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Reviewed, UniProtKB/Swiss-Prot Q12018 (CDC53_YEAST)

Last modified November 25, 2008. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cell division control protein 53
Alternative name(s):
    Cullin-A
    E3 ubiquitin ligase complex SCF subunit CDC53
Gene names
Name: CDC53
Ordered Locus Names: YDL132W
ORF Names: D2190
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length815 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The SCF complex associates with CDC34 as the E2 ubiquitin-conjugating enzyme. The functional specificity of the SCF complex depends on the type of F-box protein. SCF(CDC4) controls the G1-to-S phase transition; it directs ubiquitination of the phosphorylated CDK inhibitor SIC1 and of CDC6. SCF(CDC4) directs ubiquitination of GCN4. SCF(GRR1) directs ubiquitination of phosphorylated CLN1, CLN2 and GIC2. SCF(MET30) directs ubiquitination of MET4. SCF(DIA2) is specifically involved in the pheromone induced degradation of phosphorylated TEC1. SCF(MDM30) seems to direct ubiquitination of FZ01. Involved in the regulation of methionine biosynthesis genes.

Subunit structure

Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes formed of CUL1, SKP1/HRT1, RBX1 and a variable F-box domain-containing protein as substrate-specific adapter. Component of the SCF(CDC4) complex containing CDC4. Component of the SCF(MET30) complex containing MET30. Component of the SCF(GRR1) complex containig GRR1. Component of the probable SCF(DIA2) complex containing DIA2. Component of the probable SCF(YDR131C) complex containing YDR131C. Component of the probable SCF(YDR306C) complex containing YDR306C. Component of the probable SCF(YLR224W) complex containing YLR224W. Component of the probable SCF(YJL149W) complex containing YJL149W. Component of the probable SCF(YNL311C) complex containing YNL311C. Component of the probable SCF(MDM30) complex containing MDM30. Component of the probable SCF(UFO1) complex containing UFO1. Component of the probable SCF(HRT3) complex containing HRT3. Component of the probable SCF(YBR280C) complex containing YBR280C. Component of the probable SCF(YBR352W) complex containing YBR352W. Interacts with DCN1, YBR280C, YLR224W and YLR352W.

Subcellular location

Cytoplasm. Nucleus.

Miscellaneous

Present with 377 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the cullin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 815815Cell division control protein 53
PRO_0000119805

Regions

Region9 – 280272Required for interaction with SKP1/CBF3D and F-box protein
Region448 – 748301Required for interaction with CDC34/UBC3

Amino acid modifications

Cross-link760Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) By similarity

Experimental info

Mutagenesis4881R → C: Prevents CDC34/UBC3 interaction

Sequences

Sequence LengthMass (Da)Tools
Q12018-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 22BC8B35034EDDEF

FASTA81593,944
        10         20         30         40         50         60 
MSETLPRSDD LEATWNFIEP GINQILGNEK NQASTSKRVY KILSPTMYME VYTAIYNYCV 

        70         80         90        100        110        120 
NKSRSSGHFS TDSRTGQSTI LVGSEIYEKL KNYLKNYILN FKQSNSETFL QFYVKRWKRF 

       130        140        150        160        170        180 
TIGAIFLNHA FDYMNRYWVQ KERSDGKRHI FDVNTLCLMT WKEVMFDPSK DVLINELLDQ 

       190        200        210        220        230        240 
VTLGREGQII QRSNISTAIK SLVALGIDPQ DLKKLNLNVY IQVFEKPFLK KTQEYYTQYT 

       250        260        270        280        290        300 
NDYLEKHSVT EYIFEAHEII KREEKAMTIY WDDHTKKPLS MALNKVLITD HIEKLENEFV 

       310        320        330        340        350        360 
VLLDARDIEK ITSLYALIRR DFTLIPRMAS VFENYVKKTG ENEISSLLAM HKHNIMKNEN 

       370        380        390        400        410        420 
ANPKKLALMT AHSLSPKDYI KKLLEVHDIF SKIFNESFPD DIPLAKALDN ACGAFININE 

       430        440        450        460        470        480 
FALPAGSPKS ATSKTSEMLA KYSDILLKKA TKPEVASDMS DEDIITIFKY LTDKDAFETH 

       490        500        510        520        530        540 
YRRLFAKRLI HGTSTSAEDE ENIIQRLQAA NSMEYTGKIT KMFQDIRLSK ILEDDFAVAL 

       550        560        570        580        590        600 
KNEPDYSKAK YPDLQPFVLA ENMWPFSYQE VEFKLPKELV PSHEKLKESY SQKHNGRILK 

       610        620        630        640        650        660 
WLWPLCRGEL KADIGKPGRM PFNFTVTLFQ MAILLLYNDA DVLTLENIQE GTSLTIQHIA 

       670        680        690        700        710        720 
AAMVPFIKFK LIQQVPPGLD ALVKPETQFK LSRPYKALKT NINFASGVKN DILQSLSGGG 

       730        740        750        760        770        780 
HDNHGNKLGN KRLTEDERIE KELNTERQIF LEACIVRIMK AKRNLPHTTL VNECIAQSHQ 

       790        800        810 
RFNAKVSMVK RAIDSLIQKG YLQRGDDGES YAYLA 

« Hide

References

« Hide 'large scale' references
[1]"Cdc53p acts in concert with Cdc4p and Cdc34p to control the G1-to-S-phase transition and identifies a conserved family of proteins."
Mathias N., Johnson S.L., Winey M., Adams A.E., Goetsch L., Pringle J.R., Byers B., Goebl M.G.
Mol. Cell. Biol. 16:6634-6643(1996) [PubMed: 8943317] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of a 26,756 bp segment from the left arm of yeast chromosome IV."
Woelfl S., Haneman V., Saluz H.P.
Yeast 12:1549-1554(1996) [PubMed: 8972577] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[4]"Regulated degradation of the transcription factor Gcn4."
Kornitzer D., Raboy B., Kulka R.G., Fink G.R.
EMBO J. 13:6021-6030(1994) [PubMed: 7813440] [Abstract]
Cited for: FUNCTION.
[5]"F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex."
Skowyra D., Craig K.L., Tyers M., Elledge S.J., Harper J.W.
Cell 91:209-219(1997) [PubMed: 9346238] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[6]"A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p."
Feldman R.M., Correll C.C., Kaplan K.B., Deshaies R.J.
Cell 91:221-230(1997) [PubMed: 9346239] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[7]"The Cdc4/34/53 pathway targets Cdc6p for proteolysis in budding yeast."
Drury L.S., Perkins G., Diffley J.F.
EMBO J. 16:5966-5976(1997) [PubMed: 9312054] [Abstract]
Cited for: FUNCTION.
[8]"The Cdc42p effector Gic2p is targeted for ubiquitin-dependent degradation by the SCFGrr1 complex."
Jaquenoud M., Gulli M.P., Peter K., Peter M.
EMBO J. 17:5360-5373(1998) [PubMed: 9736614] [Abstract]
Cited for: FUNCTION.
[9]"Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F-box protein complexes that regulate cell division and methionine biosynthesis in yeast."
Patton E.E., Willems A.R., Sa D., Kuras L., Thomas D., Craig K.L., Tyers M.
Genes Dev. 12:692-705(1998) [PubMed: 9499404] [Abstract]
Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF ARG-488.
[10]"Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme Cdc34."
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.
Genes Dev. 13:1614-1626(1999) [PubMed: 10385629] [Abstract]
Cited for: INTERACTION WITH HRT1.
[11]"Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1."
Skowyra D., Koepp D.M., Kamura T., Conrad M.N., Conaway R.C., Conaway J.W., Elledge S.J., Harper J.W.
Science 284:662-665(1999) [PubMed: 10213692] [Abstract]
Cited for: FUNCTION, RECONSTITUTION OF THE SKF(GRR1)COMPLEX.
[12]"Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly."
Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.
Nat. Cell Biol. 3:384-391(2001) [PubMed: 11283612] [Abstract]
Cited for: INTERACTION WITH DCN1; YBR280C; YLR224W AND YLR352W.
[13]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[14]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[15]"Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro."
Kus B.M., Caldon C.E., Andorn-Broza R., Edwards A.M.
Proteins 54:455-467(2004) [PubMed: 14747994] [Abstract]
Cited for: RECONSTITUTION OF THE SCF(DIA2) COMPLEX, RECONSTITUTION OF THE SCF(YDR131C) COMPLEX, RECONSTITUTION OF THE SCF(YDR306C) COMPLEX, RECONSTITUTION OF THE SCF(YLR224W) COMPLEX, RECONSTITUTION OF THE SCF(YJL149W) COMPLEX, RECONSTITUTION OF THE SCF(YNL311C) COMPLEX, RECONSTITUTION OF THE SCF(MDM30) COMPLEX, RECONSTITUTION OF THE SCF(CDC4) COMPLEX, RECONSTITUTION OF THE SCF(UFO1) COMPLEX, RECONSTITUTION OF THE SCF(GRR1) COMPLEX, RECONSTITUTION OF THE SCF(HRT3) COMPLEX.
[16]"The F-box protein Dia2 regulates DNA replication."
Koepp D.M., Kile A.C., Swaminathan S., Rodriguez-Rivera V.
Mol. Biol. Cell 17:1540-1548(2006) [PubMed: 16421250] [Abstract]
Cited for: IDENTIFICATION IN THE SCF(DIA2) COMPLEX, FUNCTION OF THE SCF(DIA2) COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

U43564 Genomic DNA. Translation: AAB38821.1.
X96876 Genomic DNA. Translation: CAA65628.1.
Z74180 Genomic DNA. Translation: CAA98702.1.
PIRS67675.
RefSeqNP_010150.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:1234N.
IntActQ12018.

Proteomic databases

PeptideAtlasQ12018.

Genome annotation databases

EnsemblYDL132W. Saccharomyces cerevisiae. [Contig view]
GeneID851424.
GenomeReviewsGene locus YDL132W in contig Z71256_GR.
KEGGsce:YDL132W.
NMPDRfig|4932.3.peg.887.

Organism-specific databases

CYGDYDL132w.
SGDS000002290. CDC53.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMQ12018.

Gene expression databases

ArrayExpressQ12018.
GermOnlineYDL132W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR011991. Wing_hlx_DNA_bd.
[Graphical view]
Gene3DG3DSA:1.10.10.10. Wing_hlx_DNA_bd. 2 hits.
PfamPF00888. Cullin. 1 hit.
[Graphical view]
SMARTSM00182. CULLIN. 1 hit.
[Graphical view]
PROSITEPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubQ12018.
NextBio968633.

Entry information

Entry nameCDC53_YEAST
AccessionPrimary (citable) accession number: Q12018
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 25, 2008
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents