CD123_YEAST
ID CD123_YEAST Reviewed; 360 AA.
AC Q05791; D6VYL6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Cell division cycle protein 123;
GN Name=CDC123; OrderedLocusNames=YLR215C;
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], FUNCTION, INTERACTION WITH DMA1; DMA2
RP AND GCD11, AND MUTAGENESIS OF THR-274.
RX PubMed=15319434; DOI=10.1074/jbc.m406151200;
RA Bieganowski P., Shilinski K., Tsichlis P.N., Brenner C.;
RT "Cdc123 and checkpoint forkhead associated with RING proteins control the
RT cell cycle by controlling eIF2gamma abundance.";
RL J. Biol. Chem. 279:44656-44666(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Regulates the cell cycle in a nutrient dependent manner.
CC Accumulates in presence of nutrients and directs the destabilization of
CC DMA1 and DMA2, whose accumulation results in a G1 block. Regulates also
CC the abundance of GCD11 an essential component of the translational
CC initiation factor 2. {ECO:0000269|PubMed:15319434}.
CC -!- SUBUNIT: Interacts with DMA1, DMA2 and GCD11.
CC {ECO:0000269|PubMed:15319434}.
CC -!- INTERACTION:
CC Q05791; P32481: GCD11; NbExp=9; IntAct=EBI-34676, EBI-8924;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 4850 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CDC123 family. {ECO:0000305}.
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DR EMBL; BK005577; DAA05592.1; -; Genomic_DNA.
DR EMBL; U14913; AAB67444.1; -; Genomic_DNA.
DR EMBL; AY557956; AAS56282.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09532.1; -; Genomic_DNA.
DR PIR; S48566; S48566.
DR RefSeq; NP_013316.1; NM_001182102.1.
DR AlphaFoldDB; Q05791; -.
DR SMR; Q05791; -.
DR BioGRID; 31483; 194.
DR DIP; DIP-1886N; -.
DR IntAct; Q05791; 6.
DR MINT; Q05791; -.
DR STRING; 4932.YLR215C; -.
DR iPTMnet; Q05791; -.
DR MaxQB; Q05791; -.
DR PaxDb; Q05791; -.
DR PRIDE; Q05791; -.
DR EnsemblFungi; YLR215C_mRNA; YLR215C; YLR215C.
DR GeneID; 850912; -.
DR KEGG; sce:YLR215C; -.
DR SGD; S000004205; CDC123.
DR VEuPathDB; FungiDB:YLR215C; -.
DR eggNOG; KOG2983; Eukaryota.
DR GeneTree; ENSGT00390000003057; -.
DR HOGENOM; CLU_034402_2_0_1; -.
DR InParanoid; Q05791; -.
DR OMA; RDLNHFD; -.
DR BioCyc; YEAST:G3O-32331-MON; -.
DR PRO; PR:Q05791; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q05791; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; ISS:SGD.
DR GO; GO:0000287; F:magnesium ion binding; ISS:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1905143; P:eukaryotic translation initiation factor 2 complex assembly; IMP:SGD.
DR GO; GO:0045948; P:positive regulation of translational initiation; IMP:SGD.
DR InterPro; IPR009772; CDC123.
DR PANTHER; PTHR15323; PTHR15323; 1.
DR Pfam; PF07065; D123; 1.
DR PIRSF; PIRSF007807; Cdc123; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Reference proteome.
FT CHAIN 1..360
FT /note="Cell division cycle protein 123"
FT /id="PRO_0000227684"
FT MUTAGEN 274
FT /note="T->A: Reduces the interaction with DMA1."
FT /evidence="ECO:0000269|PubMed:15319434"
SQ SEQUENCE 360 AA; 41852 MW; 61CCC9DCEAFA1197 CRC64;
MSSQEYTTFI DIPVTRAQVE HCSYSFWSSL YPKYVPKSIV LKSLPKKFIQ YLEQDGIKLP
QEENSRSVYT EEIIRNEDND YSDWEDDEDT ATEFVQEVEP LIDFPELHQK LKDALNELGA
VAPKLNWSAP RDATWILPNN TMKCNEVNEL YLLLNASNYI MHDLQRAFKG CVDGDDIKGL
KFDLVLRQWC DMNPALEFRV FVKNAHIVGA TQRDLNYYDY LDELSDTFKD LIDEIVHDVV
LPKFPDKSFV LDVYIPRPFN KIFIVDINPF ARKTDSLLFS WNEIAAIAPP KNDVEDYELR
LVTRHNTGRF ASKEHSENHV PQDLVEASLN PEAIRELTQK WKELLSQQAK EESSDSENET
