ELOC_YEAST
ID ELOC_YEAST Reviewed; 99 AA.
AC Q03071; D6W3W8; O13292;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Elongin-C;
GN Name=ELC1; OrderedLocusNames=YPL046C;
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 INDUCTION.
RX PubMed=9425272; DOI=10.1006/bbrc.1997.7819;
RA Aso T., Conrad M.N.;
RT "Molecular cloning of DNAs encoding the regulatory subunits of elongin from
RT Saccharomyces cerevisiae and Drosophila melanogaster.";
RL Biochem. Biophys. Res. Commun. 241:334-340(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP INTERACTION WITH CIN5; PCL6 AND SNF4.
RX PubMed=10760578; DOI=10.1016/s0167-4781(00)00052-x;
RA Jackson T., Kwon E., Chachulska A.M., Hyman L.E.;
RT "Novel roles for elongin C in yeast.";
RL Biochim. Biophys. Acta 1491:161-176(2000).
RN [6]
RP IDENTIFICATION IN THE ELA1-ELC1 COMPLEX.
RX PubMed=10753924; DOI=10.1074/jbc.275.15.11174;
RA Koth C.M., Botuyan M.V., Moreland R.J., Jansma D.B., Conaway J.W.,
RA Conaway R.C., Chazin W.J., Friesen J.D., Arrowsmith C.H., Edwards A.M.;
RT "Elongin from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:11174-11180(2000).
RN [7]
RP FUNCTION.
RX PubMed=11864988; DOI=10.1074/jbc.m200800200;
RA Hyman L.E., Kwon E., Ghosh S., McGee J., Chachulska A.M., Jackson T.,
RA Baricos W.H.;
RT "Binding to Elongin C inhibits degradation of interacting proteins in
RT yeast.";
RL J. Biol. Chem. 277:15586-15591(2002).
RN [8]
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 [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP STRUCTURE BY NMR IN COMPLEX WITH THE VON HIPPEL-LINDAU PEPTIDE, AND
RP INTERACTION WITH ELA1.
RX PubMed=10430890; DOI=10.1073/pnas.96.16.9033;
RA Botuyan M.V., Koth C.M., Mer G., Chakrabartty A., Conaway J.W.,
RA Conaway R.C., Edwards A.M., Arrowsmith C.H., Chazin W.J.;
RT "Binding of elongin A or a von Hippel-Lindau peptide stabilizes the
RT structure of yeast elongin C.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:9033-9038(1999).
RN [13]
RP STRUCTURE BY NMR, AND SUBUNIT.
RX PubMed=10998253; DOI=10.1021/bi0008231;
RA Buchberger A., Howard M.J., Freund S.M.V., Proctor M., Butler P.J.G.,
RA Fersht A.R., Bycroft M.;
RT "Biophysical characterization of elongin C from Saccharomyces cerevisiae.";
RL Biochemistry 39:11137-11146(2000).
RN [14]
RP STRUCTURE BY NMR IN COMPLEX WITH THE VON HIPPEL-LINDAU PEPTIDE.
RX PubMed=11545595; DOI=10.1006/jmbi.2001.4938;
RA Botuyan M.V., Mer G., Yi G.-S., Koth C.M., Case D.A., Edwards A.M.,
RA Chazin W.J., Arrowsmith C.H.;
RT "Solution structure and dynamics of yeast elongin C in complex with a von
RT Hippel-Lindau peptide.";
RL J. Mol. Biol. 312:177-186(2001).
CC -!- FUNCTION: Prevents degradation of interacting proteins like PCL6 by the
CC proteasome. {ECO:0000269|PubMed:11864988}.
CC -!- SUBUNIT: Forms a complex with F-box protein ELA1. Interacts with CIN5,
CC PCL6 and SNF4. {ECO:0000269|PubMed:10430890,
CC ECO:0000269|PubMed:10753924, ECO:0000269|PubMed:10760578,
CC ECO:0000269|PubMed:10998253, ECO:0000269|PubMed:11545595}.
CC -!- INTERACTION:
CC Q03071; P53861: ELA1; NbExp=6; IntAct=EBI-30154, EBI-29191;
CC Q03071; P06779: RAD7; NbExp=4; IntAct=EBI-30154, EBI-14780;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: During sporulation. {ECO:0000269|PubMed:9425272}.
CC -!- MISCELLANEOUS: In contrast to other members of the family it does not
CC integrate a functional E3 ubiquitin complex.
CC -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
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DR EMBL; AB007691; BAA22612.1; -; Genomic_DNA.
DR EMBL; U44030; AAB68175.1; -; Genomic_DNA.
DR EMBL; AY558329; AAS56655.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11384.1; -; Genomic_DNA.
DR PIR; JC5792; JC5792.
DR RefSeq; NP_015279.1; NM_001183860.1.
DR PDB; 1HV2; NMR; -; A=1-99.
DR PDB; 5ZB2; X-ray; 2.30 A; B=1-99.
DR PDB; 6R6H; EM; 8.40 A; Q=1-99.
DR PDB; 6R7I; EM; 5.90 A; Q=1-99.
DR PDBsum; 1HV2; -.
DR PDBsum; 5ZB2; -.
DR PDBsum; 6R6H; -.
DR PDBsum; 6R7I; -.
DR AlphaFoldDB; Q03071; -.
DR SMR; Q03071; -.
DR BioGRID; 36134; 139.
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-6531N; -.
DR IntAct; Q03071; 2.
DR MINT; Q03071; -.
DR STRING; 4932.YPL046C; -.
DR iPTMnet; Q03071; -.
DR MaxQB; Q03071; -.
DR PaxDb; Q03071; -.
DR PRIDE; Q03071; -.
DR EnsemblFungi; YPL046C_mRNA; YPL046C; YPL046C.
DR GeneID; 856061; -.
DR KEGG; sce:YPL046C; -.
DR SGD; S000005967; ELC1.
DR VEuPathDB; FungiDB:YPL046C; -.
DR eggNOG; KOG3473; Eukaryota.
DR GeneTree; ENSGT00390000011717; -.
DR HOGENOM; CLU_130038_1_1_1; -.
DR InParanoid; Q03071; -.
DR OMA; MHIKLIS; -.
DR BioCyc; YEAST:G3O-33959-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR ChiTaRS; ELC1; yeast.
DR EvolutionaryTrace; Q03071; -.
DR PRO; PR:Q03071; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q03071; protein.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IMP:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070449; C:elongin complex; IPI:SGD.
DR GO; GO:0000113; C:nucleotide-excision repair factor 4 complex; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0070911; P:global genome nucleotide-excision repair; IMP:SGD.
DR GO; GO:0006289; P:nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0016567; P:protein ubiquitination; IEA:GOC.
DR GO; GO:0009411; P:response to UV; IDA:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:SGD.
DR DisProt; DP01430; -.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR039948; ELC1.
DR InterPro; IPR001232; SKP1-like.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR016073; Skp1_comp_POZ.
DR PANTHER; PTHR20648; PTHR20648; 1.
DR Pfam; PF03931; Skp1_POZ; 1.
DR SMART; SM00512; Skp1; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..99
FT /note="Elongin-C"
FT /id="PRO_0000239644"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT CONFLICT 64
FT /note="N -> Y (in Ref. 1; BAA22612)"
FT /evidence="ECO:0000305"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:5ZB2"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:5ZB2"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:1HV2"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:1HV2"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 51..67
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 87..97
FT /evidence="ECO:0007829|PDB:5ZB2"
SQ SEQUENCE 99 AA; 11328 MW; B77BAC75D40BD53E CRC64;
MSQDFVTLVS KDDKEYEISR SAAMISPTLK AMIEGPFRES KGRIELKQFD SHILEKAVEY
LNYNLKYSGV SEDDDEIPEF EIPTEMSLEL LLAADYLSI
