CDC23_YEAST
ID CDC23_YEAST Reviewed; 626 AA.
AC P16522; D3DLB5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Anaphase-promoting complex subunit CDC23;
DE AltName: Full=Cell division control protein 23;
GN Name=CDC23; OrderedLocusNames=YHR166C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2205535; DOI=10.1016/0378-1119(90)90172-n;
RA Doi A., Doi K.;
RT "Cloning and nucleotide sequence of the CDC23 gene of Saccharomyces
RT cerevisiae.";
RL Gene 91:123-126(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DOMAINS TPR REPEATS.
RX PubMed=2404612; DOI=10.1016/0092-8674(90)90745-z;
RA Sikorski R.S., Boguski M.S., Goebl M., Hieter P.A.;
RT "A repeating amino acid motif in CDC23 defines a family of proteins and a
RT new relationship among genes required for mitosis and RNA synthesis.";
RL Cell 60:307-317(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF ALA-39; GLY-42; GLY-80; GLU-85; SER-93;
RP THR-94; ARG-103; PRO-114; SER-123; GLY-213; GLU-306; PRO-326; GLU-398;
RP ALA-404; HIS-439; GLY-472; LEU-485 AND VAL-573.
RX PubMed=8423787; DOI=10.1128/mcb.13.2.1212-1221.1993;
RA Sikorski R.S., Michaud W.A., Hieter P.A.;
RT "p62cdc23 of Saccharomyces cerevisiae: a nuclear tetratricopeptide repeat
RT protein with two mutable domains.";
RL Mol. Cell. Biol. 13:1212-1221(1993).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=7925276; DOI=10.1002/j.1460-2075.1994.tb06752.x;
RA Lamb J.R., Michaud W.A., Sikorski R.S., Hieter P.A.;
RT "Cdc16p, Cdc23p and Cdc27p form a complex essential for mitosis.";
RL EMBO J. 13:4321-4328(1994).
RN [7]
RP FUNCTION, AND PHOSPHORYLATION AT SER-59.
RX PubMed=10871279; DOI=10.1083/jcb.149.7.1377;
RA Rudner A.D., Murray A.W.;
RT "Phosphorylation by Cdc28 activates the Cdc20-dependent activity of the
RT anaphase-promoting complex.";
RL J. Cell Biol. 149:1377-1390(2000).
RN [8]
RP FUNCTION, AND INTERACTION WITH CLB2.
RX PubMed=12413490; DOI=10.1016/s0003-9861(02)00467-8;
RA Meyn M.A. III, Melloy P.G., Li J., Holloway S.L.;
RT "The destruction box of the cyclin Clb2 binds the anaphase-promoting
RT complex/cyclosome subunit Cdc23.";
RL Arch. Biochem. Biophys. 407:189-195(2002).
RN [9]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH SWM1.
RX PubMed=12609981; DOI=10.1074/jbc.m213109200;
RA Hall M.C., Torres M.P., Schroeder G.K., Borchers C.H.;
RT "Mnd2 and Swm1 are core subunits of the Saccharomyces cerevisiae anaphase-
RT promoting complex.";
RL J. Biol. Chem. 278:16698-16705(2003).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=15280225; DOI=10.1534/genetics.103.025478;
RA Melloy P.G., Holloway S.L.;
RT "Changes in the localization of the Saccharomyces cerevisiae anaphase-
RT promoting complex upon microtubule depolymerization and spindle checkpoint
RT activation.";
RL Genetics 167:1079-1094(2004).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [12]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex
CC that controls progression through mitosis and the G1 phase of the cell
CC cycle. The APC/C is thought to confer substrate specificity and, in the
CC presence of ubiquitin-conjugating E2 enzymes, it catalyzes the
CC formation of protein-ubiquitin conjugates that are subsequently
CC degraded by the 26S proteasome. In early mitosis, the APC/C is
CC activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5,
CC and other anaphase inhibitory proteins for proteolysis, thereby
CC triggering the separation of sister chromatids at the metaphase-to-
CC anaphase transition. In late mitosis and in G1, degradation of CLB5
CC allows activation of the APC/C by CDH1, which is needed to destroy
CC CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and
CC creating the low CDK state necessary for cytokinesis and for reforming
CC prereplicative complexes in G1 prior to another round of replication.
CC {ECO:0000269|PubMed:10871279, ECO:0000269|PubMed:12413490,
CC ECO:0000269|PubMed:12609981, ECO:0000269|PubMed:7925276,
CC ECO:0000269|PubMed:8423787}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: The APC/C is composed of at least 13 subunits that stay
CC tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5,
CC APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. CDC23
CC interacts directly with SWM1 and binds the destruction box (D-box) of
CC the substrate cyclin CLB2. {ECO:0000269|PubMed:12413490,
CC ECO:0000269|PubMed:12609981, ECO:0000269|PubMed:7925276}.
CC -!- INTERACTION:
CC P16522; P40577: MND2; NbExp=3; IntAct=EBI-4216, EBI-25433;
CC P16522; Q12379: SWM1; NbExp=5; IntAct=EBI-4216, EBI-33330;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore.
CC Note=Associated with the kinetochore.
CC -!- PTM: Phosphorylated by CDC28, which is required for the early mitotic
CC activity of the APC/C in its CDC20-bound form.
CC {ECO:0000269|PubMed:10871279}.
CC -!- MISCELLANEOUS: Present with 80 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the APC8/CDC23 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D00610; BAA00485.1; -; Genomic_DNA.
DR EMBL; U00027; AAB68012.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06859.1; -; Genomic_DNA.
DR PIR; S12330; RGBY23.
DR RefSeq; NP_012036.1; NM_001179297.1.
DR AlphaFoldDB; P16522; -.
DR SMR; P16522; -.
DR BioGRID; 36600; 505.
DR ComplexPortal; CPX-756; Anaphase-Promoting core complex.
DR ComplexPortal; CPX-760; Anaphase-Promoting Complex, CDC20 variant.
DR ComplexPortal; CPX-761; Anaphase-Promoting Complex, CDH1 variant.
DR ComplexPortal; CPX-762; Anaphase-Promoting complex AMA1 variant.
DR DIP; DIP-589N; -.
DR ELM; P16522; -.
DR IntAct; P16522; 26.
DR MINT; P16522; -.
DR STRING; 4932.YHR166C; -.
DR iPTMnet; P16522; -.
DR MaxQB; P16522; -.
DR PaxDb; P16522; -.
DR PRIDE; P16522; -.
DR EnsemblFungi; YHR166C_mRNA; YHR166C; YHR166C.
DR GeneID; 856571; -.
DR KEGG; sce:YHR166C; -.
DR SGD; S000001209; CDC23.
DR VEuPathDB; FungiDB:YHR166C; -.
DR eggNOG; KOG1155; Eukaryota.
DR GeneTree; ENSGT00950000182950; -.
DR HOGENOM; CLU_018320_2_1_1; -.
DR InParanoid; P16522; -.
DR OMA; PKYLAAW; -.
DR BioCyc; YEAST:G3O-31200-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:P16522; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P16522; protein.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0030332; F:cyclin binding; IPI:SGD.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:SGD.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:SGD.
DR GO; GO:0051445; P:regulation of meiotic cell cycle; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR007192; APC8.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF04049; ANAPC8; 1.
DR Pfam; PF13181; TPR_8; 4.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Kinetochore; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; TPR repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..626
FT /note="Anaphase-promoting complex subunit CDC23"
FT /id="PRO_0000106272"
FT REPEAT 215..248
FT /note="TPR 1"
FT REPEAT 295..328
FT /note="TPR 2"
FT REPEAT 329..362
FT /note="TPR 3"
FT REPEAT 363..396
FT /note="TPR 4"
FT REPEAT 397..430
FT /note="TPR 5"
FT REPEAT 431..464
FT /note="TPR 6"
FT REPEAT 465..498
FT /note="TPR 7"
FT REPEAT 499..532
FT /note="TPR 8"
FT REPEAT 536..569
FT /note="TPR 9"
FT MOD_RES 59
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:10871279,
FT ECO:0007744|PubMed:18407956"
FT MUTAGEN 39
FT /note="A->T: In CDC23-50; G2/M cell cycle arrest at 37
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 42
FT /note="G->D: In CDC23-54; G2/M cell cycle arrest at 37
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 80
FT /note="G->S: In CDC23-44; G2/M cell cycle arrest at 37
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 85
FT /note="E->K: In CDC23-51; G2/M cell cycle arrest at 37
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 93
FT /note="S->F: In CDC23-52; G2/M cell cycle arrest at 37
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 94
FT /note="T->M: In CDC23-4; G2/M cell cycle arrest at 36
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 103
FT /note="R->Q: In CDC23-40; G2/M cell cycle arrest at 37
FT degrees Celsius; when associated with V-573."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 114
FT /note="P->L: In CDC23-53; G2/M cell cycle arrest at 37
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 114
FT /note="P->S: In CDC23-41; G2/M cell cycle arrest at 37
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 123
FT /note="S->N: In CDC23-6; G2/M cell cycle arrest at 36
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 213
FT /note="G->D: In CDC23-47; G2/M cell cycle arrest at 37
FT degrees Celsius; when associated with W-583."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 306
FT /note="E->K: In CDC23-49; G2/M cell cycle arrest at 37
FT degrees Celsius; when associated with P-326."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 326
FT /note="P->L: In CDC23-49; G2/M cell cycle arrest at 37
FT degrees Celsius; when associated with E-306."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 398
FT /note="E->K: In CDC23-37; G2/M cell cycle arrest at 30
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 404
FT /note="A->T: In CDC23-39; G2/M cell cycle arrest at 37
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 439
FT /note="H->R: In CDC23-2; G2/M cell cycle arrest at 36
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 472
FT /note="G->D: In CDC23-1; G2/M cell cycle arrest at 36
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 485
FT /note="L->F: In CDC23-56; G2/M cell cycle arrest at 37
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 573
FT /note="V->I: In CDC23-40; G2/M cell cycle arrest at 37
FT degrees Celsius; when associated with R-103."
FT /evidence="ECO:0000269|PubMed:8423787"
FT MUTAGEN 583..626
FT /note="Missing: In CDC23-47; G2/M cell cycle arrest at 37
FT degrees Celsius; when associated with G-213."
SQ SEQUENCE 626 AA; 73114 MW; 3C96FE2BC8097118 CRC64;
MNDDSQDKII HDIRIQLRKA ATELSRWKLY GSSKWAAEAL AGLAEAIDVD QTHSLADESP
LRNKQGVPKQ MFEIPQNGFG LSETEYDLYL LGSTLFDAKE FDRCVFFLKD VTNPYLKFLK
LYSKFLSWDK KSQESMENIL TTGKFTDEMY RANKDGDGSG NEDINQSGHQ RANLKMVSNE
HESQSNISSI LKEINTFLES YEIKIDDDEA DLGLALLYYL RGVILKQEKN ISKAMSSFLK
SLSCYSFNWS CWLELMDCLQ KVDDALLLNN YLYQNFQFKF SENLGSQRTI EFNIMIKFFK
LKVFEELNGQ LEDYFEDLEF LLQVFPNFTF LKAYNATISY NNLDYVTAES RFDDIVKQDP
YRLNDLETYS NILYVMQKNS KLAYLAQFVS QIDRFRPETC CIIANYYSAR QEHEKSIMYF
RRALTLDKKT TNAWTLMGHE FVELSNSHAA IECYRRAVDI CPRDFKAWFG LGQAYALLDM
HLYSLYYFQK ACTLKPWDRR IWQVLGECYS KTGNKVEAIK CYKRSIKASQ TVDQNTSIYY
RLAQLYEELE DLQECKKFMM KCVDVEELLE GIVTDETVKA RLWLAIFEIK AGNYQLAYDY
AMGVSSGTSQ EIEEARMLAR ECRRHM
