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UniProtKB - Q12834 (CDC20_HUMAN)

Entry version 205 (02 Jun 2021)
Sequence version 2 (03 Oct 2003)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q12834

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-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-9648025, EML4 and NUDC in mitotic spindle formation
R-HSA-983168, Antigen processing: Ubiquitination & Proteasome degradation

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		Q12834

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q12834

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00143

Protein family/group databases

Transport Classification Database

More...TCDBi		9.A.61.2.2, the domain of unknown function 3339 (duf3339) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cell division cycle protein 20 homolog
Alternative name(s):
p55CDC
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CDC20
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:1723, CDC20

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		603618, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q12834

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000117399.13

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

More...DisGeNETi		991

Open Targets

More...OpenTargetsi		ENSG00000117399

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA26257

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q12834, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4523283

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CDC20

Domain mapping of disease mutations (DMDM)

More...DMDMi		37537762

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000509001 – 499Cell division cycle protein 20 homologAdd BLAST499

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...EPDi		Q12834

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q12834

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q12834

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q12834

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q12834

PeptideAtlas

More...PeptideAtlasi		Q12834

PRoteomics IDEntifications database

More...PRIDEi		Q12834

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		58976

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q12834

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q12834

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q12834

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000117399, Expressed in ventricular zone and 168 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q12834, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000117399, Tissue enhanced (lymphoid tissue, testis)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of a complex with CDC20, CDC27, SPATC1 and TUBG1 (By similarity).

Interacts with NEUROD2 (By similarity).

Interacts with dimeric MAD2L1 in its closed conformation form (PubMed:9811605, PubMed:9637688, PubMed:15525512, PubMed:19098431, PubMed:29162720).

Interacts with BUB1B (PubMed:15525512, PubMed:18997788, PubMed:19098431). The phosphorylated form interacts with APC/C (PubMed:9811605, PubMed:9734353, PubMed:9637688).

Interacts with NINL (PubMed:17403670). May interact with MAD2L2 (PubMed:11459826).

Interacts with CDK5RAP2 (PubMed:19282672).

Interacts with SIRT2 (PubMed:22014574).

Interacts with isoform 1 of NEK2 (PubMed:20034488).

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).

Interacts (via the N-terminal substrate-binding domain) with FBXO5 (By similarity).

By similarity13 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		107427, 201 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3946, Mitotic Checkpoint Complex
CPX-6087, Anaphase-Promoting complex, CDC20 variant

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q12834

Database of interacting proteins

More...DIPi		DIP-29655N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q12834

Protein interaction database and analysis system

More...IntActi		Q12834, 72 interactors

Molecular INTeraction database

More...MINTi		Q12834

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000361540

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q12834

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q12834, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1499
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q12834

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni17 – 80DisorderedSequence analysisAdd BLAST64

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi52 – 72Polar residuesSequence analysisAdd BLAST21

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the WD repeat CDC20/Fizzy family.Curated

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0305, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00950000183104

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_014831_6_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q12834

Identification of Orthologs from Complete Genome Data

More...OMAi		WSPHKKE

Database of Orthologous Groups

More...OrthoDBi		1220675at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q12834

TreeFam database of animal gene trees

More...TreeFami		TF101065

Family and domain databases

Database of protein disorder

More...DisProti		DP01118

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.130.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR024977, Apc4_WD40_dom
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

The PANTHER Classification System

More...PANTHERi		PTHR19918, PTHR19918, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF12894, ANAPC4_WD40, 1 hit
PF00400, WD40, 4 hits

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00320, WD40, 7 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50978, SSF50978, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00678, WD_REPEATS_1, 1 hit
PS50082, WD_REPEATS_2, 3 hits
PS50294, WD_REPEATS_REGION, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iFD5C967AF84089E8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti101P → S in AAA19017 (PubMed:7513050).Curated1
Sequence conflicti117A → V in AAH00624 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS484.1

Protein sequence database of the Protein Information Resource

More...PIRi		A56021

NCBI Reference Sequences

More...RefSeqi		NP_001246.2, NM_001255.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000310955; ENSP00000308450; ENSG00000117399
ENST00000372462; ENSP00000361540; ENSG00000117399

Database of genes from NCBI RefSeq genomes

More...GeneIDi		991

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:991

UCSC genome browser

More...UCSCi		uc001cix.4, human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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 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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...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[»]
5KHUelectron microscopy4.80R/S1-499[»]
5LCWelectron microscopy4.00Q126-499[»]
R1-499[»]
6F0Xelectron microscopy4.60Q1-499[»]
6Q6Gelectron microscopy3.20R1-499[»]
6Q6Helectron microscopy3.20R1-499[»]
SMRiQ12834
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi107427, 201 interactors
ComplexPortaliCPX-3946, Mitotic Checkpoint Complex
CPX-6087, Anaphase-Promoting complex, CDC20 variant
CORUMiQ12834
DIPiDIP-29655N
ELMiQ12834
IntActiQ12834, 72 interactors
MINTiQ12834
STRINGi9606.ENSP00000361540

Chemistry databases

BindingDBiQ12834
ChEMBLiCHEMBL4523283

Protein family/group databases

TCDBi9.A.61.2.2, the domain of unknown function 3339 (duf3339) family

PTM databases

iPTMnetiQ12834
PhosphoSitePlusiQ12834
SwissPalmiQ12834

Genetic variation databases

BioMutaiCDC20
DMDMi37537762

Proteomic databases

EPDiQ12834
jPOSTiQ12834
MassIVEiQ12834
MaxQBiQ12834
PaxDbiQ12834
PeptideAtlasiQ12834
PRIDEiQ12834
ProteomicsDBi58976

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3864, 694 antibodies

The DNASU plasmid repository

More...DNASUi		991

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		991
DisGeNETi991

GeneCards: human genes, protein and diseases

More...GeneCardsi		CDC20
HGNCiHGNC:1723, CDC20
HPAiENSG00000117399, Tissue enhanced (lymphoid tissue, testis)
MIMi603618, gene
neXtProtiNX_Q12834
OpenTargetsiENSG00000117399
PharmGKBiPA26257
VEuPathDBiHostDB:ENSG00000117399.13

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0305, Eukaryota
GeneTreeiENSGT00950000183104
HOGENOMiCLU_014831_6_1_1
InParanoidiQ12834
OMAiWSPHKKE
OrthoDBi1220675at2759
PhylomeDBiQ12834
TreeFamiTF101065

Enzyme and pathway databases

UniPathwayiUPA00143
PathwayCommonsiQ12834
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-9648025, EML4 and NUDC in mitotic spindle formation
R-HSA-983168, Antigen processing: Ubiquitination & Proteasome degradation
SignaLinkiQ12834
SIGNORiQ12834

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		991, 796 hits in 1010 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		CDC20, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		CDC20

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		991
PharosiQ12834, Tbio

Protein Ontology

More...PROi		PR:Q12834
RNActiQ12834, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000117399, Expressed in ventricular zone and 168 other tissues
GenevisibleiQ12834, HS

Family and domain databases

DisProtiDP01118
Gene3Di2.130.10.10, 1 hit
InterProiView protein in InterPro
IPR024977, Apc4_WD40_dom
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
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

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCDC20_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q12834
Secondary accession number(s): B2R6Z6
, D3DPJ1, Q5JUY4, Q9BW56, Q9UQI9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: June 2, 2021
This is version 205 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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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