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Protein

Cell division cycle protein 20 homolog

Gene

CDC20

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Pathwayi

GO - Molecular functioni

  1. enzyme binding Source: UniProtKB
  2. protein C-terminus binding Source: UniProtKB

GO - Biological processi

  1. activation of anaphase-promoting complex activity Source: UniProtKB
  2. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  3. cell cycle Source: ProtInc
  4. cell division Source: UniProtKB-KW
  5. mitotic cell cycle Source: Reactome
  6. mitotic nuclear division Source: UniProtKB-KW
  7. mitotic spindle assembly checkpoint Source: Reactome
  8. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  9. positive regulation of cell proliferation Source: Ensembl
  10. positive regulation of synapse maturation Source: UniProtKB
  11. positive regulation of synaptic plasticity Source: UniProtKB
  12. positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition Source: Reactome
  13. protein ubiquitination Source: UniProtKB-UniPathway
  14. regulation of dendrite development Source: Ensembl
  15. regulation of meiosis Source: Ensembl
  16. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Differentiation, Mitosis, Neurogenesis, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_1041. Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
REACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_682. Mitotic Prometaphase.
REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_6875. Phosphorylation of Emi1.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
SignaLinkiQ12834.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division cycle protein 20 homolog
Alternative name(s):
p55CDC
Gene namesi
Name:CDC20
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:1723. CDC20.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication. Cytoplasmcytoskeletonspindle pole 1 Publication

GO - Cellular componenti

  1. centrosome Source: Ensembl
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. nucleoplasm Source: HPA
  5. nucleus Source: HPA
  6. perinuclear region of cytoplasm Source: Ensembl
  7. protein complex Source: Ensembl
  8. spindle Source: ProtInc
  9. spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411S → 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. 1 Publication
Mutagenesisi72 – 721S → 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. 1 Publication
Mutagenesisi92 – 921S → 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. 1 Publication
Mutagenesisi132 – 1321R → A: Loss of interaction with MAD2L1. 1 Publication
Mutagenesisi153 – 1531S → 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. 1 Publication
Mutagenesisi157 – 1571T → 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. 1 Publication
Mutagenesisi161 – 1611S → 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. 1 Publication
Mutagenesisi485 – 4851K → R: Does not affect its ability to bind the APC/C complex; when associated with R-490. 1 Publication
Mutagenesisi490 – 4901K → R: Does not affect its ability to bind the APC/C complex; when associated with R-485. 1 Publication

Organism-specific databases

PharmGKBiPA26257.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Cell division cycle protein 20 homologPRO_0000050900Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411Phosphoserine1 Publication
Modified residuei66 – 661N6-acetyllysine1 Publication
Modified residuei70 – 701Phosphothreonine1 Publication
Modified residuei72 – 721Phosphoserine1 Publication
Modified residuei92 – 921Phosphoserine1 Publication
Modified residuei106 – 1061Phosphothreonine1 Publication
Modified residuei153 – 1531Phosphoserine1 Publication
Modified residuei157 – 1571Phosphothreonine1 Publication
Modified residuei161 – 1611Phosphoserine1 Publication
Cross-linki485 – 485Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki490 – 490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Acetylated. Deacetylated at Lys-66 by SIRT2; deacetylation enhances the interaction of CDC20 with CDC27, leading to activation of anaphase promoting complex/cyclosome (APC/C).1 Publication
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 NEK2.4 Publications
Dephosphorylated by CTDP1.
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.4 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ12834.
PaxDbiQ12834.
PRIDEiQ12834.

PTM databases

PhosphoSiteiQ12834.

Miscellaneous databases

PMAP-CutDBQ12834.

Expressioni

Developmental stagei

Synthesis is initiated at G1/S, protein level peaks in M phase and protein is abruptly degraded at M/G1 transition.

Gene expression databases

BgeeiQ12834.
CleanExiHS_CDC20.
GenevestigatoriQ12834.

Organism-specific databases

HPAiCAB004525.
HPA045842.
HPA055288.

Interactioni

Subunit structurei

Found in a complex with CDC20, CDC27, SPATC1 and TUBG1. Interacts with NEUROD2 and SPATC1 (By similarity). Interacts with MAD2L1 and BUB1B. The phosphorylated form interacts with APC/C. Interacts with NINL. May interact with MAD2L2. Interacts with CDK5RAP2 and SIRT2. Interacts with isoform 1 of NEK2.By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Axin2O885662EBI-367462,EBI-7690990From a different organism.
BUB1BO6056615EBI-367462,EBI-1001438
CDC27P302607EBI-367462,EBI-994813
MAD2L1Q1325716EBI-367462,EBI-78203
MAD2L2Q9UI952EBI-367462,EBI-77889
RASSF1Q9NS23-22EBI-367462,EBI-438698
SIRT2Q8IXJ6-22EBI-367462,EBI-5240785

Protein-protein interaction databases

BioGridi107427. 146 interactions.
DIPiDIP-29655N.
IntActiQ12834. 38 interactions.
MINTiMINT-2211271.
STRINGi9606.ENSP00000308450.

Structurei

Secondary structure

1
499
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi173 – 1775Combined sources
Beta strandi190 – 1923Combined sources
Beta strandi196 – 2027Combined sources
Beta strandi205 – 2106Combined sources
Turni211 – 2133Combined sources
Beta strandi216 – 2216Combined sources
Beta strandi229 – 2346Combined sources
Beta strandi238 – 2458Combined sources
Beta strandi248 – 2547Combined sources
Turni255 – 2584Combined sources
Beta strandi259 – 2657Combined sources
Beta strandi271 – 2777Combined sources
Beta strandi280 – 2856Combined sources
Beta strandi288 – 2947Combined sources
Beta strandi297 – 2993Combined sources
Beta strandi301 – 3066Combined sources
Beta strandi312 – 3176Combined sources
Beta strandi321 – 3288Combined sources
Beta strandi333 – 3397Combined sources
Beta strandi348 – 3514Combined sources
Beta strandi358 – 3636Combined sources
Beta strandi370 – 3756Combined sources
Turni377 – 3793Combined sources
Beta strandi381 – 3866Combined sources
Turni387 – 3893Combined sources
Beta strandi392 – 3976Combined sources
Beta strandi402 – 4087Combined sources
Turni409 – 4124Combined sources
Beta strandi413 – 4186Combined sources
Turni420 – 4223Combined sources
Beta strandi425 – 4295Combined sources
Turni430 – 4323Combined sources
Beta strandi435 – 4395Combined sources
Beta strandi446 – 4516Combined sources
Beta strandi458 – 4625Combined sources
Turni463 – 4653Combined sources
Beta strandi466 – 4705Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GGAX-ray2.04A81-499[»]
4GGCX-ray1.35A161-477[»]
4GGDX-ray2.44A/B71-499[»]
4N14X-ray2.10A165-477[»]
ProteinModelPortaliQ12834.
SMRiQ12834. Positions 165-478.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati182 – 22140WD 1Add
BLAST
Repeati224 – 26340WD 2Add
BLAST
Repeati266 – 30338WD 3Add
BLAST
Repeati307 – 34640WD 4Add
BLAST
Repeati353 – 39543WD 5Add
BLAST
Repeati397 – 43842WD 6Add
BLAST
Repeati441 – 48040WD 7Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat CDC20/Fizzy family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000119352.
HOGENOMiHOG000195514.
HOVERGENiHBG001024.
InParanoidiQ12834.
KOiK03363.
OMAiVSSLCWN.
OrthoDBiEOG76X602.
PhylomeDBiQ12834.
TreeFamiTF101065.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 3 hits.
[Graphical view]
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12834-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQFAFESDL HSLLQLDAPI PNAPPARWQR KAKEAAGPAP SPMRAANRSH
60 70 80 90 100
SAGRTPGRTP GKSSSKVQTT PSKPGGDRYI PHRSAAQMEV ASFLLSKENQ
110 120 130 140 150
PENSQTPTKK EHQKAWALNL NGFDVEEAKI LRLSGKPQNA PEGYQNRLKV
160 170 180 190 200
LYSQKATPGS SRKTCRYIPS LPDRILDAPE IRNDYYLNLV DWSSGNVLAV
210 220 230 240 250
ALDNSVYLWS ASSGDILQLL QMEQPGEYIS SVAWIKEGNY LAVGTSSAEV
260 270 280 290 300
QLWDVQQQKR LRNMTSHSAR VGSLSWNSYI LSSGSRSGHI HHHDVRVAEH
310 320 330 340 350
HVATLSGHSQ EVCGLRWAPD GRHLASGGND NLVNVWPSAP GEGGWVPLQT
360 370 380 390 400
FTQHQGAVKA VAWCPWQSNV LATGGGTSDR HIRIWNVCSG ACLSAVDAHS
410 420 430 440 450
QVCSILWSPH YKELISGHGF AQNQLVIWKY PTMAKVAELK GHTSRVLSLT
460 470 480 490
MSPDGATVAS AAADETLRLW RCFELDPARR REREKASAAK SSLIHQGIR
Length:499
Mass (Da):54,723
Last modified:October 2, 2003 - v2
Checksum:iFD5C967AF84089E8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011P → S in AAA19017 (PubMed:7513050).Curated
Sequence conflicti117 – 1171A → V in AAH00624 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti402 – 4021V → M.1 Publication
VAR_030368
Natural varianti479 – 4791R → Q.1 Publication
Corresponds to variant rs45461499 [ dbSNP | Ensembl ].
VAR_030369

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS484.1.
PIRiA56021.
RefSeqiNP_001246.2. NM_001255.2.
UniGeneiHs.524947.

Genome annotation databases

EnsembliENST00000310955; ENSP00000308450; ENSG00000117399.
ENST00000372462; ENSP00000361540; ENSG00000117399.
GeneIDi991.
KEGGihsa:991.
UCSCiuc001cix.3. human.

Polymorphism databases

DMDMi37537762.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS484.1.
PIRiA56021.
RefSeqiNP_001246.2. NM_001255.2.
UniGeneiHs.524947.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GGAX-ray2.04A81-499[»]
4GGCX-ray1.35A161-477[»]
4GGDX-ray2.44A/B71-499[»]
4N14X-ray2.10A165-477[»]
ProteinModelPortaliQ12834.
SMRiQ12834. Positions 165-478.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107427. 146 interactions.
DIPiDIP-29655N.
IntActiQ12834. 38 interactions.
MINTiMINT-2211271.
STRINGi9606.ENSP00000308450.

PTM databases

PhosphoSiteiQ12834.

Polymorphism databases

DMDMi37537762.

Proteomic databases

MaxQBiQ12834.
PaxDbiQ12834.
PRIDEiQ12834.

Protocols and materials databases

DNASUi991.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310955; ENSP00000308450; ENSG00000117399.
ENST00000372462; ENSP00000361540; ENSG00000117399.
GeneIDi991.
KEGGihsa:991.
UCSCiuc001cix.3. human.

Organism-specific databases

CTDi991.
GeneCardsiGC01P043824.
H-InvDBHIX0034879.
HGNCiHGNC:1723. CDC20.
HPAiCAB004525.
HPA045842.
HPA055288.
MIMi603618. gene.
neXtProtiNX_Q12834.
PharmGKBiPA26257.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000119352.
HOGENOMiHOG000195514.
HOVERGENiHBG001024.
InParanoidiQ12834.
KOiK03363.
OMAiVSSLCWN.
OrthoDBiEOG76X602.
PhylomeDBiQ12834.
TreeFamiTF101065.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_1041. Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
REACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_682. Mitotic Prometaphase.
REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_6875. Phosphorylation of Emi1.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
SignaLinkiQ12834.

Miscellaneous databases

ChiTaRSiCDC20. human.
GeneWikiiCDC20.
GenomeRNAii991.
NextBioi4160.
PMAP-CutDBQ12834.
PROiQ12834.
SOURCEiSearch...

Gene expression databases

BgeeiQ12834.
CleanExiHS_CDC20.
GenevestigatoriQ12834.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 3 hits.
[Graphical view]
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1993) [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(1997) [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(2003) [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 (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. NIEHS SNPs program
    Submitted (MAR-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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. 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(2003) [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(1997) [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(1997) [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(1998) [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(2000) [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(2002) [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(2003) [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(2006) [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(2006) [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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH BUB1B, DEGRADATION BY THE PROTEASOME.
  18. 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(2008) [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(2008) [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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH NEK2.
  22. 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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-485 AND LYS-490, MUTAGENESIS OF LYS-485 AND LYS-490.
  24. "SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity."
    Kim H.S., Vassilopoulos A., Wang R.H., Lahusen T., Xiao Z., Xu X., Li C., Veenstra T.D., Li B., Yu H., Ji J., Wang X.W., Park S.H., Cha Y.I., Gius D., Deng C.X.
    Cancer Cell 20:487-499(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION, DEACETYLATION AT LYS-66 BY SIRT2, INTERACTION WITH SIRT2.
  25. "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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEPHOSPHORYLATION.

Entry informationi

Entry nameiCDC20_HUMAN
AccessioniPrimary (citable) accession number: Q12834
Secondary accession number(s): B2R6Z6
, D3DPJ1, Q5JUY4, Q9BW56, Q9UQI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2003
Last sequence update: October 2, 2003
Last modified: March 31, 2015
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.