ELOA1_YEAST
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 03-AUG-2022, entry version 162.
DE RecName: Full=Elongin-A;
GN Name=ELA1; OrderedLocusNames=YNL230C; 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<1071::aid-yea4>3.0.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;
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 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 [8]
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).
CC -!- SUBUNIT: Forms a complex with SKP1-like protein ELC1.
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; 92.
DR ComplexPortal; CPX-1837; CUL3-HRT1/ELC1/ELA1 ubiquitin ligase complex.
DR DIP; DIP-4281N; -.
DR IntAct; P53861; 38.
DR MINT; P53861; -.
DR STRING; 4932.YNL230C; -.
DR iPTMnet; P53861; -.
DR MaxQB; P53861; -.
DR PaxDb; P53861; -.
DR PRIDE; P53861; -.
DR EnsemblFungi; YNL230C_mRNA; YNL230C; YNL230C.
DR GeneID; 855491; -.
DR KEGG; sce:YNL230C; -.
DR SGD; S000005174; ELA1.
DR VEuPathDB; FungiDB:YNL230C; -.
DR eggNOG; KOG2821; Eukaryota.
DR HOGENOM; CLU_062289_0_0_1; -.
DR InParanoid; P53861; -.
DR OMA; RRTTFFN; -.
DR BioCyc; YEAST:G3O-33230-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 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; IC:ComplexPortal.
DR GO; GO:0016567; P:protein ubiquitination; IEA:GOC.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR010684; RNA_pol_II_trans_fac_SIII_A.
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 COMPBIAS 299..337
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
