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Database: UniProt
Entry: CDC53_YEAST
LinkDB: CDC53_YEAST
Original site: CDC53_YEAST 
ID   CDC53_YEAST             Reviewed;         815 AA.
AC   Q12018; D6VRL7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Cell division control protein 53;
DE   AltName: Full=Cullin-A;
DE   AltName: Full=E3 ubiquitin ligase complex SCF subunit CDC53;
GN   Name=CDC53; OrderedLocusNames=YDL132W; ORFNames=D2190;
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=8943317; DOI=10.1128/mcb.16.12.6634;
RA   Mathias N., Johnson S.L., Winey M., Adams A.E., Goetsch L., Pringle J.R.,
RA   Byers B., Goebl M.G.;
RT   "Cdc53p acts in concert with Cdc4p and Cdc34p to control the G1-to-S-phase
RT   transition and identifies a conserved family of proteins.";
RL   Mol. Cell. Biol. 16:6634-6643(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8972577;
RX   DOI=10.1002/(sici)1097-0061(199612)12:15<1549::aid-yea42>3.0.co;2-s;
RA   Woelfl S., Haneman V., Saluz H.P.;
RT   "Analysis of a 26,756 bp segment from the left arm of yeast chromosome
RT   IV.";
RL   Yeast 12:1549-1554(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
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.
RX   PubMed=7813440; DOI=10.1002/j.1460-2075.1994.tb06948.x;
RA   Kornitzer D., Raboy B., Kulka R.G., Fink G.R.;
RT   "Regulated degradation of the transcription factor Gcn4.";
RL   EMBO J. 13:6021-6030(1994).
RN   [6]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=9346238; DOI=10.1016/s0092-8674(00)80403-1;
RA   Skowyra D., Craig K.L., Tyers M., Elledge S.J., Harper J.W.;
RT   "F-box proteins are receptors that recruit phosphorylated substrates to the
RT   SCF ubiquitin-ligase complex.";
RL   Cell 91:209-219(1997).
RN   [7]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=9346239; DOI=10.1016/s0092-8674(00)80404-3;
RA   Feldman R.M., Correll C.C., Kaplan K.B., Deshaies R.J.;
RT   "A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of
RT   the phosphorylated CDK inhibitor Sic1p.";
RL   Cell 91:221-230(1997).
RN   [8]
RP   FUNCTION.
RX   PubMed=9312054; DOI=10.1093/emboj/16.19.5966;
RA   Drury L.S., Perkins G., Diffley J.F.;
RT   "The Cdc4/34/53 pathway targets Cdc6p for proteolysis in budding yeast.";
RL   EMBO J. 16:5966-5976(1997).
RN   [9]
RP   FUNCTION.
RX   PubMed=9736614; DOI=10.1093/emboj/17.18.5360;
RA   Jaquenoud M., Gulli M.P., Peter K., Peter M.;
RT   "The Cdc42p effector Gic2p is targeted for ubiquitin-dependent degradation
RT   by the SCFGrr1 complex.";
RL   EMBO J. 17:5360-5373(1998).
RN   [10]
RP   FUNCTION, SUBUNIT, AND MUTAGENESIS OF ARG-488.
RX   PubMed=9499404; DOI=10.1101/gad.12.5.692;
RA   Patton E.E., Willems A.R., Sa D., Kuras L., Thomas D., Craig K.L.,
RA   Tyers M.;
RT   "Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F-box protein
RT   complexes that regulate cell division and methionine biosynthesis in
RT   yeast.";
RL   Genes Dev. 12:692-705(1998).
RN   [11]
RP   INTERACTION WITH HRT1.
RX   PubMed=10385629; DOI=10.1101/gad.13.12.1614;
RA   Seol J.H., Feldman R.M.R., Zachariae W., Shevchenko A., Correll C.C.,
RA   Lyapina S., Chi Y., Galova M., Claypool J., Sandmeyer S., Nasmyth K.,
RA   Shevchenko A., Deshaies R.J.;
RT   "Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a
RT   ubiquitin ligase module that activates the E2 enzyme Cdc34.";
RL   Genes Dev. 13:1614-1626(1999).
RN   [12]
RP   FUNCTION, AND RECONSTITUTION OF THE SKF(GRR1)COMPLEX.
RX   PubMed=10213692; DOI=10.1126/science.284.5414.662;
RA   Skowyra D., Koepp D.M., Kamura T., Conrad M.N., Conaway R.C., Conaway J.W.,
RA   Elledge S.J., Harper J.W.;
RT   "Reconstitution of G1 cyclin ubiquitination with complexes containing
RT   SCFGrr1 and Rbx1.";
RL   Science 284:662-665(1999).
RN   [13]
RP   INTERACTION WITH DCN1; YBR280C; YLR224W AND YLR352W.
RX   PubMed=11283612; DOI=10.1038/35070067;
RA   Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.;
RT   "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-
RT   ATPase assembly.";
RL   Nat. Cell Biol. 3:384-391(2001).
RN   [14]
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   [15]
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   [16]
RP   RECONSTITUTION OF THE SCF(DIA2) COMPLEX, RECONSTITUTION OF THE SCF(YDR131C)
RP   COMPLEX, RECONSTITUTION OF THE SCF(YDR306C) COMPLEX, RECONSTITUTION OF THE
RP   SCF(YLR224W) COMPLEX, RECONSTITUTION OF THE SCF(YJL149W) COMPLEX,
RP   RECONSTITUTION OF THE SCF(YNL311C) COMPLEX, RECONSTITUTION OF THE
RP   SCF(MDM30) COMPLEX, RECONSTITUTION OF THE SCF(CDC4) COMPLEX, RECONSTITUTION
RP   OF THE SCF(UFO1) COMPLEX, RECONSTITUTION OF THE SCF(GRR1) COMPLEX, AND
RP   RECONSTITUTION OF THE SCF(HRT3) COMPLEX.
RX   PubMed=14747994; DOI=10.1002/prot.10620;
RA   Kus B.M., Caldon C.E., Andorn-Broza R., Edwards A.M.;
RT   "Functional interaction of 13 yeast SCF complexes with a set of yeast E2
RT   enzymes in vitro.";
RL   Proteins 54:455-467(2004).
RN   [17]
RP   IDENTIFICATION IN THE SCF(DIA2) COMPLEX, AND FUNCTION OF THE SCF(DIA2)
RP   COMPLEX.
RX   PubMed=16421250; DOI=10.1091/mbc.e05-09-0884;
RA   Koepp D.M., Kile A.C., Swaminathan S., Rodriguez-Rivera V.;
RT   "The F-box protein Dia2 regulates DNA replication.";
RL   Mol. Biol. Cell 17:1540-1548(2006).
RN   [18]
RP   INTERACTION WITH LAG2.
RX   PubMed=19763088; DOI=10.1038/emboj.2009.268;
RA   Liu Y., Mimura S., Kishi T., Kamura T.;
RT   "A longevity protein, Lag2, interacts with SCF complex and regulates SCF
RT   function.";
RL   EMBO J. 28:3366-3377(2009).
RN   [19]
RP   INTERACTION WITH LAG2.
RX   PubMed=19942853; DOI=10.1038/emboj.2009.354;
RA   Siergiejuk E., Scott D.C., Schulman B.A., Hofmann K., Kurz T., Peter M.;
RT   "Cullin neddylation and substrate-adaptors counteract SCF inhibition by the
RT   CAND1-like protein Lag2 in Saccharomyces cerevisiae.";
RL   EMBO J. 28:3845-3856(2009).
CC   -!- FUNCTION: Core component of multiple cullin-RING-based SCF (SKP1-CUL1-
CC       F-box) E3 ubiquitin-protein ligase complexes which mediate the
CC       ubiquitination and subsequent proteasomal degradation of target
CC       proteins. As a scaffold protein may contribute to catalysis through
CC       positioning of the substrate and the ubiquitin-conjugating enzyme. The
CC       SCF complex associates with CDC34 as the E2 ubiquitin-conjugating
CC       enzyme. The functional specificity of the SCF complex depends on the
CC       type of F-box protein. SCF(CDC4) controls the G1-to-S phase transition;
CC       it directs ubiquitination of the phosphorylated CDK inhibitor SIC1 and
CC       of CDC6. SCF(CDC4) directs ubiquitination of GCN4. SCF(GRR1) directs
CC       ubiquitination of phosphorylated CLN1, CLN2 and GIC2. SCF(MET30)
CC       directs ubiquitination of MET4. SCF(DIA2) is specifically involved in
CC       the pheromone induced degradation of phosphorylated TEC1. SCF(MDM30)
CC       seems to direct ubiquitination of FZ01. Involved in the regulation of
CC       methionine biosynthesis genes. {ECO:0000269|PubMed:10213692,
CC       ECO:0000269|PubMed:16421250, ECO:0000269|PubMed:7813440,
CC       ECO:0000269|PubMed:9312054, ECO:0000269|PubMed:9346238,
CC       ECO:0000269|PubMed:9346239, ECO:0000269|PubMed:9499404,
CC       ECO:0000269|PubMed:9736614}.
CC   -!- SUBUNIT: Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-
CC       protein ligase complexes formed of CUL1, SKP1/HRT1, RBX1 and a variable
CC       F-box domain-containing protein as substrate-specific adapter.
CC       Component of the SCF(CDC4) complex containing CDC4. Component of the
CC       SCF(MET30) complex containing MET30. Component of the SCF(GRR1) complex
CC       containing GRR1. Component of the probable SCF(DIA2) complex containing
CC       DIA2. Component of the probable SCF(YDR131C) complex containing
CC       YDR131C. Component of the probable SCF(YDR306C) complex containing
CC       YDR306C. Component of the probable SCF(YLR224W) complex containing
CC       YLR224W. Component of the probable SCF(YJL149W) complex containing
CC       YJL149W. Component of the probable SCF(YNL311C) complex containing
CC       YNL311C. Component of the probable SCF(MDM30) complex containing MDM30.
CC       Component of the probable SCF(UFO1) complex containing UFO1. Component
CC       of the probable SCF(HRT3) complex containing HRT3. Component of the
CC       probable SCF(YBR280C) complex containing YBR280C. Component of the
CC       probable SCF(YBR352W) complex containing YBR352W. Interacts with DCN1,
CC       YBR280C, YLR224W and YLR352W. The unneddylated form interacts with
CC       LAG2/CAND1 and the interaction mediates the exchange of the F-box
CC       substrate-specific subunit. {ECO:0000269|PubMed:10385629,
CC       ECO:0000269|PubMed:11283612, ECO:0000269|PubMed:16421250,
CC       ECO:0000269|PubMed:19763088, ECO:0000269|PubMed:19942853,
CC       ECO:0000269|PubMed:9346238, ECO:0000269|PubMed:9346239,
CC       ECO:0000269|PubMed:9499404}.
CC   -!- INTERACTION:
CC       Q12018; P14682: CDC34; NbExp=3; IntAct=EBI-4321, EBI-19730;
CC       Q12018; P07834: CDC4; NbExp=8; IntAct=EBI-4321, EBI-4434;
CC       Q12018; Q12395: DCN1; NbExp=3; IntAct=EBI-4321, EBI-29871;
CC       Q12018; P24814: GRR1; NbExp=9; IntAct=EBI-4321, EBI-7898;
CC       Q12018; Q08273: HRT1; NbExp=9; IntAct=EBI-4321, EBI-31686;
CC       Q12018; Q92325: LAG2; NbExp=10; IntAct=EBI-4321, EBI-2045650;
CC       Q12018; P39014: MET30; NbExp=10; IntAct=EBI-4321, EBI-11507;
CC       Q12018; P38352: SAF1; NbExp=7; IntAct=EBI-4321, EBI-21172;
CC       Q12018; P52286: SKP1; NbExp=29; IntAct=EBI-4321, EBI-4090;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- PTM: Neddylated; enhancing the ubiquitin-ligase activity.
CC       {ECO:0000250|UniProtKB:P47050}.
CC   -!- MISCELLANEOUS: Present with 377 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00330}.
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DR   EMBL; U43564; AAB38821.1; -; Genomic_DNA.
DR   EMBL; X96876; CAA65628.1; -; Genomic_DNA.
DR   EMBL; Z74180; CAA98702.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11727.1; -; Genomic_DNA.
DR   PIR; S67675; S67675.
DR   RefSeq; NP_010150.1; NM_001180191.1.
DR   PDB; 3O2P; X-ray; 2.23 A; E=730-815.
DR   PDB; 3O6B; X-ray; 3.10 A; B/D/F/H/J=742-815.
DR   PDBsum; 3O2P; -.
DR   PDBsum; 3O6B; -.
DR   AlphaFoldDB; Q12018; -.
DR   SMR; Q12018; -.
DR   BioGRID; 31930; 532.
DR   ComplexPortal; CPX-3234; SCF-Cdc4 ubiquitin ligase complex.
DR   ComplexPortal; CPX-3241; SCF-Grr1 ubiquitin ligase complex.
DR   ComplexPortal; CPX-3242; SCF-Mdm30 ubiquitin ligase complex.
DR   ComplexPortal; CPX-3243; SCF-Ufo1 ubiquitin ligase complex.
DR   ComplexPortal; CPX-3244; SCF-Das1 ubiquitin ligase complex.
DR   ComplexPortal; CPX-3249; SCF-MET30 E3 ubiquitin ligase complex.
DR   ComplexPortal; CPX-3250; SCF-Dia2 ubiquitin ligase complex.
DR   ComplexPortal; CPX-3253; SCF-Ylr352w ubiquitin ligase complex.
DR   ComplexPortal; CPX-3254; SCF-Saf1 ubiquitin ligase complex.
DR   ComplexPortal; CPX-3255; SCF-Hrt3 ubiquitin ligase complex.
DR   ComplexPortal; CPX-3681; SCF-Ydr131c ubiquitin ligase complex.
DR   DIP; DIP-1234N; -.
DR   IntAct; Q12018; 71.
DR   MINT; Q12018; -.
DR   STRING; 4932.YDL132W; -.
DR   MoonDB; Q12018; Predicted.
DR   iPTMnet; Q12018; -.
DR   MaxQB; Q12018; -.
DR   PaxDb; 4932-YDL132W; -.
DR   PeptideAtlas; Q12018; -.
DR   EnsemblFungi; YDL132W_mRNA; YDL132W; YDL132W.
DR   GeneID; 851424; -.
DR   KEGG; sce:YDL132W; -.
DR   AGR; SGD:S000002290; -.
DR   SGD; S000002290; CDC53.
DR   VEuPathDB; FungiDB:YDL132W; -.
DR   eggNOG; KOG2166; Eukaryota.
DR   GeneTree; ENSGT00940000154774; -.
DR   HOGENOM; CLU_004747_6_1_1; -.
DR   InParanoid; Q12018; -.
DR   OMA; IREWDRY; -.
DR   OrthoDB; 5474206at2759; -.
DR   BioCyc; YEAST:G3O-29530-MONOMER; -.
DR   Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-SCE-917937; Iron uptake and transport.
DR   Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   BioGRID-ORCS; 851424; 1 hit in 10 CRISPR screens.
DR   EvolutionaryTrace; Q12018; -.
DR   PRO; PR:Q12018; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q12018; Protein.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:SGD.
DR   GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:SGD.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071406; P:cellular response to methylmercury; NAS:ComplexPortal.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:ComplexPortal.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IGI:SGD.
DR   GO; GO:0008053; P:mitochondrial fusion; NAS:ComplexPortal.
DR   GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; NAS:ComplexPortal.
DR   GO; GO:0010828; P:positive regulation of glucose transmembrane transport; IDA:ComplexPortal.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0019222; P:regulation of metabolic process; NAS:ComplexPortal.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; NAS:ComplexPortal.
DR   GO; GO:0031335; P:regulation of sulfur amino acid metabolic process; NAS:ComplexPortal.
DR   GO; GO:0000409; P:regulation of transcription by galactose; NAS:ComplexPortal.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:SGD.
DR   GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IDA:ComplexPortal.
DR   GO; GO:0031509; P:subtelomeric heterochromatin formation; NAS:ComplexPortal.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:SGD.
DR   Gene3D; 1.20.1310.10; Cullin Repeats; 4.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR045093; Cullin.
DR   InterPro; IPR016157; Cullin_CS.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR036317; Cullin_homology_sf.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR019559; Cullin_neddylation_domain.
DR   InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11932; CULLIN; 1.
DR   PANTHER; PTHR11932:SF169; CULLIN-1; 1.
DR   Pfam; PF00888; Cullin; 1.
DR   Pfam; PF10557; Cullin_Nedd8; 1.
DR   SMART; SM00182; CULLIN; 1.
DR   SMART; SM00884; Cullin_Nedd8; 1.
DR   SUPFAM; SSF75632; Cullin homology domain; 1.
DR   SUPFAM; SSF74788; Cullin repeat-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS01256; CULLIN_1; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cytoplasm; Isopeptide bond;
KW   Nucleus; Reference proteome; Ubl conjugation.
FT   CHAIN           1..815
FT                   /note="Cell division control protein 53"
FT                   /id="PRO_0000119805"
FT   REGION          9..280
FT                   /note="Required for interaction with SKP1/CBF3D and F-box
FT                   protein"
FT   REGION          448..748
FT                   /note="Required for interaction with CDC34/UBC3"
FT   CROSSLNK        760
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in NEDD8)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13616"
FT   MUTAGEN         488
FT                   /note="R->C: Prevents CDC34/UBC3 interaction."
FT                   /evidence="ECO:0000269|PubMed:9499404"
FT   HELIX           735..762
FT                   /evidence="ECO:0007829|PDB:3O2P"
FT   STRAND          763..766
FT                   /evidence="ECO:0007829|PDB:3O2P"
FT   HELIX           767..778
FT                   /evidence="ECO:0007829|PDB:3O2P"
FT   TURN            779..781
FT                   /evidence="ECO:0007829|PDB:3O2P"
FT   HELIX           786..798
FT                   /evidence="ECO:0007829|PDB:3O2P"
FT   STRAND          801..804
FT                   /evidence="ECO:0007829|PDB:3O2P"
FT   STRAND          808..813
FT                   /evidence="ECO:0007829|PDB:3O2P"
SQ   SEQUENCE   815 AA;  93944 MW;  22BC8B35034EDDEF CRC64;
     MSETLPRSDD LEATWNFIEP GINQILGNEK NQASTSKRVY KILSPTMYME VYTAIYNYCV
     NKSRSSGHFS TDSRTGQSTI LVGSEIYEKL KNYLKNYILN FKQSNSETFL QFYVKRWKRF
     TIGAIFLNHA FDYMNRYWVQ KERSDGKRHI FDVNTLCLMT WKEVMFDPSK DVLINELLDQ
     VTLGREGQII QRSNISTAIK SLVALGIDPQ DLKKLNLNVY IQVFEKPFLK KTQEYYTQYT
     NDYLEKHSVT EYIFEAHEII KREEKAMTIY WDDHTKKPLS MALNKVLITD HIEKLENEFV
     VLLDARDIEK ITSLYALIRR DFTLIPRMAS VFENYVKKTG ENEISSLLAM HKHNIMKNEN
     ANPKKLALMT AHSLSPKDYI KKLLEVHDIF SKIFNESFPD DIPLAKALDN ACGAFININE
     FALPAGSPKS ATSKTSEMLA KYSDILLKKA TKPEVASDMS DEDIITIFKY LTDKDAFETH
     YRRLFAKRLI HGTSTSAEDE ENIIQRLQAA NSMEYTGKIT KMFQDIRLSK ILEDDFAVAL
     KNEPDYSKAK YPDLQPFVLA ENMWPFSYQE VEFKLPKELV PSHEKLKESY SQKHNGRILK
     WLWPLCRGEL KADIGKPGRM PFNFTVTLFQ MAILLLYNDA DVLTLENIQE GTSLTIQHIA
     AAMVPFIKFK LIQQVPPGLD ALVKPETQFK LSRPYKALKT NINFASGVKN DILQSLSGGG
     HDNHGNKLGN KRLTEDERIE KELNTERQIF LEACIVRIMK AKRNLPHTTL VNECIAQSHQ
     RFNAKVSMVK RAIDSLIQKG YLQRGDDGES YAYLA
//
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