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Protein

Cell division cycle protein 20 homolog

Gene

Cdc20

Organism
Mus musculus (Mouse)
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.1 Publication

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

  1. activation of anaphase-promoting complex activity Source: UniProtKB
  2. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: MGI
  3. cell division Source: UniProtKB-KW
  4. mitotic nuclear division Source: UniProtKB-KW
  5. positive regulation of cell proliferation Source: Ensembl
  6. positive regulation of synapse maturation Source: UniProtKB
  7. positive regulation of synaptic plasticity Source: UniProtKB
  8. protein ubiquitination Source: UniProtKB-UniPathway
  9. regulation of dendrite development Source: Ensembl
  10. regulation of meiosis Source: MGI
Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiREACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_204224. Phosphorylation of Emi1.
REACT_207679. Separation of Sister Chromatids.
REACT_210462. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_215601. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_222875. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_246476. Regulation of APC/C activators between G1/S and early anaphase.
REACT_248037. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_256756. Mitotic Prometaphase.
REACT_263475. Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division cycle protein 20 homolog
Short name:
mmCdc20
Alternative name(s):
p55CDC
Gene namesi
Name:Cdc20
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1859866. Cdc20.

Subcellular locationi

GO - Cellular componenti

  1. anaphase-promoting complex Source: Ensembl
  2. centrosome Source: Ensembl
  3. cytoplasm Source: MGI
  4. nucleoplasm Source: MGI
  5. nucleus Source: MGI
  6. perinuclear region of cytoplasm Source: Ensembl
  7. spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Cell division cycle protein 20 homologPRO_0000050901Add
BLAST

Amino acid modifications

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

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 (By similarity).By similarity
Dephosphorylated by CTDP1.By similarity
Ubiquitinated and degraded by the proteasome during spindle assembly checkpoint. 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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9JJ66.
PaxDbiQ9JJ66.
PRIDEiQ9JJ66.

PTM databases

PhosphoSiteiQ9JJ66.

Expressioni

Gene expression databases

BgeeiQ9JJ66.
CleanExiMM_CDC20.
GenevestigatoriQ9JJ66.

Interactioni

Subunit structurei

Interacts with MAD2L1 and BUB1B. The phosphorylated form interacts with APC/C. Interacts with NINL and MAD2L1. Interacts with CDK5RAP2. Interacts with NEK2 (By similarity). Found in a complex with CDC20, CDC27, SPATC1 and TUBG1. Interacts with NEUROD2, SIRT2 and SPATC1.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Fbxo43Q8CDI22EBI-2551389,EBI-8060482
Sirt2Q8VDQ82EBI-2551389,EBI-911012

Protein-protein interaction databases

BioGridi223749. 29 interactions.
IntActiQ9JJ66. 21 interactions.
MINTiMINT-2834618.

Structurei

3D structure databases

ProteinModelPortaliQ9JJ66.
SMRiQ9JJ66. 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.
InParanoidiQ9JJ66.
KOiK03363.
OMAiSNHIHIR.
OrthoDBiEOG76X602.
PhylomeDBiQ9JJ66.
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. 5 hits.
[Graphical view]
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JJ66-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQFVFESDL HSLLQLDAPI PNAPVARWQR KAKEATGPAP SPMRAANRSH
60 70 80 90 100
SAGRTPGRTP GKSSSKVQTT PSKPGGDRFI PQRSASQMEV ASFLLSKENQ
110 120 130 140 150
PEDRGTPTKK EHQKAWSLNL NGFDVEEAKI LRLSGKPQNA PEGYQNRLKV
160 170 180 190 200
LYSQKATPGS SRKTCRYIPS LPDRILDAPE IRNDYYLNLV DWSSGNVLAV
210 220 230 240 250
ALDNSVYLWN AGSGDILQLL QMEQPGDYIS SVAWIKEGNY LAVGTSNAEV
260 270 280 290 300
QLWDVQQQKR LRNMTSHSAR VSSLSWNSYI LSSGSRSGHI HHHDVRVAEH
310 320 330 340 350
HVATLSGHSQ EVCGLRWAPD GRHLASGGND NIVNVWPSGP GESGWAPLQT
360 370 380 390 400
FTQHQGAVKA VAWCPWQSNI LATGGGTSDR HIRIWNVCSG ACLSAVDVHS
410 420 430 440 450
QVCSILWSPH YKELISGHGF AQNQLVIWKY PTMAKVAELK GHTARVLGLT
460 470 480 490
MSPDGATVAS AAADETLRLW RCFEMDPALR REREKASVAK SSLIHQGIR
Length:499
Mass (Da):54,816
Last modified:October 3, 2003 - v2
Checksum:i81E0781BA87BA79E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851A → G in BAA97451 (Ref. 1) Curated
Sequence conflicti397 – 3971D → E in BAC36132 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB045313 mRNA. Translation: BAA97451.1.
AF312208 mRNA. Translation: AAL25714.1.
AK075998 mRNA. Translation: BAC36109.1.
AK076030 mRNA. Translation: BAC36132.1.
AK083459 mRNA. Translation: BAC38922.1.
AK168650 mRNA. Translation: BAE40507.1.
BC003215 mRNA. Translation: AAH03215.1.
CCDSiCCDS18551.1.
RefSeqiNP_075712.2. NM_023223.2.
UniGeneiMm.289747.

Genome annotation databases

EnsembliENSMUST00000006565; ENSMUSP00000006565; ENSMUSG00000006398.
GeneIDi107995.
KEGGimmu:107995.
UCSCiuc008ukc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB045313 mRNA. Translation: BAA97451.1.
AF312208 mRNA. Translation: AAL25714.1.
AK075998 mRNA. Translation: BAC36109.1.
AK076030 mRNA. Translation: BAC36132.1.
AK083459 mRNA. Translation: BAC38922.1.
AK168650 mRNA. Translation: BAE40507.1.
BC003215 mRNA. Translation: AAH03215.1.
CCDSiCCDS18551.1.
RefSeqiNP_075712.2. NM_023223.2.
UniGeneiMm.289747.

3D structure databases

ProteinModelPortaliQ9JJ66.
SMRiQ9JJ66. Positions 165-478.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223749. 29 interactions.
IntActiQ9JJ66. 21 interactions.
MINTiMINT-2834618.

PTM databases

PhosphoSiteiQ9JJ66.

Proteomic databases

MaxQBiQ9JJ66.
PaxDbiQ9JJ66.
PRIDEiQ9JJ66.

Protocols and materials databases

DNASUi107995.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006565; ENSMUSP00000006565; ENSMUSG00000006398.
GeneIDi107995.
KEGGimmu:107995.
UCSCiuc008ukc.2. mouse.

Organism-specific databases

CTDi991.
MGIiMGI:1859866. Cdc20.

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000119352.
HOGENOMiHOG000195514.
HOVERGENiHBG001024.
InParanoidiQ9JJ66.
KOiK03363.
OMAiSNHIHIR.
OrthoDBiEOG76X602.
PhylomeDBiQ9JJ66.
TreeFamiTF101065.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_204224. Phosphorylation of Emi1.
REACT_207679. Separation of Sister Chromatids.
REACT_210462. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_215601. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_222875. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_246476. Regulation of APC/C activators between G1/S and early anaphase.
REACT_248037. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_256756. Mitotic Prometaphase.
REACT_263475. Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.

Miscellaneous databases

NextBioi359849.
PROiQ9JJ66.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JJ66.
CleanExiMM_CDC20.
GenevestigatoriQ9JJ66.

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. 5 hits.
[Graphical view]
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mus musculus CDC20 mRNA, complete cds."
    Kuroda M., Oikawa K., Ohbayashi T., Iwata R., Kameta A., Ebine K.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Ssc1/Elovl1 and p55Cdc genes are co-expressed in a tail-to-tail array in proliferating cells."
    Asadi A., Jacobsson A.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  4. "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: Mammary tumor.
  5. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 59-66, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  6. "Speriolin is a novel spermatogenic cell-specific centrosomal protein associated with the seventh WD motif of Cdc20."
    Goto M., Eddy E.M.
    J. Biol. Chem. 279:42128-42138(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPATC1, IDENTIFICATION IN A COMPLEX WITH CDC27; SPATC1 AND TUBG1.
  7. "A Cdc20-APC ubiquitin signaling pathway regulates presynaptic differentiation."
    Yang Y., Kim A.H., Yamada T., Wu B., Bilimoria P.M., Ikeuchi Y., de la Iglesia N., Shen J., Bonni A.
    Science 326:575-578(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NEUROD2.
  8. "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 BY SIRT2, INTERACTION WITH SIRT2.

Entry informationi

Entry nameiCDC20_MOUSE
AccessioniPrimary (citable) accession number: Q9JJ66
Secondary accession number(s): Q3TGP1, Q8BPG4, Q99LK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: March 4, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.