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Q12834

- CDC20_HUMAN

UniProt

Q12834 - CDC20_HUMAN

Protein

Cell division cycle protein 20 homolog

Gene

CDC20

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (03 Oct 2003)
      Previous versions | rss
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    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 binding Source: UniProtKB
    3. 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. mitotic cell cycle Source: Reactome
    5. mitotic nuclear division Source: UniProtKB-KW
    6. mitotic spindle assembly checkpoint Source: Reactome
    7. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    8. positive regulation of cell proliferation Source: Ensembl
    9. positive regulation of synapse maturation Source: UniProtKB
    10. positive regulation of synaptic plasticity Source: UniProtKB
    11. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    12. protein ubiquitination Source: UniProtKB-UniPathway
    13. regulation of dendrite development Source: Ensembl
    14. regulation of meiosis Source: Ensembl
    15. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome

    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_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.
    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: 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: Reactome
    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

    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
    CDC27P302606EBI-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. 104 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 – 1775
    Beta strandi190 – 1923
    Beta strandi196 – 2027
    Beta strandi205 – 2106
    Turni211 – 2133
    Beta strandi216 – 2216
    Beta strandi229 – 2346
    Beta strandi238 – 2458
    Beta strandi248 – 2547
    Turni255 – 2584
    Beta strandi259 – 2657
    Beta strandi271 – 2777
    Beta strandi280 – 2856
    Beta strandi288 – 2947
    Beta strandi297 – 2993
    Beta strandi301 – 3066
    Beta strandi312 – 3176
    Beta strandi321 – 3288
    Beta strandi333 – 3397
    Beta strandi348 – 3514
    Beta strandi358 – 3636
    Beta strandi370 – 3756
    Turni377 – 3793
    Beta strandi381 – 3866
    Turni387 – 3893
    Beta strandi392 – 3976
    Beta strandi402 – 4087
    Turni409 – 4124
    Beta strandi413 – 4186
    Turni420 – 4223
    Beta strandi425 – 4295
    Turni430 – 4323
    Beta strandi435 – 4395
    Beta strandi446 – 4516
    Beta strandi458 – 4625
    Turni463 – 4653
    Beta strandi466 – 4705

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4GGAX-ray2.04A81-499[»]
    4GGCX-ray1.35A161-477[»]
    4GGDX-ray2.44A/B71-499[»]
    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.
    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

    MAQFAFESDL HSLLQLDAPI PNAPPARWQR KAKEAAGPAP SPMRAANRSH    50
    SAGRTPGRTP GKSSSKVQTT PSKPGGDRYI PHRSAAQMEV ASFLLSKENQ 100
    PENSQTPTKK EHQKAWALNL NGFDVEEAKI LRLSGKPQNA PEGYQNRLKV 150
    LYSQKATPGS SRKTCRYIPS LPDRILDAPE IRNDYYLNLV DWSSGNVLAV 200
    ALDNSVYLWS ASSGDILQLL QMEQPGEYIS SVAWIKEGNY LAVGTSSAEV 250
    QLWDVQQQKR LRNMTSHSAR VGSLSWNSYI LSSGSRSGHI HHHDVRVAEH 300
    HVATLSGHSQ EVCGLRWAPD GRHLASGGND NLVNVWPSAP GEGGWVPLQT 350
    FTQHQGAVKA VAWCPWQSNV LATGGGTSDR HIRIWNVCSG ACLSAVDAHS 400
    QVCSILWSPH YKELISGHGF AQNQLVIWKY PTMAKVAELK GHTSRVLSLT 450
    MSPDGATVAS AAADETLRLW RCFELDPARR REREKASAAK SSLIHQGIR 499
    Length:499
    Mass (Da):54,723
    Last modified:October 3, 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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS484.1.
    PIRi A56021.
    RefSeqi NP_001246.2. NM_001255.2.
    UniGenei Hs.524947.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali Q12834.
    SMRi Q12834. Positions 165-478.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107427. 104 interactions.
    DIPi DIP-29655N.
    IntActi Q12834. 38 interactions.
    MINTi MINT-2211271.
    STRINGi 9606.ENSP00000308450.

    PTM databases

    PhosphoSitei Q12834.

    Polymorphism databases

    DMDMi 37537762.

    Proteomic databases

    MaxQBi Q12834.
    PaxDbi Q12834.
    PRIDEi Q12834.

    Protocols and materials databases

    DNASUi 991.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000310955 ; ENSP00000308450 ; ENSG00000117399 .
    ENST00000372462 ; ENSP00000361540 ; ENSG00000117399 .
    GeneIDi 991.
    KEGGi hsa:991.
    UCSCi uc001cix.3. human.

    Organism-specific databases

    CTDi 991.
    GeneCardsi GC01P043824.
    H-InvDB HIX0034879.
    HGNCi HGNC:1723. CDC20.
    HPAi CAB004525.
    HPA045842.
    HPA055288.
    MIMi 603618. gene.
    neXtProti NX_Q12834.
    PharmGKBi PA26257.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000195514.
    HOVERGENi HBG001024.
    InParanoidi Q12834.
    KOi K03363.
    OMAi VSSLCWN.
    OrthoDBi EOG76X602.
    PhylomeDBi Q12834.
    TreeFami TF101065.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_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_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.
    SignaLinki Q12834.

    Miscellaneous databases

    GeneWikii CDC20.
    GenomeRNAii 991.
    NextBioi 4160.
    PMAP-CutDB Q12834.
    PROi Q12834.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q12834.
    CleanExi HS_CDC20.
    Genevestigatori Q12834.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00400. WD40. 3 hits.
    [Graphical view ]
    SMARTi SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 3 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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. "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(2011) [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(2012) [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 3, 2003
    Last sequence update: October 3, 2003
    Last modified: October 1, 2014
    This is version 143 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