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 03-AUG-2022, entry version 176.
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 containig 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; 521.
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 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; Q12018; -.
DR PRIDE; Q12018; -.
DR EnsemblFungi; YDL132W_mRNA; YDL132W; YDL132W.
DR GeneID; 851424; -.
DR KEGG; sce:YDL132W; -.
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; GVYTAVH; -.
DR BioCyc; YEAST:G3O-29530-MON; -.
DR Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR EvolutionaryTrace; Q12018; -.
DR PRO; PR:Q12018; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12018; protein.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
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; IC: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; IC:ComplexPortal.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IC: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; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0031335; P:regulation of sulfur amino acid metabolic process; IC:ComplexPortal.
DR GO; GO:0000409; P:regulation of transcription by galactose; IC: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 assembly; IDA:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:SGD.
DR Gene3D; 1.10.10.10; -; 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; PTHR11932; 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
DR SUPFAM; SSF75632; SSF75632; 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
