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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: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • ubiquitin-protein transferase activator activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000117399-MONOMER.
ReactomeiR-HSA-141405. Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
R-HSA-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-HSA-176417. Phosphorylation of Emi1.
R-HSA-179409. APC-Cdc20 mediated degradation of Nek2A.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ12834.
SIGNORiQ12834.
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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:1723. CDC20.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: Ensembl
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
  • perinuclear region of cytoplasm Source: Ensembl
  • protein complex Source: Ensembl
  • spindle Source: ProtInc
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi41S → 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 Publication1
Mutagenesisi72S → 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 Publication1
Mutagenesisi92S → 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 Publication1
Mutagenesisi132R → A: Loss of interaction with MAD2L1. 1 Publication1
Mutagenesisi153S → 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 Publication1
Mutagenesisi157T → 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 Publication1
Mutagenesisi161S → 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 Publication1
Mutagenesisi485K → R: Does not affect its ability to bind the APC/C complex; when associated with R-490. 1 Publication1
Mutagenesisi490K → R: Does not affect its ability to bind the APC/C complex; when associated with R-485. 1 Publication1

Organism-specific databases

DisGeNETi991.
OpenTargetsiENSG00000117399.
PharmGKBiPA26257.

Polymorphism and mutation databases

BioMutaiCDC20.
DMDMi37537762.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000509001 – 499Cell division cycle protein 20 homologAdd BLAST499

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei41PhosphoserineCombined sources1 Publication1
Modified residuei66N6-acetyllysine1 Publication1
Modified residuei70PhosphothreonineCombined sources1 Publication1
Modified residuei72Phosphoserine1 Publication1
Modified residuei92Phosphoserine1 Publication1
Modified residuei106Phosphothreonine1 Publication1
Modified residuei153Phosphoserine1 Publication1
Modified residuei157Phosphothreonine1 Publication1
Modified residuei161Phosphoserine1 Publication1
Cross-linki485Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki490Glycyl 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

EPDiQ12834.
MaxQBiQ12834.
PaxDbiQ12834.
PeptideAtlasiQ12834.
PRIDEiQ12834.

PTM databases

iPTMnetiQ12834.
PhosphoSitePlusiQ12834.

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

BgeeiENSG00000117399.
CleanExiHS_CDC20.
GenevisibleiQ12834. HS.

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.
BUB1BO6056616EBI-367462,EBI-1001438
CDC27P302607EBI-367462,EBI-994813
MAD2L1Q1325717EBI-367462,EBI-78203
MAD2L2Q9UI952EBI-367462,EBI-77889
RASSF1Q9NS23-22EBI-367462,EBI-438698
SIRT2Q8IXJ6-22EBI-367462,EBI-5240785

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107427. 168 interactors.
DIPiDIP-29655N.
IntActiQ12834. 51 interactors.
MINTiMINT-2211271.
STRINGi9606.ENSP00000308450.

Structurei

Secondary structure

1499
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi173 – 177Combined sources5
Beta strandi190 – 192Combined sources3
Beta strandi196 – 202Combined sources7
Beta strandi205 – 210Combined sources6
Turni211 – 213Combined sources3
Beta strandi216 – 221Combined sources6
Beta strandi229 – 234Combined sources6
Beta strandi238 – 245Combined sources8
Beta strandi248 – 254Combined sources7
Turni255 – 258Combined sources4
Beta strandi259 – 265Combined sources7
Beta strandi271 – 277Combined sources7
Beta strandi280 – 285Combined sources6
Beta strandi288 – 294Combined sources7
Beta strandi297 – 299Combined sources3
Beta strandi301 – 306Combined sources6
Beta strandi312 – 317Combined sources6
Beta strandi321 – 328Combined sources8
Beta strandi333 – 339Combined sources7
Beta strandi348 – 351Combined sources4
Beta strandi358 – 363Combined sources6
Beta strandi370 – 375Combined sources6
Turni377 – 379Combined sources3
Beta strandi381 – 386Combined sources6
Turni387 – 389Combined sources3
Beta strandi392 – 397Combined sources6
Beta strandi402 – 408Combined sources7
Turni409 – 412Combined sources4
Beta strandi413 – 418Combined sources6
Turni420 – 422Combined sources3
Beta strandi425 – 429Combined sources5
Turni430 – 432Combined sources3
Beta strandi435 – 439Combined sources5
Beta strandi446 – 451Combined sources6
Beta strandi458 – 462Combined sources5
Turni463 – 465Combined sources3
Beta strandi466 – 470Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GGAX-ray2.04A81-499[»]
4GGCX-ray1.35A161-477[»]
4GGDX-ray2.44A/B71-499[»]
4N14X-ray2.10A165-477[»]
5G04electron microscopy4.00R1-499[»]
5KHRelectron microscopy6.10R1-499[»]
5LCWelectron microscopy4.00Q126-499[»]
R1-499[»]
ProteinModelPortaliQ12834.
SMRiQ12834.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati182 – 221WD 1Add BLAST40
Repeati224 – 263WD 2Add BLAST40
Repeati266 – 303WD 3Add BLAST38
Repeati307 – 346WD 4Add BLAST40
Repeati353 – 395WD 5Add BLAST43
Repeati397 – 438WD 6Add BLAST42
Repeati441 – 480WD 7Add BLAST40

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

eggNOGiKOG0305. Eukaryota.
ENOG410XQ8I. LUCA.
GeneTreeiENSGT00860000133814.
HOGENOMiHOG000195514.
HOVERGENiHBG001024.
InParanoidiQ12834.
KOiK03363.
OMAiQMEMANF.
OrthoDBiEOG091G06FJ.
PhylomeDBiQ12834.
TreeFamiTF101065.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR024977. Apc4_WD40_dom.
IPR033187. CDC20.
IPR033010. Cdc20/Fizzy.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR19918. PTHR19918. 1 hit.
PTHR19918:SF3. PTHR19918:SF3. 1 hit.
PfamiPF12894. ANAPC4_WD40. 1 hit.
PF00400. WD40. 4 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 3, 2003 - v2
Checksum:iFD5C967AF84089E8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti101P → S in AAA19017 (PubMed:7513050).Curated1
Sequence conflicti117A → V in AAH00624 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_030368402V → M.1 PublicationCorresponds to variant rs45443196dbSNPEnsembl.1
Natural variantiVAR_030369479R → Q.1 PublicationCorresponds to variant rs45461499dbSNPEnsembl.1

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.4. human.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GGAX-ray2.04A81-499[»]
4GGCX-ray1.35A161-477[»]
4GGDX-ray2.44A/B71-499[»]
4N14X-ray2.10A165-477[»]
5G04electron microscopy4.00R1-499[»]
5KHRelectron microscopy6.10R1-499[»]
5LCWelectron microscopy4.00Q126-499[»]
R1-499[»]
ProteinModelPortaliQ12834.
SMRiQ12834.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107427. 168 interactors.
DIPiDIP-29655N.
IntActiQ12834. 51 interactors.
MINTiMINT-2211271.
STRINGi9606.ENSP00000308450.

PTM databases

iPTMnetiQ12834.
PhosphoSitePlusiQ12834.

Polymorphism and mutation databases

BioMutaiCDC20.
DMDMi37537762.

Proteomic databases

EPDiQ12834.
MaxQBiQ12834.
PaxDbiQ12834.
PeptideAtlasiQ12834.
PRIDEiQ12834.

Protocols and materials databases

DNASUi991.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310955; ENSP00000308450; ENSG00000117399.
ENST00000372462; ENSP00000361540; ENSG00000117399.
GeneIDi991.
KEGGihsa:991.
UCSCiuc001cix.4. human.

Organism-specific databases

CTDi991.
DisGeNETi991.
GeneCardsiCDC20.
H-InvDBHIX0034879.
HGNCiHGNC:1723. CDC20.
HPAiCAB004525.
HPA045842.
HPA055288.
MIMi603618. gene.
neXtProtiNX_Q12834.
OpenTargetsiENSG00000117399.
PharmGKBiPA26257.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0305. Eukaryota.
ENOG410XQ8I. LUCA.
GeneTreeiENSGT00860000133814.
HOGENOMiHOG000195514.
HOVERGENiHBG001024.
InParanoidiQ12834.
KOiK03363.
OMAiQMEMANF.
OrthoDBiEOG091G06FJ.
PhylomeDBiQ12834.
TreeFamiTF101065.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000117399-MONOMER.
ReactomeiR-HSA-141405. Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
R-HSA-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-HSA-176417. Phosphorylation of Emi1.
R-HSA-179409. APC-Cdc20 mediated degradation of Nek2A.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ12834.
SIGNORiQ12834.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000117399.
CleanExiHS_CDC20.
GenevisibleiQ12834. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR024977. Apc4_WD40_dom.
IPR033187. CDC20.
IPR033010. Cdc20/Fizzy.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR19918. PTHR19918. 1 hit.
PTHR19918:SF3. PTHR19918:SF3. 1 hit.
PfamiPF12894. ANAPC4_WD40. 1 hit.
PF00400. WD40. 4 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...

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: November 30, 2016
This is version 168 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

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 one 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.