CUL3_YEAST
ID CUL3_YEAST Reviewed; 744 AA.
AC P53202; D6VUE0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Cullin-3;
DE AltName: Full=Cullin-B;
GN Name=CUL3; OrderedLocusNames=YGR003W;
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], AND FUNCTION.
RX PubMed=12676951; DOI=10.1074/jbc.m210358200;
RA Michel J.J., McCarville J.F., Xiong Y.;
RT "A role for Saccharomyces cerevisiae Cul8 ubiquitin ligase in proper
RT anaphase progression.";
RL J. Biol. Chem. 278:22828-22837(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 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 [5]
RP FUNCTION.
RX PubMed=17296727; DOI=10.1128/mcb.00091-07;
RA Ribar B., Prakash L., Prakash S.;
RT "ELA1 and CUL3 are required along with ELC1 for RNA polymerase II
RT polyubiquitylation and degradation in DNA-damaged yeast cells.";
RL Mol. Cell. Biol. 27:3211-3216(2007).
CC -!- FUNCTION: Component of a ubiquitin-protein ligase. Together with ELA1
CC is required for polyubiquitination and degradation of RBP1.
CC {ECO:0000269|PubMed:12676951, ECO:0000269|PubMed:17296727}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- PTM: Neddylated; enhancing the ubiquitin-ligase activity.
CC {ECO:0000250|UniProtKB:P47050}.
CC -!- MISCELLANEOUS: Present with 172 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; AY387706; AAQ91375.1; -; Genomic_DNA.
DR EMBL; Z72788; CAA96986.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08101.1; -; Genomic_DNA.
DR PIR; S64292; S64292.
DR RefSeq; NP_011517.1; NM_001181132.1.
DR AlphaFoldDB; P53202; -.
DR SMR; P53202; -.
DR BioGRID; 33247; 129.
DR ComplexPortal; CPX-1191; Global genome repair CUL3/RAD7/RAD16/ELC1 ubiquitin ligase complex.
DR ComplexPortal; CPX-1837; CUL3-HRT1/ELC1/ELA1 ubiquitin ligase complex.
DR DIP; DIP-5506N; -.
DR IntAct; P53202; 3.
DR MINT; P53202; -.
DR STRING; 4932.YGR003W; -.
DR iPTMnet; P53202; -.
DR MaxQB; P53202; -.
DR PaxDb; P53202; -.
DR PRIDE; P53202; -.
DR EnsemblFungi; YGR003W_mRNA; YGR003W; YGR003W.
DR GeneID; 852886; -.
DR KEGG; sce:YGR003W; -.
DR SGD; S000003235; CUL3.
DR VEuPathDB; FungiDB:YGR003W; -.
DR eggNOG; KOG2166; Eukaryota.
DR HOGENOM; CLU_004747_7_1_1; -.
DR InParanoid; P53202; -.
DR OMA; MFKDMTI; -.
DR BioCyc; YEAST:G3O-30734-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:P53202; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53202; protein.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
DR GO; GO:0070911; P:global genome nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0006289; P:nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0009411; P:response to UV; IDA:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
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 Isopeptide bond; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..744
FT /note="Cullin-3"
FT /id="PRO_0000119806"
FT CROSSLNK 688
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
SQ SEQUENCE 744 AA; 86115 MW; 6C4EB4A70F3CB18F CRC64;
MITNKKIKIS VPEKLGLSEE SFEESWETVK YAIDHIYSDD MADLSFEQVY KTIYTIVLNK
KGPILYNRLK DYLIQKLALL RETIVKDNTH DYEFLGTMAR LWEVQCHCFK ITGDLMMYMD
KVYCKPNRCM EVYDMCLDLF RIEILQKCSS SLISALISDI ERIRNLGSVD SEHTSLWKVL
IGMMETLHDN RDSFFLTDFE PVLISATEEY YNKAIDIELL TPIESLEKIR KLRQFESMLD
SSFLNVDSHN KLKTVLENVL IWGKLSDIIE DLTHEAMVIS NGKLLQEIYD LSSEEKYRVT
VIESIKSYIN KNAINIPFNE GNRKKGQNAI TWSSEIVELY RSQHSFLESI DFGSVRLNNL
TGDVSNAILG DVFSMYFSKE GALPSEYLST YVDHCMKRTK EKDAEIVKIK QDLLDSTKLI
GLLTEKDIFE KIYKKQLSRR LLQQRSLVEI EKWMVQMIKK VLGTFFTSKL EIMLRDISLS
SEMYQAFQHS TINSIEYLSF APQVLTRTSW PFQSTNPIDE GISLPPRMSQ ILAGFEGYYS
LKYKERVLKW AHHLSVIEIG CQFNSGYYEI SFSVYAGVIF LLFEDYEELT LGEIYELTHI
PIDDVKSLVM SMSTIPRCKI LKKSSSSGNM KFSVNYFFSS PNRKVKVPVI ACPLPSQKSD
NLATASSVDT YDNEIVMELS AIIVRIMKTE GKLSHQQLLE RTTKRTQSRL SLTPSILKRS
IQLLIEKEYI QRNADDPSYY HYLS
