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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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391A → T in CDC23-50; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication
Mutagenesisi42 – 421G → D in CDC23-54; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication
Mutagenesisi80 – 801G → S in CDC23-44; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication
Mutagenesisi85 – 851E → K in CDC23-51; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication
Mutagenesisi93 – 931S → F in CDC23-52; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication
Mutagenesisi94 – 941T → M in CDC23-4; G2/M cell cycle arrest at 36 degrees Celsius. 1 Publication
Mutagenesisi103 – 1031R → Q in CDC23-40; G2/M cell cycle arrest at 37 degrees Celsius; when associated with V-573. 1 Publication
Mutagenesisi114 – 1141P → L in CDC23-53; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication
Mutagenesisi114 – 1141P → S in CDC23-41; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication
Mutagenesisi123 – 1231S → N in CDC23-6; G2/M cell cycle arrest at 36 degrees Celsius. 1 Publication
Mutagenesisi213 – 2131G → D in CDC23-47; G2/M cell cycle arrest at 37 degrees Celsius; when associated with W-583. 1 Publication
Mutagenesisi306 – 3061E → K in CDC23-49; G2/M cell cycle arrest at 37 degrees Celsius; when associated with P-326. 1 Publication
Mutagenesisi326 – 3261P → L in CDC23-49; G2/M cell cycle arrest at 37 degrees Celsius; when associated with E-306. 1 Publication
Mutagenesisi398 – 3981E → K in CDC23-37; G2/M cell cycle arrest at 30 degrees Celsius. 1 Publication
Mutagenesisi404 – 4041A → T in CDC23-39; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication
Mutagenesisi439 – 4391H → R in CDC23-2; G2/M cell cycle arrest at 36 degrees Celsius. 1 Publication
Mutagenesisi472 – 4721G → D in CDC23-1; G2/M cell cycle arrest at 36 degrees Celsius. 1 Publication
Mutagenesisi485 – 4851L → F in CDC23-56; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication
Mutagenesisi573 – 5731V → I in CDC23-40; G2/M cell cycle arrest at 37 degrees Celsius; when associated with R-103. 1 Publication
Mutagenesisi583 – 62644Missing in CDC23-47; G2/M cell cycle arrest at 37 degrees Celsius; when associated with G-213. Add
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 626626Anaphase-promoting complex subunit CDC23PRO_0000106272Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591Phosphoserine; by CDC28Combined sources1 Publication

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.
PeptideAtlasiP16522.
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 interactions.
DIPiDIP-589N.
IntActiP16522. 21 interactions.
MINTiMINT-498933.

Structurei

3D structure databases

ProteinModelPortaliP16522.
SMRiP16522. Positions 10-563.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati215 – 24834TPR 1Add
BLAST
Repeati295 – 32834TPR 2Add
BLAST
Repeati329 – 36234TPR 3Add
BLAST
Repeati363 – 39634TPR 4Add
BLAST
Repeati397 – 43034TPR 5Add
BLAST
Repeati431 – 46434TPR 6Add
BLAST
Repeati465 – 49834TPR 7Add
BLAST
Repeati499 – 53234TPR 8Add
BLAST
Repeati536 – 56934TPR 9Add
BLAST

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.
OMAiSHAAIEC.
OrthoDBiEOG7KDFKN.

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. Positions 10-563.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP16522.

Proteomic databases

MaxQBiP16522.
PeptideAtlasiP16522.
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.
OMAiSHAAIEC.
OrthoDBiEOG7KDFKN.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciYEAST:G3O-31200-MONOMER.

Miscellaneous databases

NextBioi982417.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and nucleotide sequence of the CDC23 gene of Saccharomyces cerevisiae."
    Doi A., Doi K.
    Gene 91:123-126(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis."
    Sikorski R.S., Boguski M.S., Goebl M., Hieter P.A.
    Cell 60:307-317(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAINS TPR REPEATS.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "p62cdc23 of Saccharomyces cerevisiae: a nuclear tetratricopeptide repeat protein with two mutable domains."
    Sikorski R.S., Michaud W.A., Hieter P.A.
    Mol. Cell. Biol. 13:1212-1221(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ALA-39; GLY-42; GLY-80; GLU-85; SER-93; THR-94; ARG-103; PRO-114; SER-123; GLY-213; GLU-306; PRO-326; GLU-398; ALA-404; HIS-439; GLY-472; LEU-485 AND VAL-573.
  6. "Cdc16p, Cdc23p and Cdc27p form a complex essential for mitosis."
    Lamb J.R., Michaud W.A., Sikorski R.S., Hieter P.A.
    EMBO J. 13:4321-4328(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  7. "Phosphorylation by Cdc28 activates the Cdc20-dependent activity of the anaphase-promoting complex."
    Rudner A.D., Murray A.W.
    J. Cell Biol. 149:1377-1390(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-59.
  8. "The destruction box of the cyclin Clb2 binds the anaphase-promoting complex/cyclosome subunit Cdc23."
    Meyn M.A. III, Melloy P.G., Li J., Holloway S.L.
    Arch. Biochem. Biophys. 407:189-195(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CLB2.
  9. "Mnd2 and Swm1 are core subunits of the Saccharomyces cerevisiae anaphase-promoting complex."
    Hall M.C., Torres M.P., Schroeder G.K., Borchers C.H.
    J. Biol. Chem. 278:16698-16705(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH SWM1.
  10. "Changes in the localization of the Saccharomyces cerevisiae anaphase-promoting complex upon microtubule depolymerization and spindle checkpoint activation."
    Melloy P.G., Holloway S.L.
    Genetics 167:1079-1094(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: May 11, 2016
This is version 169 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.