ID   ELOA1_YEAST             Reviewed;         379 AA.
AC   P53861; D6W0W2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   10-JUN-2026, entry version 177.
DE   RecName: Full=Elongin-A;
GN   Name=ELA1 {ECO:0000312|SGD:S000005174};
GN   OrderedLocusNames=YNL230C {ECO:0000312|SGD:S000005174};
GN   ORFNames=N1161;
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=8896273;
RX   DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1071::aid-yea4%3e3.0.co;2-s;
RA   Pandolfo D., de Antoni A., Lanfranchi G., Valle G.;
RT   "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open
RT   reading frames including a novel gene encoding a globin-like domain.";
RL   Yeast 12:1071-1076(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873; DOI=10.1038/387s093;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(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   INTERACTION WITH ELC1.
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   [5]
RP   IDENTIFICATION OF 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   [6]
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   [7]
RP   FUNCTION, AND IDENTIFICATION IN A CRL3 E3 UBIQUITIN LIGASE COMPLEX.
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).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-278, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [10]
RP   INTERACTION WITH DEF1 AND RPO21.
RX   PubMed=23993092; DOI=10.1016/j.cell.2013.07.028;
RA   Wilson M.D., Harreman M., Taschner M., Reid J., Walker J.,
RA   Erdjument-Bromage H., Tempst P., Svejstrup J.Q.;
RT   "Proteasome-mediated processing of Def1, a critical step in the cellular
RT   response to transcription stress.";
RL   Cell 154:983-995(2013).
CC   -!- FUNCTION: As part of the CRL3 E3 ubiquitin ligase complex;
CC       polyubiquitylates monoubiquitylated RNA polymerase II subunit RPO21 to
CC       trigger its proteolysis; plays a role in global genomic repair.
CC       {ECO:0000269|PubMed:17296727}.
CC   -!- SUBUNIT: Heterodimer with ELC1 (PubMed:10430890, PubMed:10753924).
CC       Component of a CRL3 E3 ubiquitin ligase complex consisting of the
CC       cullin CUL3, the linker protein ELC1, the substrate receptor ELA1, and
CC       the RING protein HRT1 (Probable). Interacts with the large RNA
CC       polymerase II subunit RPO21 in a DEF1-dependent manner
CC       (PubMed:23993092). Interacts (via C-terminus) with DEF1 (via CUE
CC       domain); the interaction is direct (PubMed:23993092).
CC       {ECO:0000269|PubMed:10430890, ECO:0000269|PubMed:10753924,
CC       ECO:0000269|PubMed:23993092, ECO:0000305|PubMed:17296727}.
CC   -!- INTERACTION:
CC       P53861; Q03071: ELC1; NbExp=6; IntAct=EBI-29191, EBI-30154;
CC   -!- MISCELLANEOUS: Present with 815 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: In contrast to other members of the family it does not
CC       integrate a functional E3 ubiquitin complex.
CC   -!- SIMILARITY: Belongs to the ELA1 family. {ECO:0000305}.
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DR   EMBL; Z69381; CAA93368.1; -; Genomic_DNA.
DR   EMBL; Z71506; CAA96135.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10328.1; -; Genomic_DNA.
DR   PIR; S63196; S63196.
DR   RefSeq; NP_014169.1; NM_001183068.1.
DR   AlphaFoldDB; P53861; -.
DR   BioGRID; 35608; 102.
DR   ComplexPortal; CPX-1837; CUL3-HRT1-ELC1-ELA1 ubiquitin ligase complex.
DR   DIP; DIP-4281N; -.
DR   FunCoup; P53861; 129.
DR   IntAct; P53861; 40.
DR   MINT; P53861; -.
DR   STRING; 4932.YNL230C; -.
DR   GlyGen; P53861; 3 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P53861; -.
DR   PaxDb; 4932-YNL230C; -.
DR   PeptideAtlas; P53861; -.
DR   EnsemblFungi; YNL230C_mRNA; YNL230C; YNL230C.
DR   GeneID; 855491; -.
DR   KEGG; sce:YNL230C; -.
DR   AGR; SGD:S000005174; -.
DR   SGD; S000005174; ELA1.
DR   VEuPathDB; FungiDB:YNL230C; -.
DR   eggNOG; KOG2821; Eukaryota.
DR   HOGENOM; CLU_062289_0_0_1; -.
DR   InParanoid; P53861; -.
DR   OMA; RMLYFKY; -.
DR   OrthoDB; 21513at2759; -.
DR   BioCyc; YEAST:G3O-33230-MONOMER; -.
DR   BioGRID-ORCS; 855491; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P53861; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53861; protein.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IMP:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0070449; C:elongin complex; IPI:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0006289; P:nucleotide-excision repair; NAS:ComplexPortal.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR   Gene3D; 6.10.250.3180; -; 1.
DR   InterPro; IPR051870; Elongin-A_domain.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR010684; RNA_pol_II_trans_fac_SIII_A.
DR   PANTHER; PTHR15141; TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 3; 1.
DR   PANTHER; PTHR15141:SF76; TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 3; 1.
DR   Pfam; PF06881; Elongin_A; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..379
FT                   /note="Elongin-A"
FT                   /id="PRO_0000203386"
FT   DOMAIN          19..63
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REGION          1..143
FT                   /note="ELC1-binding"
FT   REGION          225..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..379
FT                   /note="Interacts with DEF1"
FT   COMPBIAS        231..240
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         235
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   379 AA;  43981 MW;  293F68C0AC709889 CRC64;
     MKSLQTLCEI SLMRNHSNIQ SVSNVPYHLL KRILQKVKIP QLLKLEKSNV LLIFDDDELW
     LEFLRQDFPT NVHEQFVSKR DIICKYYFDF VKENDIELYH SNQDLLKSCV RQSVVKDIRN
     NKYRIPYRML YSKYQQEVEK KQEESAERLR LEMQKLQQER EKKQTIVVDH TVYFKKRNTK
     KTTRLHNEPH SQLYMKSLKD HESRLKHFKD GGFNIAKRHA QRVAFGGQAG GQSSSPKKGP
     LSIKPEPVKV NRQMDNVTAE KKDVTQPITP VKKRRSESPS IFLNRKKPAL FRPTPKTNAA
     GSRPHTTAIT NDHRTTSHPY PHKDVVTSIS SVTANPVTKG HKKKKSGIFV RNAGSDGDSF
     PHVTATGPTT RPYIYEPRK
//