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UniProtKB - Q12834 (CDC20_HUMAN)

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Protein

Cell division cycle protein 20 homolog

Gene

CDC20

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

  • anaphase-promoting complex binding Source: InterPro
  • enzyme binding Source: UniProtKB
  • histone deacetylase binding Source: Ensembl
  • protein C-terminus binding Source: UniProtKB
  • ubiquitin-protein transferase activator activity Source: InterPro
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

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

Enzyme and pathway databases

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-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000117399.13
HGNCiHGNC:1723 CDC20
MIMi603618 gene
neXtProtiNX_Q12834

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
ProteomicsDBi58976

PTM databases

iPTMnetiQ12834
PhosphoSitePlusiQ12834

Miscellaneous databases

PMAP-CutDBiQ12834

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. Interacts with HSF1 (via phosphorylated form); this interaction occurs in mitosis in a MAD2L1-dependent manner and prevents PLK1-stimulated degradation of HSF1 by blocking the recruitment of the SCF(BTRC) ubiquitin ligase complex (PubMed:18794143).By similarity12 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • histone deacetylase binding Source: Ensembl
  • protein C-terminus binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi107427, 180 interactors
CORUMiQ12834
DIPiDIP-29655N
ELMiQ12834
IntActiQ12834, 67 interactors
MINTiQ12834
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

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

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0305 Eukaryota
ENOG410XQ8I LUCA
GeneTreeiENSGT00870000136444
HOGENOMiHOG000195514
HOVERGENiHBG001024
InParanoidiQ12834
KOiK03363
OMAiWQSNILA
OrthoDBiEOG091G06FJ
PhylomeDBiQ12834
TreeFamiTF101065

Family and domain databases

Gene3Di2.130.10.10, 1 hit
InterProiView protein in InterPro
IPR024977 Apc4_WD40_dom
IPR033187 CDC20
IPR033010 Cdc20/Fizzy
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR001680 WD40_repeat
IPR019775 WD40_repeat_CS
IPR017986 WD40_repeat_dom
IPR036322 WD40_repeat_dom_sf
PANTHERiPTHR19918 PTHR19918, 1 hit
PTHR19918:SF3 PTHR19918:SF3, 1 hit
PfamiView protein in Pfam
PF12894 ANAPC4_WD40, 1 hit
PF00400 WD40, 4 hits
SMARTiView protein in SMART
SM00320 WD40, 7 hits
SUPFAMiSSF50978 SSF50978, 1 hit
PROSITEiView protein in PROSITE
PS00678 WD_REPEATS_1, 1 hit
PS50082 WD_REPEATS_2, 3 hits
PS50294 WD_REPEATS_REGION, 1 hit

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 → M1 PublicationCorresponds to variant dbSNP:rs45443196Ensembl.1
Natural variantiVAR_030369479R → Q1 PublicationCorresponds to variant dbSNP:rs45461499Ensembl.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 No translation available.
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

Similar proteinsi

Entry informationi

Entry nameiCDC20_HUMAN
AccessioniPrimary (citable) accession number: Q12834
Secondary accession number(s): B2R6Z6
, D3DPJ1, Q5JUY4, Q9BW56, Q9UQI9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: July 18, 2018
This is version 183 of the entry and version 2 of the sequence. See 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

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