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 27-MAR-2024, entry version 218. 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.14.5.3350-3363.1994; 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 RETRACTED PAPER. 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 RETRACTION NOTICE OF PUBMED:10459014. RX PubMed=15824138; DOI=10.1083/jcb.199901060032505r; RA Tanaka H., Yasuda H., Todokoro K.; RL J. Cell Biol. 169:205-205(2005). RN [13] 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 [14] 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 [15] 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 [16] 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 [17] 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 [18] 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 [19] 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 [20] 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 [21] 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 [22] 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 [23] 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 [24] 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 [25] 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 [26] 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 [27] 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 [28] 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). RN [29] RP INTERACTION WITH CCNF. RX PubMed=27653696; DOI=10.1016/j.celrep.2016.08.058; RA Choudhury R., Bonacci T., Arceci A., Lahiri D., Mills C.A., Kernan J.L., RA Branigan T.B., DeCaprio J.A., Burke D.J., Emanuele M.J.; RT "APC/C and SCF(cyclin F) Constitute a Reciprocal Feedback Circuit RT Controlling S-Phase Entry."; RL Cell Rep. 16:3359-3372(2016). RN [30] RP INTERACTION WITH MAD2L1. RX PubMed=29162720; DOI=10.1074/jbc.ra117.000555; RA Ji W., Luo Y., Ahmad E., Liu S.T.; RT "Direct interactions of mitotic arrest deficient 1 (MAD1) domains with each RT other and MAD2 conformers are required for mitotic checkpoint signaling."; RL J. Biol. Chem. 293:484-496(2018). RN [31] RP INVOLVEMENT IN OZEMA14, VARIANTS OZEMA14 182-ARG--ARG-499 DEL; CYS-228; RP GLN-322 AND ARG-439, CHARACTERIZATION OF VARIANTS OZEMA14 182-ARG--ARG-499 RP DEL; CYS-228; GLN-322 AND ARG-439, SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=32666501; DOI=10.1007/s13238-020-00756-0; RA Zhao L., Xue S., Yao Z., Shi J., Chen B., Wu L., Sun L., Xu Y., Yan Z., RA Li B., Mao X., Fu J., Zhang Z., Mu J., Wang W., Du J., Liu S., Dong J., RA Wang W., Li Q., He L., Jin L., Liang X., Kuang Y., Sun X., Wang L., RA Sang Q.; RT "Biallelic mutations in CDC20 cause female infertility characterized by RT abnormalities in oocyte maturation and early embryonic development."; RL Protein Cell 11:921-927(2020). RN [32] RP VARIANT SER-286, INTERACTION WITH BUB1B, SUBCELLULAR LOCATION, AND RP CHARACTERIZATION OF VARIANT SER-286. RX PubMed=33094908; DOI=10.1111/acel.13251; RA Fujita H., Sasaki T., Miyamoto T., Akutsu S.N., Sato S., Mori T., RA Nakabayashi K., Hata K., Suzuki H., Kosaki K., Matsuura S., Matsubara Y., RA Amagai M., Kubo A.; RT "Premature aging syndrome showing random chromosome number instabilities RT with CDC20 mutation."; RL Aging Cell 19:e13251-e13251(2020). RN [33] RP VARIANTS OZEMA14 GLN-296; 322-ARG--ARG-499 DEL; GLN-322 AND CYS-385, AND RP CHARACTERIZATION OF VARIANTS OZEMA14 GLN-296; 322-ARG--ARG-499 DEL; GLN-322 RP AND CYS-385. RX PubMed=33898437; DOI=10.3389/fcell.2021.647130; RA Zhao L., Guan Y., Meng Q., Wang W., Wu L., Chen B., Hu J., Zhu J., RA Zhang Z., Mu J., Chen Y., Sun Y., Wu T., Wang W., Zhou Z., Dong J., RA Zeng Y., Liu R., Li Q., Du J., Kuang Y., Sang Q., Wang L.; RT "Identification of novel mutations in CDC20: Expanding the mutational RT spectrum for female infertility."; RL Front. Cell Dev. Biol. 9:647130-647130(2021). RN [34] RP VARIANT OZEMA14 CYS-228. RX PubMed=34218387; DOI=10.1007/s10815-021-02269-z; RA Xu Y., Zhu X., Wang M., Cai L., Ge Q., Fu Y., Jin L.; RT "The homozygous p.Tyr228Cys variant in CDC20 causes oocyte maturation RT arrest: an additional evidence supporting the causality between CDC20 RT mutation and female infertility."; RL J. Assist. Reprod. Genet. 38:2219-2222(2021). RN [35] RP VARIANTS OZEMA14 THR-211 AND 262-ARG--ARG-499 DEL. RX PubMed=33683667; DOI=10.1007/s43032-021-00524-3; RA Huang L., Wang F., Kong S., Wang Y., Song G., Lu F., Ji J., Luo L., RA Tong X.; RT "Novel Mutations in CDC20 Are Associated with Female Infertility Due to RT Oocyte Maturation Abnormality and Early Embryonic Arrest."; RL Reprod. Sci. 28:1930-1938(2021). CC -!- FUNCTION: Involved in the metaphase/anaphase transition of cell cycle CC (PubMed:32666501). Required for full ubiquitin ligase activity of the CC anaphase 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. The CDC20-APC/C complex promotes proper CC dilation formation and radial migration by degrading CCDC41 (By CC similarity). {ECO:0000250|UniProtKB:Q9JJ66, CC ECO:0000269|PubMed:32666501, ECO:0000269|PubMed:9637688, CC ECO:0000269|PubMed:9734353, ECO:0000269|PubMed:9811605}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Component of a complex with CDC20, CDC27, SPATC1 and TUBG1 (By CC similarity). Interacts with NEUROD2 (By similarity). Interacts with CC dimeric MAD2L1 in its closed conformation form (PubMed:9811605, CC PubMed:9637688, PubMed:15525512, PubMed:19098431, PubMed:29162720). CC Interacts with BUB1B (PubMed:15525512, PubMed:18997788, CC PubMed:19098431, PubMed:33094908). The phosphorylated form interacts CC with APC/C (PubMed:9811605, PubMed:9734353, PubMed:9637688). Interacts CC with NINL (PubMed:17403670). May interact with MAD2L2 CC (PubMed:11459826). Interacts with CDK5RAP2 (PubMed:19282672). Interacts CC with SIRT2 (PubMed:22014574). Interacts with isoform 1 of NEK2 CC (PubMed:20034488). Interacts with HSF1 (via phosphorylated form); this CC interaction occurs in mitosis in a MAD2L1-dependent manner and prevents CC PLK1-stimulated degradation of HSF1 by blocking the recruitment of the CC SCF(BTRC) ubiquitin ligase complex (PubMed:18794143). Interacts (via CC the N-terminal substrate-binding domain) with FBXO5 (By similarity). CC Interacts with CCNF (PubMed:27653696). {ECO:0000250|UniProtKB:Q9JJ66, CC ECO:0000269|PubMed:11459826, ECO:0000269|PubMed:15525512, CC ECO:0000269|PubMed:17403670, ECO:0000269|PubMed:18794143, CC ECO:0000269|PubMed:18997788, ECO:0000269|PubMed:19098431, CC ECO:0000269|PubMed:19282672, ECO:0000269|PubMed:20034488, CC ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:27653696, CC ECO:0000269|PubMed:29162720, ECO:0000269|PubMed:33094908, 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=13; 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}. Chromosome, CC centromere, kinetochore {ECO:0000269|PubMed:32666501, CC ECO:0000269|PubMed:33094908}. Cytoplasm, cytoskeleton, spindle pole CC {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 (PubMed:14657031). Phosphorylated by CC BUB1 at Ser-41; Ser-72; Ser-92; Ser-153; Thr-157 and Ser-161 CC (PubMed:15525512). Phosphorylated by NEK2 (PubMed:20034488). CC {ECO:0000269|PubMed:14657031, ECO:0000269|PubMed:15525512, CC 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 -!- DISEASE: Oocyte/zygote/embryo maturation arrest 14 (OZEMA14) CC [MIM:620276]: An autosomal recessive female infertility disorder CC characterized by oocyte maturation arrest, fertilization failure, CC and/or early embryonic arrest. {ECO:0000269|PubMed:32666501, CC ECO:0000269|PubMed:33683667, ECO:0000269|PubMed:33898437, CC ECO:0000269|PubMed:34218387}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family. {ECO:0000305}. CC -!- CAUTION: Originally thought to be phosphorylated by MPF during mitosis. CC However this paper was retracted due to falsification of data. CC {ECO:0000305|PubMed:10459014, ECO:0000305|PubMed:15824138}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40003/CDC20"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/cdc20/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 AlphaFoldDB; Q12834; -. DR EMDB; EMD-3385; -. DR EMDB; EMD-4037; -. DR EMDB; EMD-4166; -. DR EMDB; EMD-4465; -. DR EMDB; EMD-4466; -. DR EMDB; EMD-4467; -. DR SMR; Q12834; -. DR BioGRID; 107427; 241. DR ComplexPortal; CPX-3946; Mitotic Checkpoint Complex. DR ComplexPortal; CPX-6087; Anaphase-promoting complex, CDC20 variant. DR CORUM; Q12834; -. DR DIP; DIP-29655N; -. DR ELM; Q12834; -. DR IntAct; Q12834; 74. DR MINT; Q12834; -. DR STRING; 9606.ENSP00000361540; -. DR BindingDB; Q12834; -. DR ChEMBL; CHEMBL4523283; -. DR TCDB; 8.A.92.1.14; the g-protein AlphaBetaGama complex (gpc) family. DR GlyGen; Q12834; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000361540; -. DR PeptideAtlas; Q12834; -. DR ProteomicsDB; 58976; -. DR Pumba; Q12834; -. DR Antibodypedia; 3864; 775 antibodies from 38 providers. DR DNASU; 991; -. DR Ensembl; ENST00000310955.11; ENSP00000308450.5; ENSG00000117399.14. DR Ensembl; ENST00000372462.1; ENSP00000361540.1; ENSG00000117399.14. DR GeneID; 991; -. DR KEGG; hsa:991; -. DR MANE-Select; ENST00000310955.11; ENSP00000308450.5; NM_001255.3; NP_001246.2. DR UCSC; uc001cix.4; human. DR AGR; HGNC:1723; -. DR CTD; 991; -. DR DisGeNET; 991; -. DR GeneCards; CDC20; -. DR HGNC; HGNC:1723; CDC20. DR HPA; ENSG00000117399; Tissue enhanced (bone marrow, lymphoid tissue, testis). DR MalaCards; CDC20; -. DR MIM; 603618; gene. DR MIM; 620276; phenotype. DR neXtProt; NX_Q12834; -. DR OpenTargets; ENSG00000117399; -. DR PharmGKB; PA26257; -. DR VEuPathDB; HostDB:ENSG00000117399; -. DR eggNOG; KOG0305; Eukaryota. DR GeneTree; ENSGT00950000183104; -. DR HOGENOM; CLU_014831_6_1_1; -. DR InParanoid; Q12834; -. DR OMA; CSGACLN; -. DR OrthoDB; 20041at2759; -. DR PhylomeDB; Q12834; -. DR TreeFam; TF101065; -. DR PathwayCommons; Q12834; -. 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; 845 hits in 1188 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 139 other cell types or tissues. DR GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProt. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB. DR GO; GO:0033597; C:mitotic checkpoint complex; IPI:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. 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; IDA:UniProt. DR GO; GO:1990757; F:ubiquitin ligase activator activity; IBA:GO_Central. DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0044784; P:metaphase/anaphase transition of cell cycle; ISS:UniProtKB. DR GO; GO:1990949; P:metaphase/anaphase transition of meiosis I; IMP:UniProtKB. 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 signaling; NAS:ComplexPortal. DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. DR GO; GO:1905786; P:positive regulation of anaphase-promoting complex-dependent catabolic process; IBA:GO_Central. DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IDA:UniProt. 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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. DR GO; GO:0051445; P:regulation of meiotic cell cycle; NAS:ComplexPortal. DR GO; GO:0040020; P:regulation of meiotic nuclear division; IEA:Ensembl. DR GO; GO:0007346; P:regulation of mitotic cell cycle; NAS:ComplexPortal. DR CDD; cd00200; WD40; 1. DR DisProt; DP01118; -. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR024977; Apc4-like_WD40_dom. DR InterPro; IPR033010; Cdc20/Fizzy. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR19918; CELL DIVISION CYCLE 20 CDC20 FIZZY -RELATED; 1. DR PANTHER; PTHR19918:SF3; CELL DIVISION CYCLE PROTEIN 20 HOMOLOG; 1. DR Pfam; PF12894; ANAPC4_WD40; 1. DR Pfam; PF00400; WD40; 3. DR SMART; SM00320; WD40; 7. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 3. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; Q12834; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cell cycle; Cell division; Centromere; KW Chromosome; Cytoplasm; Cytoskeleton; Differentiation; Disease variant; KW Isopeptide bond; Kinetochore; Mitosis; Neurogenesis; Phosphoprotein; KW Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway; KW 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 REGION 17..80 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 52..72 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 41 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15525512, FT ECO:0007744|PubMed:23186163" FT MOD_RES 66 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:22014574" FT MOD_RES 70 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:14657031, FT ECO:0007744|PubMed:23186163" 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 182..499 FT /note="Missing (in OZEMA14; severely decreased function in FT metaphase/anaphase transition of meiosis I; does not fully FT rescue metaphase I arrest in CDC20-knocked down mouse FT oocytes; decreased function in positive regulation of FT anaphase-promoting complex-dependent catabolic process; FT fails to localize to the kinetochore)" FT /evidence="ECO:0000269|PubMed:32666501" FT /id="VAR_088388" FT VARIANT 211 FT /note="A -> T (in OZEMA14; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33683667" FT /id="VAR_088389" FT VARIANT 228 FT /note="Y -> C (in OZEMA14; decreased function in FT metaphase/anaphase transition of meiosis I; does not fully FT rescue metaphase I arrest in CDC20-knocked down mouse FT oocytes; decreased function in positive regulation of FT anaphase-promoting complex-dependent catabolic process; FT shows normal kinetochore localization)" FT /evidence="ECO:0000269|PubMed:32666501, FT ECO:0000269|PubMed:34218387" FT /id="VAR_088390" FT VARIANT 262..499 FT /note="Missing (in OZEMA14; dbSNP:rs754957702)" FT /evidence="ECO:0000269|PubMed:33683667" FT /id="VAR_088391" FT VARIANT 286 FT /note="R -> S (found in a patient with mosaic variagated FT aneuploidy syndrome 1; uncertain significance; decreased FT interaction with BUB1B during the formation of the mitotic FT checkpoint complex; shows normal kinetochore localization)" FT /evidence="ECO:0000269|PubMed:33094908" FT /id="VAR_088392" FT VARIANT 296 FT /note="R -> Q (in OZEMA14; uncertain significance; FT decreased function in metaphase/anaphase transition of FT meiosis I; does not fully rescue metaphase I arrest in FT CDC20-knocked down mouse oocytes; decreased function in FT positive regulation of anaphase-promoting complex-dependent FT catabolic process; shows normal kinetochore localization)" FT /evidence="ECO:0000269|PubMed:33898437" FT /id="VAR_088393" FT VARIANT 322..499 FT /note="Missing (in OZEMA14; severely decreased function in FT metaphase/anaphase transition of meiosis I; does not fully FT rescue metaphase I arrest in CDC20-knocked down mouse FT oocytes; decreased function in positive regulation of FT anaphase-promoting complex-dependent catabolic process; FT fails to localize to the kinetochore)" FT /evidence="ECO:0000269|PubMed:32666501, FT ECO:0000269|PubMed:33898437" FT /id="VAR_088394" FT VARIANT 322 FT /note="R -> Q (in OZEMA14; severely decreased function in FT metaphase/anaphase transition of meiosis I; does not fully FT rescue metaphase I arrest in CDC20-knocked down mouse FT oocytes; decreased function in positive regulation of FT anaphase-promoting complex-dependent catabolic process; FT shows normal kinetochore localization)" FT /evidence="ECO:0000269|PubMed:32666501, FT ECO:0000269|PubMed:33898437" FT /id="VAR_088395" FT VARIANT 385 FT /note="W -> C (in OZEMA14; decreased function in FT metaphase/anaphase transition of meiosis I; does not fully FT rescue metaphase I arrest in CDC20-knocked down mouse FT oocytes; slightly decreased function in positive regulation FT of anaphase-promoting complex-dependent catabolic process; FT shows normal kinetochore localization)" FT /evidence="ECO:0000269|PubMed:33898437" FT /id="VAR_088396" FT VARIANT 402 FT /note="V -> M (in dbSNP:rs45443196)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_030368" FT VARIANT 439 FT /note="L -> R (in OZEMA14; uncertain significance; FT decreased function in metaphase/anaphase transition of FT meiosis I; does not fully rescue metaphase I arrest in FT CDC20-knocked down mouse oocytes; decreased function in FT positive regulation of anaphase-promoting complex-dependent FT catabolic process; shows normal kinetochore localization)" FT /evidence="ECO:0000269|PubMed:32666501" FT /id="VAR_088397" 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:0007829|PDB:6Q6G" FT HELIX 85..96 FT /evidence="ECO:0007829|PDB:6Q6G" FT TURN 97..99 FT /evidence="ECO:0007829|PDB:6Q6G" FT HELIX 107..120 FT /evidence="ECO:0007829|PDB:6Q6G" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:6Q6G" FT HELIX 125..127 FT /evidence="ECO:0007829|PDB:6Q6G" FT STRAND 173..177 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 190..192 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 196..202 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 205..210 FT /evidence="ECO:0007829|PDB:4GGC" FT TURN 211..213 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 216..221 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 224..226 FT /evidence="ECO:0007829|PDB:6Q6G" FT STRAND 229..234 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 238..245 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 248..254 FT /evidence="ECO:0007829|PDB:4GGC" FT TURN 255..258 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 259..265 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 271..277 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 280..285 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 288..294 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 297..299 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 301..306 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 312..317 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 321..328 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 333..339 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 342..345 FT /evidence="ECO:0007829|PDB:6Q6G" FT STRAND 348..351 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 358..363 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 365..367 FT /evidence="ECO:0007829|PDB:6Q6H" FT STRAND 370..375 FT /evidence="ECO:0007829|PDB:4GGC" FT TURN 377..379 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 381..386 FT /evidence="ECO:0007829|PDB:4GGC" FT TURN 387..389 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 392..397 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 402..408 FT /evidence="ECO:0007829|PDB:4GGC" FT TURN 409..412 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 413..418 FT /evidence="ECO:0007829|PDB:4GGC" FT TURN 420..422 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 425..429 FT /evidence="ECO:0007829|PDB:4GGC" FT TURN 430..432 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 435..439 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 446..451 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 453..455 FT /evidence="ECO:0007829|PDB:6Q6G" FT STRAND 458..462 FT /evidence="ECO:0007829|PDB:4GGC" FT TURN 463..465 FT /evidence="ECO:0007829|PDB:4GGC" FT STRAND 466..470 FT /evidence="ECO:0007829|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 //