Q12834 (CDC20_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	499 AA.
Sequence status	Complete.
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. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces presynaptic differentiation. Ref.2 Ref.9 Ref.10
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Found in a complex with CDC20, CDC27, SPATC1 and TUBG1. Interacts with SPATC1. Interacts with NEUROD2 By similarity. Interacts with MAD2L1 and BUB1B. The phosphorylated form interacts with APC/C. Interacts with NINL. May interact with MAD2L2. Interacts with CDK5RAP2. Interacts with isoform 1 of NEK2. Ref.2 Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.17 Ref.19 Ref.20 Ref.21
Subcellular location	Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle pole Ref.21.
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). Phosphorylated by BUB1 at Ser-41; Ser-72; Ser-92; Ser-153; Thr-157 and Ser-161. Phosphorylated by NEK2. Ref.11 Ref.13 Ref.14 Ref.21 Ref.24 Dephosphorylated by CTDP1. Ref.11 Ref.13 Ref.14 Ref.21 Ref.24 Ubiquitinated and degraded by the proteasome during spindle assembly checkpoint. Deubiquitinated by USP44, leading to stabilize the MAD2L1-CDC20-APC/C ternary complex, thereby preventing premature activation of the APC/C. Ubiquitinated at Lys-490 during prometaphase. Ubiquitination at Lys-485 and Lys-490 has no effect on its ability to bind the APC/C completo bind the APC/C complex. Ref.16 Ref.17 Ref.19 Ref.23
Sequence similarities	Belongs to the WD repeat CDC20/Fizzy family. Contains 7 WD repeats.

Ontologies

Keywords
Biological process	Cell cycle Cell division Differentiation Mitosis Neurogenesis Ubl conjugation pathway
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Polymorphism
Domain	Repeat WD repeat
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of anaphase-promoting complex activity Inferred from direct assay Ref.12. Source: UniProtKB anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.16. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW mitotic prometaphase Traceable author statement. Source: Reactome mitotic spindle assembly checkpoint Traceable author statement. Source: Reactome negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of synapse maturation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of synaptic plasticity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome protein ubiquitination Inferred from electronic annotation. Source: UniProtKB-UniPathway regulation of dendrite development Inferred from electronic annotation. Source: Compara regulation of meiosis Inferred from electronic annotation. Source: Compara
Cellular_component	centrosome Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara spindle Traceable author statement Ref.1. Source: ProtInc spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BUB1B	O60566	8	EBI-367462,EBI-1001438
CDC27	P30260	6	EBI-367462,EBI-994813
MAD2L1	Q13257	5	EBI-367462,EBI-78203
MAD2L2	Q9UI95	2	EBI-367462,EBI-77889
RASSF1	Q9NS23-2	2	EBI-367462,EBI-438698
SIRT2	Q8IXJ6-2	2	EBI-367462,EBI-5240785

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.14

Modified residue

70

1

Phosphothreonine Ref.13

Modified residue

72

1

Phosphoserine Ref.14

Modified residue

92

1

Phosphoserine Ref.14

Modified residue

106

1

Phosphothreonine Ref.13

Modified residue

153

1

Phosphoserine Ref.14

Modified residue

157

1

Phosphothreonine Ref.14

Modified residue

161

1

Phosphoserine Ref.14

Cross-link

485

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.23

Cross-link

490

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.23

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

41

1

S → A: Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-72; A-92; A-153; A-157 and A-161. Ref.14

Mutagenesis

72

1

S → A: Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-41; A-92; A-153; A-157 and A-161. Ref.14

Mutagenesis

92

1

S → A: Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-41; A-72; A-153; A-157 and A-161. Ref.14

Mutagenesis

132

1

R → A: Loss of interaction with MAD2L1. Ref.19

Mutagenesis

153

1

S → A: Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-42; A-72; A-92; A-157 and A-161. Ref.14

Mutagenesis

157

1

T → A: Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-42; A-72; A-92; A-153 and A-161. Ref.14

Mutagenesis

161

1

S → A: Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-72; A-92; A-153; A-157 and A-161. Ref.14

Mutagenesis

485

1

K → R: Does not affect its ability to bind the APC/C complex; when associated with R-490. Ref.23

Mutagenesis

490

1

K → R: Does not affect its ability to bind the APC/C complex; when associated with R-485. Ref.23

Sequence conflict

101

1

P → S in AAA19017. Ref.1

Sequence conflict

117

1

A → V in AAH00624. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

499

Helix Strand Turn

Details...

Beta strand

173 – 177

5

Beta strand

190 – 192

3

Beta strand

196 – 202

7

Beta strand

205 – 210

6

Turn

211 – 213

3

Beta strand

216 – 221

6

Beta strand

229 – 234

6

Beta strand

238 – 245

8

Beta strand

248 – 254

7

Turn

255 – 258

4

Beta strand

259 – 265

7

Beta strand

271 – 277

7

Beta strand

280 – 285

6

Beta strand

288 – 294

7

Beta strand

297 – 299

3

Beta strand

301 – 306

6

Beta strand

312 – 317

6

Beta strand

321 – 328

8

Beta strand

333 – 339

7

Beta strand

348 – 351

4

Beta strand

358 – 363

6

Beta strand

370 – 375

6

Turn

377 – 379

3

Beta strand

381 – 386

6

Turn

387 – 389

3

Beta strand

392 – 397

6

Beta strand

402 – 408

7

Turn

409 – 412

4

Beta strand

413 – 418

6

Turn

420 – 422

3

Beta strand

425 – 429

5

Turn

430 – 432

3

Beta strand

435 – 439

5

Beta strand

446 – 451

6

Beta strand

458 – 462

5

Turn

463 – 465

3

Beta strand

466 – 470

5

Sequences

	Sequence		Length	Mass (Da)
	Q12834 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon, Colon adenocarcinoma, Lymph, Muscle, Ovary and Skin.
[9]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH APC/C.
[10]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MAD2L1 AND APC/C.
[11]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[12]	"MAD2B is an inhibitor of the anaphase-promoting complex." Chen J., Fang G. Genes Dev. 15:1765-1770(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAD2L2.
[13]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-70 AND THR-106.
[14]	"Phosphorylation of Cdc20 by Bub1 provides a catalytic mechanism for APC/C inhibition by the spindle checkpoint." Tang Z., Shu H., Oncel D., Chen S., Yu H. Mol. Cell 16:387-397(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-41; SER-72; SER-92; SER-153; THR-157 AND SER-161, MASS SPECTROMETRY, INTERACTION WITH BUB1B AND MAD2L1, MUTAGENESIS OF SER-41; SER-72; SER-92; SER-153; THR-157 AND SER-161.
[15]	"Cell cycle-dependent expression of centrosomal ninein-like protein in human cells is regulated by the anaphase-promoting complex." Wang Y., Zhan Q. J. Biol. Chem. 282:17712-17719(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NINL.
[16]	"Anaphase initiation is regulated by antagonistic ubiquitination and deubiquitination activities." Stegmeier F., Rape M., Draviam V.M., Nalepa G., Sowa M.E., Ang X.L., McDonald E.R. III, Li M.Z., Hannon G.J., Sorger P.K., Kirschner M.W., Harper J.W., Elledge S.J. Nature 446:876-881(2007) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP44.
[17]	"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] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH BUB1B, DEGRADATION BY THE PROTEASOME.
[18]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[19]	"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] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH MAD2L1 AND BUB1B, DEGRADATION BY THE PROTEASOME, MUTAGENESIS OF ARG-132.
[20]	"CDK5RAP2 is required for spindle checkpoint function." Zhang X., Liu D., Lv S., Wang H., Zhong X., Liu B., Wang B., Liao J., Li J., Pfeifer G.P., Xu X. Cell Cycle 8:1206-1216(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CDK5RAP2.
[21]	"Nek2 targets the mitotic checkpoint proteins Mad2 and Cdc20: a mechanism for aneuploidy in cancer." Liu Q., Hirohashi Y., Du X., Greene M.I., Wang Q. Exp. Mol. Pathol. 88:225-233(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH NEK2.
[22]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]	"APC15 drives the turnover of MCC-CDC20 to make the spindle assembly checkpoint responsive to kinetochore attachment." Mansfeld J., Collin P., Collins M.O., Choudhary J.S., Pines J. Nat. Cell Biol. 13:1234-1243(2011) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION AT LYS-485 AND LYS-490, MUTAGENESIS OF LYS-485 AND LYS-490.
[24]	"Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit." Visconti R., Palazzo L., Della Monica R., Grieco D. Nat. Commun. 3:894-894(2012) [PubMed] [Europe PMC] [Abstract] Cited for: DEPHOSPHORYLATION.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
CH471059 Genomic DNA. Translation: EAX07101.1.
CH471059 Genomic DNA. Translation: EAX07102.1.
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. NM_001255.2.

UniGene

Hs.524947.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4GGA	X-ray	2.04	A	81-499	[»]
4GGC	X-ray	1.35	A	161-477	[»]
4GGD	X-ray	2.44	A/B	71-499	[»]

ProteinModelPortal

Q12834.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29655N.

IntAct

Q12834. 31 interactions.

MINT

MINT-2211271.

STRING

9606.ENSP00000308450.

PTM databases

PhosphoSite

Q12834.

Polymorphism databases

DMDM

37537762.

Proteomic databases

PaxDb

Q12834.

PRIDE

Q12834.

Protocols and materials databases

DNASU

991.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310955; ENSP00000308450; ENSG00000117399.
ENST00000372462; ENSP00000361540; ENSG00000117399.

GeneID

991.

KEGG

hsa:991.

UCSC

uc001cix.3. human.

Organism-specific databases

CTD

991.

GeneCards

GC01P043824.

H-InvDB

HIX0034879.

HGNC

HGNC:1723. CDC20.

HPA

CAB004525.

MIM

603618. gene.

neXtProt

NX_Q12834.

PharmGKB

PA26257.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2319.

HOGENOM

HOG000195514.

HOVERGEN

HBG001024.

InParanoid

Q12834.

KO

K03363.

OMA

RTPGKSN.

OrthoDB

EOG4CC414.

PhylomeDB

Q12834.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.

UniPathway

UPA00143.

Gene expression databases

Bgee

Q12834.

CleanEx

HS_CDC20.

Genevestigator

Q12834.

GermOnline

ENSG00000117399. Homo sapiens.

Family and domain databases

Gene3D

2.130.10.10. 1 hit.

InterPro

IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]

Pfam

PF00400. WD40. 3 hits.
[Graphical view]

SMART

SM00320. WD40. 7 hits.
[Graphical view]

SUPFAM

SSF50978. WD40_like. 1 hit.

PROSITE

PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

991.

NextBio

4160.

PMAP-CutDB

Q12834.

SOURCE

Search...

Entry information

Entry name

CDC20_HUMAN

Accession

Primary (citable) accession number: Q12834
Secondary accession number(s): B2R6Z6 , D3DPJ1, Q5JUY4, Q9BW56, Q9UQI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	October 3, 2003
Last modified:	May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.