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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-Experimental evidence at protein leveli

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

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

  • cyclin binding Source: SGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-31200-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaphase-promoting complex subunit CDC23
Alternative name(s):
Cell division control protein 23
Gene namesi
Name:CDC23
Ordered Locus Names:YHR166C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR166C.
SGDiS000001209. CDC23.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: SGD
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001062721 – 626Anaphase-promoting complex subunit CDC23Add BLAST626

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei59Phosphoserine; by CDC28Combined sources1 Publication1

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

MaxQBiP16522.
PRIDEiP16522.

PTM databases

iPTMnetiP16522.

Interactioni

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

Binary interactionsi

WithEntry#Exp.IntActNotes
MND2P405773EBI-4216,EBI-25433
SWM1Q123794EBI-4216,EBI-33330

GO - Molecular functioni

  • cyclin binding Source: SGD

Protein-protein interaction databases

BioGridi36600. 106 interactors.
DIPiDIP-589N.
IntActiP16522. 21 interactors.
MINTiMINT-498933.

Structurei

3D structure databases

ProteinModelPortaliP16522.
SMRiP16522.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

Sequence similaritiesi

Belongs to the APC8/CDC23 family.Curated
Contains 9 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

GeneTreeiENSGT00550000074886.
HOGENOMiHOG000115852.
InParanoidiP16522.
KOiK03355.
OMAiNAWTLMG.
OrthoDBiEOG092C176G.

Family and domain databases

Gene3Di1.25.40.10. 6 hits.
InterProiIPR007192. APC8.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF04049. ANAPC8. 1 hit.
PF13414. TPR_11. 1 hit.
PF13181. TPR_8. 4 hits.
[Graphical view]
SMARTiSM00028. TPR. 6 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 5 hits.
PROSITEiPS50005. TPR. 6 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

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
Checksum:i3C96FE2BC8097118
GO

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.

Genome annotation databases

EnsemblFungiiYHR166C; YHR166C; YHR166C.
GeneIDi856571.
KEGGisce:YHR166C.

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

ProteinModelPortaliP16522.
SMRiP16522.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36600. 106 interactors.
DIPiDIP-589N.
IntActiP16522. 21 interactors.
MINTiMINT-498933.

PTM databases

iPTMnetiP16522.

Proteomic databases

MaxQBiP16522.
PRIDEiP16522.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR166C; YHR166C; YHR166C.
GeneIDi856571.
KEGGisce:YHR166C.

Organism-specific databases

EuPathDBiFungiDB:YHR166C.
SGDiS000001209. CDC23.

Phylogenomic databases

GeneTreeiENSGT00550000074886.
HOGENOMiHOG000115852.
InParanoidiP16522.
KOiK03355.
OMAiNAWTLMG.
OrthoDBiEOG092C176G.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciYEAST:G3O-31200-MONOMER.

Miscellaneous databases

PROiP16522.

Family and domain databases

Gene3Di1.25.40.10. 6 hits.
InterProiIPR007192. APC8.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF04049. ANAPC8. 1 hit.
PF13414. TPR_11. 1 hit.
PF13181. TPR_8. 4 hits.
[Graphical view]
SMARTiSM00028. TPR. 6 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 5 hits.
PROSITEiPS50005. TPR. 6 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCDC23_YEAST
AccessioniPrimary (citable) accession number: P16522
Secondary accession number(s): D3DLB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: November 2, 2016
This is version 174 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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.