CDC20_MOUSE
ID CDC20_MOUSE Reviewed; 499 AA.
AC Q9JJ66; Q3TGP1; Q8BPG4; Q99LK3;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Cell division cycle protein 20 homolog;
DE Short=mmCdc20;
DE AltName: Full=p55CDC;
GN Name=Cdc20;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kuroda M., Oikawa K., Ohbayashi T., Iwata R., Kameta A., Ebine K.;
RT "Mus musculus CDC20 mRNA, complete cds.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Asadi A., Jacobsson A.;
RT "Ssc1/Elovl1 and p55Cdc genes are co-expressed in a tail-to-tail array in
RT proliferating cells.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [5]
RP PROTEIN SEQUENCE OF 59-66, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP INTERACTION WITH FBXO5.
RX PubMed=15526037; DOI=10.1038/sj.emboj.7600448;
RA Paronetto M.P., Giorda E., Carsetti R., Rossi P., Geremia R., Sette C.;
RT "Functional interaction between p90Rsk2 and Emi1 contributes to the
RT metaphase arrest of mouse oocytes.";
RL EMBO J. 23:4649-4659(2004).
RN [7]
RP INTERACTION WITH SPATC1, AND IDENTIFICATION IN A COMPLEX WITH CDC27; SPATC1
RP AND TUBG1.
RX PubMed=15280373; DOI=10.1074/jbc.m403190200;
RA Goto M., Eddy E.M.;
RT "Speriolin is a novel spermatogenic cell-specific centrosomal protein
RT associated with the seventh WD motif of Cdc20.";
RL J. Biol. Chem. 279:42128-42138(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH NEUROD2.
RX PubMed=19900895; DOI=10.1126/science.1177087;
RA Yang Y., Kim A.H., Yamada T., Wu B., Bilimoria P.M., Ikeuchi Y.,
RA de la Iglesia N., Shen J., Bonni A.;
RT "A Cdc20-APC ubiquitin signaling pathway regulates presynaptic
RT differentiation.";
RL Science 326:575-578(2009).
RN [9]
RP ACETYLATION, DEACETYLATION BY SIRT2, AND INTERACTION 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).
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:19900895}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of a complex with CDC20, CDC27, SPATC1 and TUBG1
CC (PubMed:15280373). Interacts with NEUROD2 (PubMed:19900895). Interacts
CC with dimeric MAD2L1 in its closed conformation form (By similarity).
CC Interacts with BUB1B (By similarity). The phosphorylated form interacts
CC with APC/C (By similarity). Interacts with NINL (By similarity). May
CC interact with MAD2L2 (By similarity). Interacts with CDK5RAP2 (By
CC similarity). Interacts with SIRT2 (PubMed:22014574). Interacts with
CC isoform 1 of NEK2 (By similarity). 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 (By
CC similarity). Interacts (via the N-terminal substrate-binding domain)
CC with FBXO5 (PubMed:15526037). Interacts with CCNF (By similarity).
CC {ECO:0000250|UniProtKB:Q12834, ECO:0000269|PubMed:15280373,
CC ECO:0000269|PubMed:15526037, ECO:0000269|PubMed:19900895,
CC ECO:0000269|PubMed:22014574}.
CC -!- INTERACTION:
CC Q9JJ66; Q8CDI2: Fbxo43; NbExp=2; IntAct=EBI-2551389, EBI-8060482;
CC Q9JJ66; Q8VDQ8: Sirt2; NbExp=2; IntAct=EBI-2551389, EBI-911012;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Dephosphorylated by CTDP1. {ECO:0000250}.
CC -!- PTM: Ubiquitinated and degraded by the proteasome during spindle
CC assembly checkpoint. 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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family. {ECO:0000305}.
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DR EMBL; AB045313; BAA97451.1; -; mRNA.
DR EMBL; AF312208; AAL25714.1; -; mRNA.
DR EMBL; AK075998; BAC36109.1; -; mRNA.
DR EMBL; AK076030; BAC36132.1; -; mRNA.
DR EMBL; AK083459; BAC38922.1; -; mRNA.
DR EMBL; AK168650; BAE40507.1; -; mRNA.
DR EMBL; BC003215; AAH03215.1; -; mRNA.
DR CCDS; CCDS18551.1; -.
DR RefSeq; NP_075712.2; NM_023223.2.
DR AlphaFoldDB; Q9JJ66; -.
DR SMR; Q9JJ66; -.
DR BioGRID; 223749; 48.
DR ComplexPortal; CPX-3968; Mitotic Checkpoint Complex.
DR IntAct; Q9JJ66; 39.
DR MINT; Q9JJ66; -.
DR STRING; 10090.ENSMUSP00000006565; -.
DR iPTMnet; Q9JJ66; -.
DR PhosphoSitePlus; Q9JJ66; -.
DR EPD; Q9JJ66; -.
DR MaxQB; Q9JJ66; -.
DR PaxDb; Q9JJ66; -.
DR PeptideAtlas; Q9JJ66; -.
DR PRIDE; Q9JJ66; -.
DR ProteomicsDB; 283764; -.
DR Antibodypedia; 3864; 716 antibodies from 38 providers.
DR DNASU; 107995; -.
DR Ensembl; ENSMUST00000006565; ENSMUSP00000006565; ENSMUSG00000006398.
DR GeneID; 107995; -.
DR KEGG; mmu:107995; -.
DR UCSC; uc008ukc.2; mouse.
DR CTD; 991; -.
DR MGI; MGI:1859866; Cdc20.
DR VEuPathDB; HostDB:ENSMUSG00000006398; -.
DR eggNOG; KOG0305; Eukaryota.
DR GeneTree; ENSGT00950000183104; -.
DR HOGENOM; CLU_014831_6_1_1; -.
DR InParanoid; Q9JJ66; -.
DR OMA; NGHEDRV; -.
DR OrthoDB; 1220675at2759; -.
DR PhylomeDB; Q9JJ66; -.
DR TreeFam; TF101065; -.
DR Reactome; R-MMU-141405; Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
DR Reactome; R-MMU-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-MMU-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-MMU-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-MMU-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-MMU-176417; Phosphorylation of Emi1.
DR Reactome; R-MMU-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 107995; 25 hits in 76 CRISPR screens.
DR ChiTaRS; Cdc20; mouse.
DR PRO; PR:Q9JJ66; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9JJ66; protein.
DR Bgee; ENSMUSG00000006398; Expressed in cleaving embryo and 220 other tissues.
DR ExpressionAtlas; Q9JJ66; baseline and differential.
DR Genevisible; Q9JJ66; MM.
DR GO; GO:0005680; C:anaphase-promoting complex; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0033597; C:mitotic checkpoint complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0010997; F:anaphase-promoting complex binding; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:1990757; F:ubiquitin ligase activator activity; IBA:GO_Central.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IGI:MGI.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:MGI.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IC:ComplexPortal.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; ISO:MGI.
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:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0090129; P:positive regulation of synapse maturation; IDA:UniProtKB.
DR GO; GO:0031915; P:positive regulation of synaptic plasticity; IDA:UniProtKB.
DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0050773; P:regulation of dendrite development; ISO:MGI.
DR GO; GO:0040020; P:regulation of meiotic nuclear division; IGI:MGI.
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; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19918; PTHR19918; 1.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Differentiation; Direct protein sequencing; Isopeptide bond; Mitosis;
KW Neurogenesis; Phosphoprotein; 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_0000050901"
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 27..82
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:0000250|UniProtKB:Q12834"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT MOD_RES 157
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT CROSSLNK 485
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT CROSSLNK 490
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT CONFLICT 85
FT /note="A -> G (in Ref. 1; BAA97451)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="D -> E (in Ref. 3; BAC36132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 54816 MW; 81E0781BA87BA79E CRC64;
MAQFVFESDL HSLLQLDAPI PNAPVARWQR KAKEATGPAP SPMRAANRSH SAGRTPGRTP
GKSSSKVQTT PSKPGGDRFI PQRSASQMEV ASFLLSKENQ PEDRGTPTKK EHQKAWSLNL
NGFDVEEAKI LRLSGKPQNA PEGYQNRLKV LYSQKATPGS SRKTCRYIPS LPDRILDAPE
IRNDYYLNLV DWSSGNVLAV ALDNSVYLWN AGSGDILQLL QMEQPGDYIS SVAWIKEGNY
LAVGTSNAEV QLWDVQQQKR LRNMTSHSAR VSSLSWNSYI LSSGSRSGHI HHHDVRVAEH
HVATLSGHSQ EVCGLRWAPD GRHLASGGND NIVNVWPSGP GESGWAPLQT FTQHQGAVKA
VAWCPWQSNI LATGGGTSDR HIRIWNVCSG ACLSAVDVHS QVCSILWSPH YKELISGHGF
AQNQLVIWKY PTMAKVAELK GHTARVLGLT MSPDGATVAS AAADETLRLW RCFEMDPALR
REREKASVAK SSLIHQGIR
