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Entry version 204 (07 Oct 2020)
Sequence version 1 (01 Aug 1990)
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Protein

Anaphase-promoting complex subunit CDC23

Gene

CDC23

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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

Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.5 Publications

Miscellaneous

Present with 80 molecules/cell in log phase SD medium.1 Publication

<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

  • cyclin binding Source: SGD

GO - Biological processi

<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, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-179409, APC-Cdc20 mediated degradation of Nek2A
R-SCE-983168, Antigen processing: Ubiquitination & Proteasome degradation

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

More...
UniPathwayi
UPA00143

<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:
Anaphase-promoting complex subunit CDC23
Alternative name(s):
Cell division control protein 23
<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:CDC23
Ordered Locus Names:YHR166C
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<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 identifieri559292 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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
  • UP000002311 <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 VIII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YHR166C

Saccharomyces Genome Database

More...
SGDi
S000001209, CDC23

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

<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>Mutagenesisi39A → T in CDC23-50; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication1
Mutagenesisi42G → D in CDC23-54; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication1
Mutagenesisi80G → S in CDC23-44; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication1
Mutagenesisi85E → K in CDC23-51; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication1
Mutagenesisi93S → F in CDC23-52; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication1
Mutagenesisi94T → M in CDC23-4; G2/M cell cycle arrest at 36 degrees Celsius. 1 Publication1
Mutagenesisi103R → Q in CDC23-40; G2/M cell cycle arrest at 37 degrees Celsius; when associated with V-573. 1 Publication1
Mutagenesisi114P → L in CDC23-53; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication1
Mutagenesisi114P → S in CDC23-41; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication1
Mutagenesisi123S → N in CDC23-6; G2/M cell cycle arrest at 36 degrees Celsius. 1 Publication1
Mutagenesisi213G → D in CDC23-47; G2/M cell cycle arrest at 37 degrees Celsius; when associated with W-583. 1 Publication1
Mutagenesisi306E → K in CDC23-49; G2/M cell cycle arrest at 37 degrees Celsius; when associated with P-326. 1 Publication1
Mutagenesisi326P → L in CDC23-49; G2/M cell cycle arrest at 37 degrees Celsius; when associated with E-306. 1 Publication1
Mutagenesisi398E → K in CDC23-37; G2/M cell cycle arrest at 30 degrees Celsius. 1 Publication1
Mutagenesisi404A → T in CDC23-39; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication1
Mutagenesisi439H → R in CDC23-2; G2/M cell cycle arrest at 36 degrees Celsius. 1 Publication1
Mutagenesisi472G → D in CDC23-1; G2/M cell cycle arrest at 36 degrees Celsius. 1 Publication1
Mutagenesisi485L → F in CDC23-56; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication1
Mutagenesisi573V → I in CDC23-40; G2/M cell cycle arrest at 37 degrees Celsius; when associated with R-103. 1 Publication1
Mutagenesisi583 – 626Missing in CDC23-47; G2/M cell cycle arrest at 37 degrees Celsius; when associated with G-213. Add BLAST44

<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_00001062721 – 626Anaphase-promoting complex subunit CDC23Add BLAST626

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 residuei59Phosphoserine; by CDC28Combined sources1 Publication1

<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

Phosphorylated by CDC28, which is required for the early mitotic activity of the APC/C in its CDC20-bound form.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P16522

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

More...
PaxDbi
P16522

PRoteomics IDEntifications database

More...
PRIDEi
P16522

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P16522

<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

The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. CDC23 interacts directly with SWM1 and binds the destruction box (D-box) of the substrate cyclin CLB2.

3 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
36600, 503 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-756, Anaphase-Promoting core complex
CPX-760, Anaphase-Promoting Complex, CDC20 variant
CPX-761, Anaphase-Promoting Complex, CDH1 variant
CPX-762, Anaphase-Promoting complex AMA1 variant

Database of interacting proteins

More...
DIPi
DIP-589N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P16522

Protein interaction database and analysis system

More...
IntActi
P16522, 26 interactors

Molecular INTeraction database

More...
MINTi
P16522

STRING: functional protein association networks

More...
STRINGi
4932.YHR166C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P16522, protein

<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>Repeati215 – 248TPR 1Add BLAST34
Repeati295 – 328TPR 2Add BLAST34
Repeati329 – 362TPR 3Add BLAST34
Repeati363 – 396TPR 4Add BLAST34
Repeati397 – 430TPR 5Add BLAST34
Repeati431 – 464TPR 6Add BLAST34
Repeati465 – 498TPR 7Add BLAST34
Repeati499 – 532TPR 8Add BLAST34
Repeati536 – 569TPR 9Add BLAST34

<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 APC8/CDC23 family.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1155, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000182950

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_018320_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P16522

KEGG Orthology (KO)

More...
KOi
K03355

Identification of Orthologs from Complete Genome Data

More...
OMAi
EYDRCAA

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.40.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007192, APC8
IPR013026, TPR-contain_dom
IPR011990, TPR-like_helical_dom_sf
IPR019734, TPR_repeat

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04049, ANAPC8, 1 hit
PF13181, TPR_8, 4 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00028, TPR, 6 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48452, SSF48452, 3 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50005, TPR, 6 hits
PS50293, TPR_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.

P16522-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNDDSQDKII HDIRIQLRKA ATELSRWKLY GSSKWAAEAL AGLAEAIDVD
60 70 80 90 100
QTHSLADESP LRNKQGVPKQ MFEIPQNGFG LSETEYDLYL LGSTLFDAKE
110 120 130 140 150
FDRCVFFLKD VTNPYLKFLK LYSKFLSWDK KSQESMENIL TTGKFTDEMY
160 170 180 190 200
RANKDGDGSG NEDINQSGHQ RANLKMVSNE HESQSNISSI LKEINTFLES
210 220 230 240 250
YEIKIDDDEA DLGLALLYYL RGVILKQEKN ISKAMSSFLK SLSCYSFNWS
260 270 280 290 300
CWLELMDCLQ KVDDALLLNN YLYQNFQFKF SENLGSQRTI EFNIMIKFFK
310 320 330 340 350
LKVFEELNGQ LEDYFEDLEF LLQVFPNFTF LKAYNATISY NNLDYVTAES
360 370 380 390 400
RFDDIVKQDP YRLNDLETYS NILYVMQKNS KLAYLAQFVS QIDRFRPETC
410 420 430 440 450
CIIANYYSAR QEHEKSIMYF RRALTLDKKT TNAWTLMGHE FVELSNSHAA
460 470 480 490 500
IECYRRAVDI CPRDFKAWFG LGQAYALLDM HLYSLYYFQK ACTLKPWDRR
510 520 530 540 550
IWQVLGECYS KTGNKVEAIK CYKRSIKASQ TVDQNTSIYY RLAQLYEELE
560 570 580 590 600
DLQECKKFMM KCVDVEELLE GIVTDETVKA RLWLAIFEIK AGNYQLAYDY
610 620
AMGVSSGTSQ EIEEARMLAR ECRRHM
Length:626
Mass (Da):73,114
Last modified:August 1, 1990 - v1
<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:i3C96FE2BC8097118
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D00610 Genomic DNA Translation: BAA00485.1
U00027 Genomic DNA Translation: AAB68012.1
BK006934 Genomic DNA Translation: DAA06859.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S12330, RGBY23

NCBI Reference Sequences

More...
RefSeqi
NP_012036.1, NM_001179297.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YHR166C_mRNA; YHR166C; YHR166C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
856571

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YHR166C

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00610 Genomic DNA Translation: BAA00485.1
U00027 Genomic DNA Translation: AAB68012.1
BK006934 Genomic DNA Translation: DAA06859.1
PIRiS12330, RGBY23
RefSeqiNP_012036.1, NM_001179297.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGRIDi36600, 503 interactors
ComplexPortaliCPX-756, Anaphase-Promoting core complex
CPX-760, Anaphase-Promoting Complex, CDC20 variant
CPX-761, Anaphase-Promoting Complex, CDH1 variant
CPX-762, Anaphase-Promoting complex AMA1 variant
DIPiDIP-589N
ELMiP16522
IntActiP16522, 26 interactors
MINTiP16522
STRINGi4932.YHR166C

PTM databases

iPTMnetiP16522

Proteomic databases

MaxQBiP16522
PaxDbiP16522
PRIDEiP16522

Genome annotation databases

EnsemblFungiiYHR166C_mRNA; YHR166C; YHR166C
GeneIDi856571
KEGGisce:YHR166C

Organism-specific databases

EuPathDBiFungiDB:YHR166C
SGDiS000001209, CDC23

Phylogenomic databases

eggNOGiKOG1155, Eukaryota
GeneTreeiENSGT00950000182950
HOGENOMiCLU_018320_2_1_1
InParanoidiP16522
KOiK03355
OMAiEYDRCAA

Enzyme and pathway databases

UniPathwayiUPA00143
ReactomeiR-SCE-179409, APC-Cdc20 mediated degradation of Nek2A
R-SCE-983168, Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P16522
RNActiP16522, protein

Family and domain databases

Gene3Di1.25.40.10, 2 hits
InterProiView protein in InterPro
IPR007192, APC8
IPR013026, TPR-contain_dom
IPR011990, TPR-like_helical_dom_sf
IPR019734, TPR_repeat
PfamiView protein in Pfam
PF04049, ANAPC8, 1 hit
PF13181, TPR_8, 4 hits
SMARTiView protein in SMART
SM00028, TPR, 6 hits
SUPFAMiSSF48452, SSF48452, 3 hits
PROSITEiView protein in PROSITE
PS50005, TPR, 6 hits
PS50293, TPR_REGION, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiCDC23_YEAST
<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: P16522
Secondary accession number(s): D3DLB5
<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: August 1, 1990
Last sequence update: August 1, 1990
Last modified: October 7, 2020
This is version 204 of the entry and version 1 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 programFungal Protein Annotation Program

<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

Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families
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