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UniProtKB/Swiss-Prot entry P07834


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CDC4_YEAST
Primary accession number P07834
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on November 1, 1995 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 94)
Name and origin of the protein
Protein name Cell division control protein 4
Synonyms F-box protein CDC4
E3 ubiquitin ligase complex SCF subunit CDC4
Gene name
Name: CDC4
OrderedLocusNames: YFL009W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0022-2836(87)90646-2; PubMed=3309335 [NCBI, ExPASy, EBI, Israel, Japan]
Yochem J., Byers B.;
"Structural comparison of the yeast cell division cycle gene CDC4 and a related pseudogene.";
J. Mol. Biol. 195:233-245(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
DOI=10.1038/ng0795-261; PubMed=7670463 [NCBI, ExPASy, EBI, Israel, Japan]
Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T.;
"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae.";
Nat. Genet. 10:261-268(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-579.
STRAIN=ATCC 204511 / S288c / AB972;
Barrell B.G., Churcher C., Rajandream M.A.;
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION.
PubMed=7813440 [NCBI, ExPASy, EBI, Israel, Japan]
Kornitzer D., Raboy B., Kulka R.G., Fink G.R.;
"Regulated degradation of the transcription factor Gcn4.";
EMBO J. 13:6021-6030(1994).
[5]
INTERACTION WITH SKP1/CBF3D.
STRAIN=ATCC 204508 / S288c;
DOI=10.1016/S0092-8674(00)80098-7; PubMed=8706131 [NCBI, ExPASy, EBI, Israel, Japan]
Bai C., Sen P., Hofmann K., Ma L., Goebl M., Harper J.W., Elledge S.J.;
"SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box.";
Cell 86:263-274(1996).
[6]
FUNCTION, AND SUBUNIT.
DOI=10.1016/S0092-8674(00)80403-1; PubMed=9346238 [NCBI, ExPASy, EBI, Israel, Japan]
Skowyra D., Craig K.L., Tyers M., Elledge S.J., Harper J.W.;
"F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex.";
Cell 91:209-219(1997).
[7]
FUNCTION, AND SUBUNIT.
DOI=10.1016/S0092-8674(00)80404-3; PubMed=9346239 [NCBI, ExPASy, EBI, Israel, Japan]
Feldman R.M., Correll C.C., Kaplan K.B., Deshaies R.J.;
"A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p.";
Cell 91:221-230(1997).
[8]
FUNCTION, AND INTERACTION WITH SKP1.
DOI=10.1093/emboj/16.18.5629; PubMed=9312022 [NCBI, ExPASy, EBI, Israel, Japan]
Li F.N., Johnston M.;
"Grr1 of Saccharomyces cerevisiae is connected to the ubiquitin proteolysis machinery through Skp1: coupling glucose sensing to gene expression and the cell cycle.";
EMBO J. 16:5629-5638(1997).
[9]
FUNCTION, AND INTERACTION WITH CDC6.
DOI=10.1093/emboj/16.19.5966; PubMed=9312054 [NCBI, ExPASy, EBI, Israel, Japan]
Drury L.S., Perkins G., Diffley J.F.;
"The Cdc4/34/53 pathway targets Cdc6p for proteolysis in budding yeast.";
EMBO J. 16:5966-5976(1997).
[10]
FUNCTION, AND SUBUNIT.
DOI=10.1093/emboj/17.18.5360; PubMed=9736614 [NCBI, ExPASy, EBI, Israel, Japan]
Jaquenoud M., Gulli M.P., Peter K., Peter M.;
"The Cdc42p effector Gic2p is targeted for ubiquitin-dependent degradation by the SCFGrr1 complex.";
EMBO J. 17:5360-5373(1998).
[11]
INTERACTION WITH CDC53.
PubMed=9499404 [NCBI, ExPASy, EBI, Israel, Japan]
Patton E.E., Willems A.R., Sa D., Kuras L., Thomas D., Craig K.L., Tyers M.;
"Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F-box protein complexes that regulate cell division and methionine biosynthesis in yeast.";
Genes Dev. 12:692-705(1998).
[12]
INTERACTION WITH HRT1.
PubMed=10385629 [NCBI, ExPASy, EBI, Israel, Japan]
Seol J.H., Feldman R.M.R., Zachariae W., Shevchenko A., Correll C.C., Lyapina S., Chi Y., Galova M., Claypool J., Sandmeyer S., Nasmyth K., Shevchenko A., Deshaies R.J.;
"Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme Cdc34.";
Genes Dev. 13:1614-1626(1999).
[13]
FUNCTION.
PubMed=10409741 [NCBI, ExPASy, EBI, Israel, Japan]
Goh P.Y., Surana U.;
"Cdc4, a protein required for the onset of S phase, serves an essential function during G(2)/M transition in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 19:5512-5522(1999).
[14]
FUNCTION, AND RECONSTITUTION OF THE SKF(GRR1)COMPLEX.
DOI=10.1126/science.284.5414.662; PubMed=10213692 [NCBI, ExPASy, EBI, Israel, Japan]
Skowyra D., Koepp D.M., Kamura T., Conrad M.N., Conaway R.C., Conaway J.W., Elledge S.J., Harper J.W.;
"Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1.";
Science 284:662-665(1999).
[15]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 82-LYS-ARG-83 AND LYS-85.
DOI=10.1093/emboj/19.22.6085; PubMed=11080155 [NCBI, ExPASy, EBI, Israel, Japan]
Blondel M., Galan J.M., Chi Y., Lafourcade C., Longaretti C., Deshaies R.J., Peter M.;
"Nuclear-specific degradation of Far1 is controlled by the localization of the F-box protein Cdc4.";
EMBO J. 19:6085-6097(2000).
[16]
INTERACTION WITH CIC1.
DOI=10.1093/emboj/20.16.4423; PubMed=11500370 [NCBI, ExPASy, EBI, Israel, Japan]
Jaeger S., Strayle J., Heinemeyer W., Wolf D.H.;
"Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4.";
EMBO J. 20:4423-4431(2001).
[17]
INTERACTION WITH SKP1, AND RECONSTITUTION OF THE SCF(CDC4) COMPLEX.
DOI=10.1002/prot.10620; PubMed=14747994 [NCBI, ExPASy, EBI, Israel, Japan]
Kus B.M., Caldon C.E., Andorn-Broza R., Edwards A.M.;
"Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro.";
Proteins 54:455-467(2004).
[18]
HOMODIMERIZATION, AND INTERACTION WITH SIC1.
DOI=10.1016/j.molcel.2007.02.022; PubMed=17434132 [NCBI, ExPASy, EBI, Israel, Japan]
Hao B., Oehlmann S., Sowa M.E., Harper J.W., Pavletich N.P.;
"Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases.";
Mol. Cell 26:131-143(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-31, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
  • FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and binds to phosphorylated target proteins. Directs ubiquitination of the phosphorylated CDK inhibitor SIC1. Involved in the degradation of CDC6 together with CDC34/UBC3 and CDC53, and in restricting the degradation of FAR1 to the nucleus. Is essential for initiation of DNA replication and separation of the spindle pole bodies to form the poles of the mitotic spindle. It also plays a role in bud development, fusion of zygotic nuclei after conjugation and various aspects of sporulation. Required for HTA1-HTB1 locus transcription activation. Required for G1/S and G2/M transition.
  • PATHWAY: Protein modification; protein ubiquitination.
  • SUBUNIT: Interacts with DCD53 and SKP1. Component of the SCF(CDC4) complex containing CDC53, SKP1, RBX1 and CDC4. CDC34. Interacts with CDC6 and CIC1. Interacts with SIC1; the interaction involves a SIC1 double phosphorylated motif (degron). Homodimerizes; the dimerization increases SIC1 ubiquitination in vitro.
  • INTERACTION:
    Q12018:CDC53; NbExp=2; IntAct=EBI-4434, EBI-4321;
    P38779:CIC1; NbExp=1; IntAct=EBI-4434, EBI-24538;
    P52286:SKP1; NbExp=3; IntAct=EBI-4434, EBI-4090;
  • SUBCELLULAR LOCATION: Nucleus.
  • SIMILARITY: Contains 1 F-box domain.
  • SIMILARITY: Contains 7 WD repeats.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X05625; CAA29113.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D50617; BAA09229.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z46255; CAA86341.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S56245; S56245.
RefSeq NP_116585.1; -.
3D structure databases
PDB
1NEX; X-ray; 2.70 A; B/D=263-744.[ExPASy / RCSB / EBI]
2P63; X-ray; 2.67 A; A/B/C/D=222-273.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1NEX; -.
2P63; -.
ModBase P07834.
Protein-protein interaction databases
DIP DIP:1625N; -.
IntAct P07834; -.
Organism-specific databases
CYGD YFL009w; -.
SGD S000001885; CDC4.
Yeast-GFP YFL009W.
Gene expression databases
ArrayExpress P07834; -.
GermOnline YFL009W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0016363; Cellular component: nuclear matrix (inferred from direct assay from SGD).
GO:0043224; Cellular component: nuclear SCF ubiquitin ligase complex (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0000082; Biological process: G1/S transition of mitotic cell cycle (inferred from mutant phenotype from SGD).
GO:0000086; Biological process: G2/M transition of mitotic cell cycle (inferred from genetic interaction from SGD).
GO:0007126; Biological process: meiosis (inferred from mutant phenotype from SGD).
GO:0042787; Biological process: protein ubiquitination during ubiquitin-dependent protein catabolic process (inferred from direct assay from SGD).
GO:0031146; Biological process: SCF-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR001810; F-box.
IPR015943; WD40/YVTN_repeat-like.
IPR001680; WD40_repeat.
Graphical view of domain structure.
Gene3D G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
Pfam PF00646; F-box; 1.
PF00400; WD40; 6.
Pfam graphical view of domain structure.
PRINTS PR00320; GPROTEINBRPT.
ProDom PD000018; WD40; 2.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00256; FBOX; 1.
SM00320; WD40; 7.
SMART graphical view of domain structure.
PROSITE PS50181; FBOX; 1.
PS00678; WD_REPEATS_1; 4.
PS50082; WD_REPEATS_2; 5.
PS50294; WD_REPEATS_REGION; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P07834.
Genome annotation databases
Ensembl YFL009W; Saccharomyces cerevisiae. [Contig view]
GeneID 850539; -.
GenomeReviews D50617_GR; YFL009W.
KEGG sce:YFL009W; -.
NMPDR fig|4932.3.peg.2277; -.
Phylogenomic databases
HOGENOM P07834; -.
Other
LinkHub P07834; -.
ProtoNet P07834.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell cycle; Cell division; Complete proteome; Mitosis; Nucleus; Phosphoprotein; Repeat; Sporulation; Ubl conjugation pathway; WD repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   779  779     Cell division control protein 4. PRO_0000050899
DOMAIN   272   319  48     F-box. 
REPEAT   380   408  29     WD 1. 
REPEAT   420   449  30     WD 2. 
REPEAT   461   493  33     WD 3. 
REPEAT   528   556  29     WD 4. 
REPEAT   568   598  31     WD 5. 
REPEAT   630   658  29     WD 6. 
REPEAT   669   698  30     WD 7. 
MOTIF   82    85  4     Nuclear localization signal. 
MOD_RES   3     3        Phosphoserine. 
MOD_RES   31    31        Phosphoserine. 
MUTAGEN   82    82        K->A: Prevents nuclear localization; when associated with A-83 and A-85. 
MUTAGEN   83    83        R->A: Prevents nuclear localization; when associated with A-82 and A-85. 
MUTAGEN   83    83        R->G: Prevents nuclear localization. 
MUTAGEN   85    85        K->A: Prevents nuclear localization; when associated with A-82 and A-83. 
CONFLICT   460   460        K -> E (in Ref. 1; CAA29113). 
HELIX   228   234  7      
HELIX   235   237  3      
HELIX   242   253  12      
HELIX   274   277  4      
HELIX   280   287  8      
HELIX   292   298  7      
TURN   299   301  3      
HELIX   303   310  8      
HELIX   314   322  9      
TURN   328   330  3      
HELIX   331   341  11      
HELIX   347   366  20      
STRAND   373   378  6      
STRAND   381   383  3      
STRAND   385   391  7      
STRAND   394   399  6      
STRAND   402   408  7      
TURN   409   412  4      
STRAND   413   419  7      
STRAND   425   431  7      
TURN   432   434  3      
STRAND   435   440  6      
STRAND   445   449  5      
TURN   450   453  4      
STRAND   454   459  6      
STRAND   466   474  9      
STRAND   477   484  8      
STRAND   487   493  7      
STRAND   511   514  4      
TURN   516   518  3      
STRAND   522   527  6      
STRAND   533   539  7      
STRAND   542   547  6      
STRAND   552   556  5      
TURN   557   560  4      
STRAND   561   566  6      
STRAND   573   579  7      
TURN   580   583  4      
STRAND   584   589  6      
STRAND   594   598  5      
TURN   599   601  3      
STRAND   624   628  5      
STRAND   637   640  4      
STRAND   642   648  7      
STRAND   652   658  7      
TURN   659   661  3      
STRAND   664   669  6      
STRAND   678   681  4      
STRAND   683   690  8      
STRAND   693   698  6      
TURN   699   701  3      
TURN   709   712  4      
STRAND   714   722  9      
STRAND   725   734  10      
STRAND   736   742  7      
Sequence information
Length: 779 AA [This is the length of the unprocessed precursor] Molecular weight: 86090 Da [This is the MW of the unprocessed precursor] CRC64: 0348F2F8FA78F3BC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGSFPLAEFP LRDIPVPYSY RVSGGIASSG SVTALVTAAG THRNSSTAKT VETEDGEEDI 

        70         80         90        100        110        120 
DEYQRKRAAG SGESTPERSD FKRVKHDNHK TLHPVNLQNT GAASVDNDGL HNLTDISNDA 

       130        140        150        160        170        180 
EKLLMSVDDG SAAPSTLSVN MGVASHNVAA PTTVNAATIT GSDVSNNVNS ATINNPMEEG 

       190        200        210        220        230        240 
ALPLSPTASS PGTTTPLAKT TKTINNNNNI ADLIESKDSI ISPEYLSDEI FSAINNNLPH 

       250        260        270        280        290        300 
AYFKNLLFRL VANMDRSELS DLGTLIKDNL KRDLITSLPF EISLKIFNYL QFEDIINSLG 

       310        320        330        340        350        360 
VSQNWNKIIR KSTSLWKKLL ISENFVSPKG FNSLNLKLSQ KYPKLSQQDR LRLSFLENIF 

       370        380        390        400        410        420 
ILKNWYNPKF VPQRTTLRGH MTSVITCLQF EDNYVITGAD DKMIRVYDSI NKKFLLQLSG 

       430        440        450        460        470        480 
HDGGVWALKY AHGGILVSGS TDRTVRVWDI KKGCCTHVFK GHNSTVRCLD IVEYKNIKYI 

       490        500        510        520        530        540 
VTGSRDNTLH VWKLPKESSV PDHGEEHDYP LVFHTPEENP YFVGVLRGHM ASVRTVSGHG 

       550        560        570        580        590        600 
NIVVSGSYDN TLIVWDVAQM KCLYILSGHT DRIYSTIYDH ERKRCISASM DTTIRIWDLE 

       610        620        630        640        650        660 
NIWNNGECSY ATNSASPCAK ILGAMYTLQG HTALVGLLRL SDKFLVSAAA DGSIRGWDAN 

       670        680        690        700        710        720 
DYSRKFSYHH TNLSAITTFY VSDNILVSGS ENQFNIYNLR SGKLVHANIL KDADQIWSVN 

       730        740        750        760        770 
FKGKTLVAAV EKDGQSFLEI LDFSKASKIN YVSNPVNSSS SSLESISTSL GLTRTTIIP 

P07834 in FASTA format

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