inhibition by the spindle checkpoint.";
RL   Mol. Cell 16:387-397(2004).
RN   [15]
RP   INTERACTION WITH NINL.
RX   PubMed=17403670; DOI=10.1074/jbc.m701350200;
RA   Wang Y., Zhan Q.;
RT   "Cell cycle-dependent expression of centrosomal ninein-like protein in
RT   human cells is regulated by the anaphase-promoting complex.";
RL   J. Biol. Chem. 282:17712-17719(2007).
RN   [16]
RP   UBIQUITINATION, AND DEUBIQUITINATION BY USP44.
RX   PubMed=17443180; DOI=10.1038/nature05694;
RA   Stegmeier F., Rape M., Draviam V.M., Nalepa G., Sowa M.E., Ang X.L.,
RA   McDonald E.R. III, Li M.Z., Hannon G.J., Sorger P.K., Kirschner M.W.,
RA   Harper J.W., Elledge S.J.;
RT   "Anaphase initiation is regulated by antagonistic ubiquitination and
RT   deubiquitination activities.";
RL   Nature 446:876-881(2007).
RN   [17]
RP   INTERACTION WITH HSF1.
RX   PubMed=18794143; DOI=10.1158/0008-5472.can-08-0129;
RA   Lee Y.J., Kim E.H., Lee J.S., Jeoung D., Bae S., Kwon S.H., Lee Y.S.;
RT   "HSF1 as a mitotic regulator: phosphorylation of HSF1 by Plk1 is essential
RT   for mitotic progression.";
RL   Cancer Res. 68:7550-7560(2008).
RN   [18]
RP   UBIQUITINATION, INTERACTION WITH BUB1B, AND DEGRADATION BY THE PROTEASOME.
RX   PubMed=18997788; DOI=10.1038/ncb1799;
RA   Nilsson J., Yekezare M., Minshull J., Pines J.;
RT   "The APC/C maintains the spindle assembly checkpoint by targeting Cdc20 for
RT   destruction.";
RL   Nat. Cell Biol. 10:1411-1420(2008).
RN   [19]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [20]
RP   UBIQUITINATION, INTERACTION WITH MAD2L1 AND BUB1B, DEGRADATION BY THE
RP   PROTEASOME, AND MUTAGENESIS OF ARG-132.
RX   PubMed=19098431; DOI=10.4161/cc.8.1.7606;
RA   Ge S., Skaar J.R., Pagano M.;
RT   "APC/C- and Mad2-mediated degradation of Cdc20 during spindle checkpoint
RT   activation.";
RL   Cell Cycle 8:167-171(2009).
RN   [21]
RP   INTERACTION WITH CDK5RAP2.
RX   PubMed=19282672; DOI=10.4161/cc.8.8.8205;
RA   Zhang X., Liu D., Lv S., Wang H., Zhong X., Liu B., Wang B., Liao J.,
RA   Li J., Pfeifer G.P., Xu X.;
RT   "CDK5RAP2 is required for spindle checkpoint function.";
RL   Cell Cycle 8:1206-1216(2009).
RN   [22]
RP   SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH NEK2.
RX   PubMed=20034488; DOI=10.1016/j.yexmp.2009.12.004;
RA   Liu Q., Hirohashi Y., Du X., Greene M.I., Wang Q.;
RT   "Nek2 targets the mitotic checkpoint proteins Mad2 and Cdc20: a mechanism
RT   for aneuploidy in cancer.";
RL   Exp. Mol. Pathol. 88:225-233(2010).
RN   [23]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [24]
RP   UBIQUITINATION AT LYS-485 AND LYS-490, AND MUTAGENESIS OF LYS-485 AND
RP   LYS-490.
RX   PubMed=21926987; DOI=10.1038/ncb2347;
RA   Mansfeld J., Collin P., Collins M.O., Choudhary J.S., Pines J.;
RT   "APC15 drives the turnover of MCC-CDC20 to make the spindle assembly
RT   checkpoint responsive to kinetochore attachment.";
RL   Nat. Cell Biol. 13:1234-1243(2011).
RN   [25]
RP   ACETYLATION AT LYS-66, DEACETYLATION AT LYS-66 BY SIRT2, AND INTERACTION
RP   WITH SIRT2.
RX   PubMed=22014574; DOI=10.1016/j.ccr.2011.09.004;
RA   Kim H.S., Vassilopoulos A., Wang R.H., Lahusen T., Xiao Z., Xu X., Li C.,
RA   Veenstra T.D., Li B., Yu H., Ji J., Wang X.W., Park S.H., Cha Y.I.,
RA   Gius D., Deng C.X.;
RT   "SIRT2 maintains genome integrity and suppresses tumorigenesis through
RT   regulating APC/C activity.";
RL   Cancer Cell 20:487-499(2011).
RN   [26]
RP   DEPHOSPHORYLATION.
RX   PubMed=22692537; DOI=10.1038/ncomms1886;
RA   Visconti R., Palazzo L., Della Monica R., Grieco D.;
RT   "Fcp1-dependent dephosphorylation is required for M-phase-promoting factor
RT   inactivation at mitosis exit.";
RL   Nat. Commun. 3:894-894(2012).
RN   [27]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND THR-70, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Required for full ubiquitin ligase activity of the anaphase
CC       promoting complex/cyclosome (APC/C) and may confer substrate
CC       specificity upon the complex. Is regulated by MAD2L1: in metaphase the
CC       MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the
CC       CDC20-APC/C binary complex is active in degrading substrates. The
CC       CDC20-APC/C complex positively regulates the formation of synaptic
CC       vesicle clustering at active zone to the presynaptic membrane in
CC       postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces
CC       presynaptic differentiation. {ECO:0000269|PubMed:9637688,
CC       ECO:0000269|PubMed:9734353, ECO:0000269|PubMed:9811605}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Found in a complex with CDC20, CDC27, SPATC1 and TUBG1.
CC       Interacts with NEUROD2 and SPATC1 (By similarity). Interacts with
CC       MAD2L1 and BUB1B. The phosphorylated form interacts with APC/C.
CC       Interacts with NINL. May interact with MAD2L2. Interacts with CDK5RAP2
CC       and SIRT2. Interacts with isoform 1 of NEK2. Interacts with HSF1 (via
CC       phosphorylated form); this interaction occurs in mitosis in a MAD2L1-
CC       dependent manner and prevents PLK1-stimulated degradation of HSF1 by
CC       blocking the recruitment of the SCF(BTRC) ubiquitin ligase complex
CC       (PubMed:18794143). Interacts (via the N-terminal substrate-binding
CC       domain) with FBXO5 (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q9JJ66, ECO:0000269|PubMed:11459826,
CC       ECO:0000269|PubMed:15525512, ECO:0000269|PubMed:17403670,
CC       ECO:0000269|PubMed:18794143, ECO:0000269|PubMed:18997788,
CC       ECO:0000269|PubMed:19098431, ECO:0000269|PubMed:19282672,
CC       ECO:0000269|PubMed:20034488, ECO:0000269|PubMed:22014574,
CC       ECO:0000269|PubMed:9637688, ECO:0000269|PubMed:9734353,
CC       ECO:0000269|PubMed:9811605}.
CC   -!- INTERACTION:
CC       Q12834; Q9UJX5: ANAPC4; NbExp=9; IntAct=EBI-367462, EBI-2554854;
CC       Q12834; O60566: BUB1B; NbExp=32; IntAct=EBI-367462, EBI-1001438;
CC       Q12834; P30260: CDC27; NbExp=12; IntAct=EBI-367462, EBI-994813;
CC       Q12834; Q13257: MAD2L1; NbExp=34; IntAct=EBI-367462, EBI-78203;
CC       Q12834; Q9UI95: MAD2L2; NbExp=2; IntAct=EBI-367462, EBI-77889;
CC       Q12834; Q9NS23-2: RASSF1; NbExp=2; IntAct=EBI-367462, EBI-438698;
CC       Q12834; Q8IXJ6-2: SIRT2; NbExp=2; IntAct=EBI-367462, EBI-5240785;
CC       Q12834; O88566: Axin2; Xeno; NbExp=2; IntAct=EBI-367462, EBI-7690990;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000269|PubMed:20034488}. Cytoplasm,
CC       cytoskeleton, spindle pole {ECO:0000269|PubMed:20034488}.
CC   -!- DEVELOPMENTAL STAGE: Synthesis is initiated at G1/S, protein level
CC       peaks in M phase and protein is abruptly degraded at M/G1 transition.
CC   -!- PTM: Acetylated. Deacetylated at Lys-66 by SIRT2; deacetylation
CC       enhances the interaction of CDC20 with CDC27, leading to activation of
CC       anaphase promoting complex/cyclosome (APC/C).
CC       {ECO:0000269|PubMed:22014574}.
CC   -!- PTM: Phosphorylated during mitosis, probably by maturation promoting
CC       factor (MPF). Phosphorylated by BUB1 at Ser-41; Ser-72; Ser-92; Ser-
CC       153; Thr-157 and Ser-161. Phosphorylated by NEK2.
CC       {ECO:0000269|PubMed:10459014, ECO:0000269|PubMed:14657031,
CC       ECO:0000269|PubMed:15525512, ECO:0000269|PubMed:20034488}.
CC   -!- PTM: Dephosphorylated by CTDP1.
CC   -!- PTM: Ubiquitinated and degraded by the proteasome during spindle
CC       assembly checkpoint. Deubiquitinated by USP44, leading to stabilize the
CC       MAD2L1-CDC20-APC/C ternary complex, thereby preventing premature
CC       activation of the APC/C. Ubiquitinated at Lys-490 during prometaphase.
CC       Ubiquitination at Lys-485 and Lys-490 has no effect on its ability to
CC       bind the APC/C complex. {ECO:0000269|PubMed:17443180,
CC       ECO:0000269|PubMed:18997788, ECO:0000269|PubMed:19098431,
CC       ECO:0000269|PubMed:21926987}.
CC   -!- SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/CDC20ID40003ch1p34.html";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/cdc20/";
DR   EMBL; U05340; AAA19017.1; -; mRNA.
DR   EMBL; AF099644; AAD16405.1; -; mRNA.
DR   EMBL; AK312780; BAG35643.1; -; mRNA.
DR   EMBL; BT007388; AAP36052.1; -; mRNA.
DR   EMBL; DQ473545; ABE96834.1; -; Genomic_DNA.
DR   EMBL; AL139289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX07101.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX07102.1; -; Genomic_DNA.
DR   EMBL; BC000624; AAH00624.1; -; mRNA.
DR   EMBL; BC001088; AAH01088.1; -; mRNA.
DR   EMBL; BC006272; AAH06272.1; -; mRNA.
DR   EMBL; BC009425; AAH09425.1; -; mRNA.
DR   EMBL; BC009426; AAH09426.1; -; mRNA.
DR   EMBL; BC010044; AAH10044.1; -; mRNA.
DR   EMBL; BC012803; AAH12803.1; -; mRNA.
DR   EMBL; BC012827; AAH12827.1; -; mRNA.
DR   EMBL; BC013303; AAH13303.1; -; mRNA.
DR   EMBL; BC015998; AAH15998.1; -; mRNA.
DR   EMBL; BC024257; AAH24257.1; -; mRNA.
DR   EMBL; BC031294; AAH31294.1; -; mRNA.
DR   EMBL; BC110321; AAI10322.1; -; mRNA.
DR   CCDS; CCDS484.1; -.
DR   PIR; A56021; A56021.
DR   RefSeq; NP_001246.2; NM_001255.2.
DR   PDB; 4GGA; X-ray; 2.04 A; A=81-499.
DR   PDB; 4GGC; X-ray; 1.35 A; A=161-477.
DR   PDB; 4GGD; X-ray; 2.44 A; A/B=71-499.
DR   PDB; 4N14; X-ray; 2.10 A; A=165-477.
DR   PDB; 5G04; EM; 4.00 A; R=1-499.
DR   PDB; 5KHR; EM; 6.10 A; R=1-499.
DR   PDB; 5KHU; EM; 4.80 A; R/S=1-499.
DR   PDB; 5LCW; EM; 4.00 A; Q=126-499, R=1-499.
DR   PDB; 6F0X; EM; 4.60 A; Q=1-499.
DR   PDB; 6Q6G; EM; 3.20 A; R=1-499.
DR   PDB; 6Q6H; EM; 3.20 A; R=1-499.
DR   PDBsum; 4GGA; -.
DR   PDBsum; 4GGC; -.
DR   PDBsum; 4GGD; -.
DR   PDBsum; 4N14; -.
DR   PDBsum; 5G04; -.
DR   PDBsum; 5KHR; -.
DR   PDBsum; 5KHU; -.
DR   PDBsum; 5LCW; -.
DR   PDBsum; 6F0X; -.
DR   PDBsum; 6Q6G; -.
DR   PDBsum; 6Q6H; -.
DR   SMR; Q12834; -.
DR   BioGRID; 107427; 192.
DR   ComplexPortal; CPX-3946; Mitotic Checkpoint Complex.
DR   CORUM; Q12834; -.
DR   DIP; DIP-29655N; -.
DR   ELM; Q12834; -.
DR   IntAct; Q12834; 72.
DR   MINT; Q12834; -.
DR   STRING; 9606.ENSP00000361540; -.
DR   iPTMnet; Q12834; -.
DR   PhosphoSitePlus; Q12834; -.
DR   SwissPalm; Q12834; -.
DR   BioMuta; CDC20; -.
DR   DMDM; 37537762; -.
DR   EPD; Q12834; -.
DR   jPOST; Q12834; -.
DR   MassIVE; Q12834; -.
DR   MaxQB; Q12834; -.
DR   PaxDb; Q12834; -.
DR   PeptideAtlas; Q12834; -.
DR   PRIDE; Q12834; -.
DR   ProteomicsDB; 58976; -.
DR   Antibodypedia; 3864; 673 antibodies.
DR   DNASU; 991; -.
DR   Ensembl; ENST00000310955; ENSP00000308450; ENSG00000117399.
DR   Ensembl; ENST00000372462; ENSP00000361540; ENSG00000117399.
DR   GeneID; 991; -.
DR   KEGG; hsa:991; -.
DR   UCSC; uc001cix.4; human.
DR   CTD; 991; -.
DR   DisGeNET; 991; -.
DR   EuPathDB; HostDB:ENSG00000117399.13; -.
DR   GeneCards; CDC20; -.
DR   HGNC; HGNC:1723; CDC20.
DR   HPA; ENSG00000117399; Tissue enhanced (lymphoid tissue, testis).
DR   MIM; 603618; gene.
DR   neXtProt; NX_Q12834; -.
DR   OpenTargets; ENSG00000117399; -.
DR   PharmGKB; PA26257; -.
DR   eggNOG; KOG0305; Eukaryota.
DR   eggNOG; ENOG410XQ8I; LUCA.
DR   GeneTree; ENSGT00950000183104; -.
DR   HOGENOM; CLU_014831_6_1_1; -.
DR   InParanoid; Q12834; -.
DR   KO; K03363; -.
DR   OMA; WSPHKKE; -.
DR   OrthoDB; 1220675at2759; -.
DR   PhylomeDB; Q12834; -.
DR   TreeFam; TF101065; -.
DR   Reactome; R-HSA-141405; Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
DR   Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR   Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR   Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR   Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR   Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR   Reactome; R-HSA-176417; Phosphorylation of Emi1.
DR   Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR   Reactome; R-HSA-68877; Mitotic Prometaphase.
DR   Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q12834; -.
DR   SIGNOR; Q12834; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 991; 744 hits in 791 CRISPR screens.
DR   ChiTaRS; CDC20; human.
DR   GeneWiki; CDC20; -.
DR   GenomeRNAi; 991; -.
DR   Pharos; Q12834; Tbio.
DR   PRO; PR:Q12834; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q12834; protein.
DR   Bgee; ENSG00000117399; Expressed in oocyte and 149 other tissues.
DR   Genevisible; Q12834; HS.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0005819; C:spindle; TAS:ProtInc.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0010997; F:anaphase-promoting complex binding; IEA:InterPro.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IEA:InterPro.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:Ensembl.
DR   GO; GO:0090307; P:mitotic spindle assembly; IEA:Ensembl.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint; TAS:Reactome.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0090129; P:positive regulation of synapse maturation; ISS:UniProtKB.
DR   GO; GO:0031915; P:positive regulation of synaptic plasticity; ISS:UniProtKB.
DR   GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; IDA:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0050773; P:regulation of dendrite development; IEA:Ensembl.
DR   GO; GO:0040020; P:regulation of meiotic nuclear division; IEA:Ensembl.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   DisProt; DP01118; -.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR024977; Apc4_WD40_dom.
DR   InterPro; IPR033010; Cdc20/Fizzy.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR19918; PTHR19918; 1.
DR   Pfam; PF12894; ANAPC4_WD40; 1.
DR   Pfam; PF00400; WD40; 4.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell cycle; Cell division; Cytoplasm;
KW   Cytoskeleton; Differentiation; Isopeptide bond; Mitosis; Neurogenesis;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation;
KW   Ubl conjugation pathway; WD repeat.
FT   CHAIN           1..499
FT                   /note="Cell division cycle protein 20 homolog"
FT                   /id="PRO_0000050900"
FT   REPEAT          182..221
FT                   /note="WD 1"
FT   REPEAT          224..263
FT                   /note="WD 2"
FT   REPEAT          266..303
FT                   /note="WD 3"
FT   REPEAT          307..346
FT                   /note="WD 4"
FT   REPEAT          353..395
FT                   /note="WD 5"
FT   REPEAT          397..438
FT                   /note="WD 6"
FT   REPEAT          441..480
FT                   /note="WD 7"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163,
FT                   ECO:0000269|PubMed:15525512"
FT   MOD_RES         66
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:22014574"
FT   MOD_RES         70
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:23186163,
FT                   ECO:0000269|PubMed:14657031"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:15525512"
FT   MOD_RES         92
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:15525512"
FT   MOD_RES         106
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:14657031"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:15525512"
FT   MOD_RES         157
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:15525512"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:15525512"
FT   CROSSLNK        485
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:21926987"
FT   CROSSLNK        490
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:21926987"
FT   VARIANT         402
FT                   /note="V -> M (in dbSNP:rs45443196)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_030368"
FT   VARIANT         479
FT                   /note="R -> Q (in dbSNP:rs45461499)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_030369"
FT   MUTAGEN         41
FT                   /note="S->A: Loss of BUB1-mediated phosphorylation and
FT                   inhibition and partially defective spindle-assembly
FT                   checkpoint; when associated with A-72; A-92; A-153; A-157
FT                   and A-161."
FT                   /evidence="ECO:0000269|PubMed:15525512"
FT   MUTAGEN         72
FT                   /note="S->A: Loss of BUB1-mediated phosphorylation and
FT                   inhibition and partially defective spindle-assembly
FT                   checkpoint; when associated with A-41; A-92; A-153; A-157
FT                   and A-161."
FT                   /evidence="ECO:0000269|PubMed:15525512"
FT   MUTAGEN         92
FT                   /note="S->A: Loss of BUB1-mediated phosphorylation and
FT                   inhibition and partially defective spindle-assembly
FT                   checkpoint; when associated with A-41; A-72; A-153; A-157
FT                   and A-161."
FT                   /evidence="ECO:0000269|PubMed:15525512"
FT   MUTAGEN         132
FT                   /note="R->A: Loss of interaction with MAD2L1."
FT                   /evidence="ECO:0000269|PubMed:19098431"
FT   MUTAGEN         153
FT                   /note="S->A: Loss of BUB1-mediated phosphorylation and
FT                   inhibition and partially defective spindle-assembly
FT                   checkpoint; when associated with A-42; A-72; A-92; A-157
FT                   and A-161."
FT                   /evidence="ECO:0000269|PubMed:15525512"
FT   MUTAGEN         157
FT                   /note="T->A: Loss of BUB1-mediated phosphorylation and
FT                   inhibition and partially defective spindle-assembly
FT                   checkpoint; when associated with A-42; A-72; A-92; A-153
FT                   and A-161."
FT                   /evidence="ECO:0000269|PubMed:15525512"
FT   MUTAGEN         161
FT                   /note="S->A: Loss of BUB1-mediated phosphorylation and
FT                   inhibition and partially defective spindle-assembly
FT                   checkpoint; when associated with A-72; A-92; A-153; A-157
FT                   and A-161."
FT                   /evidence="ECO:0000269|PubMed:15525512"
FT   MUTAGEN         485
FT                   /note="K->R: Does not affect its ability to bind the APC/C
FT                   complex; when associated with R-490."
FT                   /evidence="ECO:0000269|PubMed:21926987"
FT   MUTAGEN         490
FT                   /note="K->R: Does not affect its ability to bind the APC/C
FT                   complex; when associated with R-485."
FT                   /evidence="ECO:0000269|PubMed:21926987"
FT   CONFLICT        101
FT                   /note="P -> S (in Ref. 1; AAA19017)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="A -> V (in Ref. 8; AAH00624)"
FT                   /evidence="ECO:0000305"
FT   STRAND          78..80
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           85..96
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            97..99
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           107..120
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          121..123
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           125..127
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          173..177
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          190..192
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          196..202
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          205..210
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   TURN            211..213
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          216..221
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          224..226
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          229..234
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          238..245
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          248..254
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   TURN            255..258
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          259..265
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          271..277
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          280..285
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          288..294
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          297..299
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          301..306
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          312..317
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          321..328
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          333..339
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          342..345
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          348..351
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          358..363
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          365..367
FT                   /evidence="ECO:0000244|PDB:6Q6H"
FT   STRAND          370..375
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   TURN            377..379
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          381..386
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   TURN            387..389
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          392..397
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          402..408
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   TURN            409..412
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          413..418
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   TURN            420..422
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          425..429
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   TURN            430..432
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          435..439
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          446..451
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          453..455
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          458..462
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   TURN            463..465
FT                   /evidence="ECO:0000244|PDB:4GGC"
FT   STRAND          466..470
FT                   /evidence="ECO:0000244|PDB:4GGC"
SQ   SEQUENCE   499 AA;  54723 MW;  FD5C967AF84089E8 CRC64;
     MAQFAFESDL HSLLQLDAPI PNAPPARWQR KAKEAAGPAP SPMRAANRSH SAGRTPGRTP
     GKSSSKVQTT PSKPGGDRYI PHRSAAQMEV ASFLLSKENQ PENSQTPTKK EHQKAWALNL
     NGFDVEEAKI LRLSGKPQNA PEGYQNRLKV LYSQKATPGS SRKTCRYIPS LPDRILDAPE
     IRNDYYLNLV DWSSGNVLAV ALDNSVYLWS ASSGDILQLL QMEQPGEYIS SVAWIKEGNY
     LAVGTSSAEV QLWDVQQQKR LRNMTSHSAR VGSLSWNSYI LSSGSRSGHI HHHDVRVAEH
     HVATLSGHSQ EVCGLRWAPD GRHLASGGND NLVNVWPSAP GEGGWVPLQT FTQHQGAVKA
     VAWCPWQSNV LATGGGTSDR HIRIWNVCSG ACLSAVDAHS QVCSILWSPH YKELISGHGF
     AQNQLVIWKY PTMAKVAELK GHTSRVLSLT MSPDGATVAS AAADETLRLW RCFELDPARR
     REREKASAAK SSLIHQGIR
//
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