Reviewed, UniProtKB/Swiss-Prot Q12834 (CDC20_HUMAN)

Names and origin

Protein names

Recommended name:
    Cell division cycle protein 20 homolog
Alternative name(s):
    p55CDC

Gene names

Name:

CDC20

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	499 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for full ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) and may confer substrate specificity upon the complex. Is regulated by MAD2L1. In metaphase the MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the CDC20-APC/C binary complex is active in degrading substrates. Ref.2 Ref.8 Ref.9
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Found in a complex with CDC20, CDC27, SPATC1 and TUBG1. Interacts with SPATC1 By similarity. Interacts with MAD2L1 and BUB1B. The phosphorylated form interacts with APC/C.
Developmental stage	Synthesis is initiated at G1/S, protein level peaks in M phase and protein is abruptly degraded at M/G1 transition.
Post-translational modification	Phosphorylated during mitosis, probably by maturation promoting factor (MPF). Ref.10 Ref.11 Ref.13 Ubiquitinated and degraded by the proteasome during spindle assembly checkpoint.
Sequence similarities	Belongs to the WD repeat CDC20/Fizzy family. Contains 7 WD repeats.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Coding sequence diversity	Polymorphism
Domain	Repeat WD repeat
PTM	Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome
Cellular component	cytosol Inferred from Experiment. Source: Reactome nucleoplasm Inferred from Experiment. Source: Reactome spindle Ref.1 Traceable author statement. Source: ProtInc
Molecular function	protein C-terminus binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BUB1B	O60566	4	EBI-367462,EBI-1001438
CCDC59	Q9P031	1	EBI-367462,EBI-1047110
KRT31	Q15323	1	EBI-367462,EBI-948001
KRT32	Q14532	1	EBI-367462,EBI-1044146
KRT33A	O76009	1	EBI-367462,EBI-1051692
KRT85	P78386	1	EBI-367462,EBI-1049371
KRTAP19-5	Q3LI72	1	EBI-367462,EBI-1048945
KRTAP9-2	Q9BYQ4	1	EBI-367462,EBI-1044640
KRTAP9-3	Q9BYQ3	1	EBI-367462,EBI-1043191
MAD2L1	Q13257	1	EBI-367462,EBI-78203
MAD2L2	Q9UI95	2	EBI-367462,EBI-77889
RASSF1	Q9NS23-2	2	EBI-367462,EBI-438698
YARS2	Q9Y2Z4	1	EBI-367462,EBI-1049286

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 499	499	Cell division cycle protein 20 homolog		PRO_0000050900
Regions
	Repeat	182 – 221	40	WD 1
	Repeat	224 – 263	40	WD 2
	Repeat	266 – 303	38	WD 3
	Repeat	307 – 346	40	WD 4
	Repeat	353 – 395	43	WD 5
	Repeat	397 – 438	42	WD 6
	Repeat	441 – 480	40	WD 7
Amino acid modifications
	Modified residue	41	1	Phosphoserine Ref.13
	Modified residue	70	1	Phosphothreonine Ref.11
	Modified residue	106	1	Phosphothreonine Ref.11
Natural variations
	Natural variant	402	1	V → M Ref.5		VAR_030368
	Natural variant	479	1	R → Q Ref.5		VAR_030369
Experimental info
	Mutagenesis	132	1	R → A: Loss of interaction with MAD2L1.
	Sequence conflict	101	1	P → S in AAA19017. Ref.1
	Sequence conflict	117	1	A → V in AAH00624. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q12834-1 [UniParc]. Last modified October 3, 2003. Version 2. Checksum: FD5C967AF84089E8	FASTA	499	54,723
	10 20 30 40 50 60 MAQFAFESDL HSLLQLDAPI PNAPPARWQR KAKEAAGPAP SPMRAANRSH SAGRTPGRTP 70 80 90 100 110 120 GKSSSKVQTT PSKPGGDRYI PHRSAAQMEV ASFLLSKENQ PENSQTPTKK EHQKAWALNL 130 140 150 160 170 180 NGFDVEEAKI LRLSGKPQNA PEGYQNRLKV LYSQKATPGS SRKTCRYIPS LPDRILDAPE 190 200 210 220 230 240 IRNDYYLNLV DWSSGNVLAV ALDNSVYLWS ASSGDILQLL QMEQPGEYIS SVAWIKEGNY 250 260 270 280 290 300 LAVGTSSAEV QLWDVQQQKR LRNMTSHSAR VGSLSWNSYI LSSGSRSGHI HHHDVRVAEH 310 320 330 340 350 360 HVATLSGHSQ EVCGLRWAPD GRHLASGGND NLVNVWPSAP GEGGWVPLQT FTQHQGAVKA 370 380 390 400 410 420 VAWCPWQSNV LATGGGTSDR HIRIWNVCSG ACLSAVDAHS QVCSILWSPH YKELISGHGF 430 440 450 460 470 480 AQNQLVIWKY PTMAKVAELK GHTSRVLSLT MSPDGATVAS AAADETLRLW RCFELDPARR 490 REREKASAAK SSLIHQGIR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel mammalian protein, p55CDC, present in dividing cells is associated with protein kinase activity and has homology to the Saccharomyces cerevisiae cell division cycle proteins Cdc20 and Cdc4." Weinstein J., Jacobsen F.W., Hsu-Chen J., Wu T., Baum L.G. Mol. Cell. Biol. 14:3350-3363(1994) [PubMed: 7513050] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Activation of the human anaphase-promoting complex by proteins of the CDC20/Fizzy family." Kramer E.R., Gieffers C., Hoelzl G., Hengstschlaeger M., Peters J.-M. Curr. Biol. 8:1207-1210(1998) [PubMed: 9811605] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MAD2L1 AND APC/C. Tissue: Liver and Spleen.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	NIEHS SNPs program Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-402 AND GLN-479.
[6]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon, Colon adenocarcinoma, Lymph, Muscle, Ovary and Skin.
[8]	"Direct binding of CDC20 protein family members activates the anaphase-promoting complex in mitosis and G1." Fang G., Yu H., Kirschner M.W. Mol. Cell 2:163-171(1998) [PubMed: 9734353] [Abstract] Cited for: FUNCTION, INTERACTION WITH APC/C.
[9]	"The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation." Fang G., Yu H., Kirschner M.W. Genes Dev. 12:1871-1883(1998) [PubMed: 9637688] [Abstract] Cited for: FUNCTION, INTERACTION WITH MAD2L1 AND APC/C.
[10]	"Regulation of APC activity by phosphorylation and regulatory factors." Kotani S., Tanaka H., Yasuda H., Todokoro K. J. Cell Biol. 146:791-800(1999) [PubMed: 10459014] [Abstract] Cited for: PHOSPHORYLATION.
[11]	"Mitotic regulation of the human anaphase-promoting complex by phosphorylation." Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J., Peters J.-M. EMBO J. 22:6598-6609(2003) [PubMed: 14657031] [Abstract] Cited for: PHOSPHORYLATION AT THR-70 AND THR-106.
[12]	"The APC/C maintains the spindle assembly checkpoint by targeting Cdc20 for destruction." Nilsson J., Yekezare M., Minshull J., Pines J. Nat. Cell Biol. 10:1411-1420(2008) [PubMed: 18997788] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH BUB1B, DEGRADATION BY THE PROTEASOME.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, MASS SPECTROMETRY.
[14]	"APC/C- and Mad2-mediated degradation of Cdc20 during spindle checkpoint activation." Ge S., Skaar J.R., Pagano M. Cell Cycle 8:167-171(2009) [PubMed: 19098431] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH MAD2L1 AND BUB1B, DEGRADATION BY THE PROTEASOME, MUTAGENESIS OF ARG-132.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases
EMBLGenBankDDBJ	U05340 mRNA. Translation: AAA19017.1. AF099644 mRNA. Translation: AAD16405.1. AK312780 mRNA. Translation: BAG35643.1. BT007388 mRNA. Translation: AAP36052.1. DQ473545 Genomic DNA. Translation: ABE96834.1. AL139289 Genomic DNA. Translation: CAB92757.1. BC000624 mRNA. Translation: AAH00624.1. BC001088 mRNA. Translation: AAH01088.1. BC006272 mRNA. Translation: AAH06272.1. BC009425 mRNA. Translation: AAH09425.1. BC009426 mRNA. Translation: AAH09426.1. BC010044 mRNA. Translation: AAH10044.1. BC012803 mRNA. Translation: AAH12803.1. BC012827 mRNA. Translation: AAH12827.1. BC013303 mRNA. Translation: AAH13303.1. BC015998 mRNA. Translation: AAH15998.1. BC024257 mRNA. Translation: AAH24257.1. BC031294 mRNA. Translation: AAH31294.1. BC110321 mRNA. Translation: AAI10322.1.
IPI	IPI00329526.
PIR	A56021.
RefSeq	NP_001246.2.
UniGene	Hs.524947
3D structure databases
HSSP	HSSP built from PDB template 1ERJ based on UniProtKB P16649.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q12834. 14 interactions.
PTM databases
PhosphoSite	Q12834.
Proteomic databases
PRIDE	Q12834.
Genome annotation databases
Ensembl	ENSG00000117399. Homo sapiens. [Contig view]
GeneID	991.
KEGG	hsa:991.
Organism-specific databases
GeneCards	GC01P043597.
HGNC	HGNC:1723. CDC20.
HPA	CAB004525.
MIM	603618. gene.
PharmGKB	PA26257.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q12834.
HOVERGEN	Q12834.
OMA	Q12834. LRLWRCF.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
Gene expression databases
CleanEx	HS_CDC20.
GermOnline	ENSG00000117399. Homo sapiens.
Family and domain databases
InterPro	IPR015943. WD40/YVTN_repeat-like. IPR001680. WD40_repeat. IPR019782. WD40_repeat_2. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_region. IPR019781. WD40_repeat_sg. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
Pfam	PF00400. WD40. 4 hits. [Graphical view]
ProDom	PD004563. Fizzy. 1 hit. PD000018. WD40. 2 hits. [Graphical view] [Entries sharing at least one domain]
SMART	SM00320. WD40. 7 hits. [Graphical view]
PROSITE	PS00678. WD_REPEATS_1. 1 hit. PS50082. WD_REPEATS_2. 3 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	4160.
PMAP-CutDB	Q12834.
SOURCE	Search...

Entry information

Entry name

CDC20_HUMAN

Accession

Primary (citable) accession number: Q12834
Secondary accession number(s): B2R6Z6 , Q5JUY4, Q9BW56, Q9UQI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	October 3, 2003
Last modified:	June 16, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)