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Q12834 (CDC20_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cell division cycle protein 20 homolog
Alternative name(s):
p55CDC
Gene names
Name:CDC20
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Protein existenceEvidence 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 1of NEK2. Ref.2 Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.17 Ref.19 Ref.20 Ref.21

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle 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 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 processCell cycle
Cell division
Differentiation
Mitosis
Neurogenesis
Ubl conjugation pathway
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityPolymorphism
   DomainRepeat
WD repeat
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation 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 cycle

Traceable author statement PubMed 9682218. Source: ProtInc

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

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: Ensembl

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: Ensembl

regulation of meiosis

Inferred from electronic annotation. Source: Ensembl

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

   Cellular_componentcentrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

spindle

Traceable author statement Ref.1. Source: ProtInc

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionenzyme binding

Inferred from physical interaction Ref.16. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction PubMed 10700282. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 499499Cell division cycle protein 20 homolog
PRO_0000050900

Regions

Repeat182 – 22140WD 1
Repeat224 – 26340WD 2
Repeat266 – 30338WD 3
Repeat307 – 34640WD 4
Repeat353 – 39543WD 5
Repeat397 – 43842WD 6
Repeat441 – 48040WD 7

Amino acid modifications

Modified residue411Phosphoserine Ref.14
Modified residue701Phosphothreonine Ref.13
Modified residue721Phosphoserine Ref.14
Modified residue921Phosphoserine Ref.14
Modified residue1061Phosphothreonine Ref.13
Modified residue1531Phosphoserine Ref.14
Modified residue1571Phosphothreonine Ref.14
Modified residue1611Phosphoserine Ref.14
Cross-link485Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.23
Cross-link490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.23

Natural variations

Natural variant4021V → M. Ref.5
VAR_030368
Natural variant4791R → Q. Ref.5
Corresponds to variant rs45461499 [ dbSNP | Ensembl ].
VAR_030369

Experimental info

Mutagenesis411S → 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
Mutagenesis721S → 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
Mutagenesis921S → 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
Mutagenesis1321R → A: Loss of interaction with MAD2L1. Ref.19
Mutagenesis1531S → 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
Mutagenesis1571T → 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
Mutagenesis1611S → 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
Mutagenesis4851K → R: Does not affect its ability to bind the APC/C complex; when associated with R-490. Ref.23
Mutagenesis4901K → R: Does not affect its ability to bind the APC/C complex; when associated with R-485. Ref.23
Sequence conflict1011P → S in AAA19017. Ref.1
Sequence conflict1171A → V in AAH00624. Ref.8

Secondary structure

.................................................................. 499
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12834 [UniParc].

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

FASTA49954,723
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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.

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.
PIRA56021.
RefSeqNP_001246.2. NM_001255.2.
UniGeneHs.524947.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GGAX-ray2.04A81-499[»]
4GGCX-ray1.35A161-477[»]
4GGDX-ray2.44A/B71-499[»]
ProteinModelPortalQ12834.
SMRQ12834. Positions 165-478.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107427. 100 interactions.
DIPDIP-29655N.
IntActQ12834. 35 interactions.
MINTMINT-2211271.
STRING9606.ENSP00000308450.

PTM databases

PhosphoSiteQ12834.

Polymorphism databases

DMDM37537762.

Proteomic databases

PaxDbQ12834.
PRIDEQ12834.

Protocols and materials databases

DNASU991.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310955; ENSP00000308450; ENSG00000117399.
ENST00000372462; ENSP00000361540; ENSG00000117399.
GeneID991.
KEGGhsa:991.
UCSCuc001cix.3. human.

Organism-specific databases

CTD991.
GeneCardsGC01P043824.
H-InvDBHIX0034879.
HGNCHGNC:1723. CDC20.
HPACAB004525.
HPA045842.
HPA055288.
MIM603618. gene.
neXtProtNX_Q12834.
PharmGKBPA26257.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000195514.
HOVERGENHBG001024.
InParanoidQ12834.
KOK03363.
OMARTPGKSN.
OrthoDBEOG76X602.
PhylomeDBQ12834.
TreeFamTF101065.

Enzyme and pathway databases

ReactomeREACT_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.
SignaLinkQ12834.
UniPathwayUPA00143.

Gene expression databases

BgeeQ12834.
CleanExHS_CDC20.
GenevestigatorQ12834.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 3 hits.
[Graphical view]
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCDC20.
GenomeRNAi991.
NextBio4160.
PMAP-CutDBQ12834.
PROQ12834.
SOURCESearch...

Entry information

Entry nameCDC20_HUMAN
AccessionPrimary (citable) accession number: Q12834
Secondary accession number(s): B2R6Z6 expand/collapse secondary AC list , D3DPJ1, Q5JUY4, Q9BW56, Q9UQI9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: April 16, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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