Cell division cycle protein 20 homolog

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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

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Protein attributes

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

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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.
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. 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).
Sequence similarities	Belongs to the WD repeat CDC20/Fizzy family. Contains 7 WD repeats.

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Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Coding sequence diversity	Polymorphism
Domain	Repeat WD repeat
PTM	Phosphoprotein
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 binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
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-1052389
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

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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

Modified residue

70

1

Phosphothreonine

Modified residue

106

1

Phosphothreonine

Natural variations

Natural variant

402

1

V → M

VAR_030368

Natural variant

479

1

R → Q

VAR_030369

Experimental info

Sequence conflict

101

1

P → S in AAA19017. Ref.1

Sequence conflict

117

1

A → V in AAH00624. Ref.6

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Sequences

Sequence

Length

Mass (Da)

Tools

Q12834-1 [UniParc].

Last modified October 3, 2003. Version 2.
Checksum: FD5C967AF84089E8
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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

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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]	"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].
[4]	"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)." Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A. Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-402 AND GLN-479.
[5]	"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. Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	U05340 mRNA. Translation: AAA19017.1. AF099644 mRNA. Translation: AAD16405.1. 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.
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.
PTM databases
PhosphoSite	Q12834.
Polymorphism databases
NIEHS-SNPs	Search...
Genome annotation databases
Ensembl	ENSG00000117399. Homo sapiens. [Contig view]
GeneID	991.
KEGG	hsa:991.
Organism-specific databases
HGNC	HGNC:1723. CDC20.
HPA	CAB004525.
MIM	603618. gene.
PharmGKB	PA26257.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	Q12834.
HOVERGEN	Q12834.
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. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
Pfam	PF00400. WD40. 6 hits. [Graphical view]
PRINTS	PR00320. GPROTEINBRPT.
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
LinkHub	Q12834.
NextBio	4160.
SOURCE	Search...

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Entry information

Entry name

CDC20_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	October 3, 2003
Last modified:	November 25, 2008
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents