ESF2_YEAST
ID ESF2_YEAST Reviewed; 316 AA.
AC P53743; D6W1M9;
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=Pre-rRNA-processing protein ESF2;
DE AltName: Full=18S rRNA factor 2;
GN Name=ESF2; Synonyms=ABT1; OrderedLocusNames=YNR054C; ORFNames=N3491;
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 [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 [2]
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 [3]
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 [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, AND IDENTIFICATION IN A 90S PRERIBOSOME.
RX PubMed=15964808; DOI=10.1128/mcb.25.13.5523-5534.2005;
RA Hoang T., Peng W.-T., Vanrobays E., Krogan N., Hiley S., Beyer A.L.,
RA Osheim Y.N., Greenblatt J., Hughes T.R., Lafontaine D.L.J.;
RT "Esf2p, a U3-associated factor required for small-subunit processome
RT assembly and compaction.";
RL Mol. Cell. Biol. 25:5523-5534(2005).
RN [6]
RP FUNCTION, INTERACTION WITH DBP8, AND RRNA-BINDING.
RX PubMed=16772403; DOI=10.1093/nar/gkl419;
RA Granneman S., Lin C., Champion E.A., Nandineni M.R., Zorca C.,
RA Baserga S.J.;
RT "The nucleolar protein Esf2 interacts directly with the DExD/H box RNA
RT helicase, Dbp8, to stimulate ATP hydrolysis.";
RL Nucleic Acids Res. 34:3189-3199(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-13 AND SER-14, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-13 AND SER-14, 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 -!- FUNCTION: Involved in the small subunit (SSU) processome assembly and
CC function, and in the 18S rRNA synthesis. Required for the early
CC cleavages at sites A0, A1 and A2. Stimulates DBP8 RNA helicase ATPase
CC activity. {ECO:0000269|PubMed:15964808, ECO:0000269|PubMed:16772403}.
CC -!- SUBUNIT: Component of the 90S pre-ribosomes. Interacts directly with
CC DBP8. {ECO:0000269|PubMed:15964808, ECO:0000269|PubMed:16772403}.
CC -!- INTERACTION:
CC P53743; P38719: DBP8; NbExp=4; IntAct=EBI-28537, EBI-5633;
CC P53743; Q06344: ESF1; NbExp=6; IntAct=EBI-28537, EBI-34121;
CC P53743; Q03532: HAS1; NbExp=2; IntAct=EBI-28537, EBI-8170;
CC P53743; P20448: HCA4; NbExp=2; IntAct=EBI-28537, EBI-5612;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 12800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ESF2/ABP1 family. {ECO:0000305}.
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DR EMBL; Z71669; CAA96335.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10595.1; -; Genomic_DNA.
DR PIR; S63385; S63385.
DR RefSeq; NP_014452.1; NM_001183231.1.
DR AlphaFoldDB; P53743; -.
DR BioGRID; 35879; 166.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-6417N; -.
DR IntAct; P53743; 28.
DR MINT; P53743; -.
DR STRING; 4932.YNR054C; -.
DR iPTMnet; P53743; -.
DR MaxQB; P53743; -.
DR PaxDb; P53743; -.
DR PRIDE; P53743; -.
DR EnsemblFungi; YNR054C_mRNA; YNR054C; YNR054C.
DR GeneID; 855790; -.
DR KEGG; sce:YNR054C; -.
DR SGD; S000005337; ESF2.
DR VEuPathDB; FungiDB:YNR054C; -.
DR eggNOG; KOG3152; Eukaryota.
DR GeneTree; ENSGT00390000002062; -.
DR HOGENOM; CLU_054086_0_0_1; -.
DR InParanoid; P53743; -.
DR OMA; TRKHNDF; -.
DR BioCyc; YEAST:G3O-33360-MON; -.
DR PRO; PR:P53743; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53743; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0034462; P:small-subunit processome assembly; IMP:SGD.
DR CDD; cd12263; RRM_ABT1_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR039119; ABT1/Esf2.
DR InterPro; IPR034353; ABT1/ESF2_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR PANTHER; PTHR12311; PTHR12311; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA processing.
FT CHAIN 1..316
FT /note="Pre-rRNA-processing protein ESF2"
FT /id="PRO_0000203480"
FT DOMAIN 114..204
FT /note="RRM"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 316 AA; 36408 MW; 5F38B88CDEEFC01F CRC64;
MSEKVNSDFE DFSSDEETDQ HNVLIQTKKK ISSKDDIFSK KVEDIESENE SDIEEEQKQE
EKEDVEQPDK ENGEKLDREV EEQASSTTSL DLKTEKLRQL VKSKAAKKSK HKTGVVYFSS
IPPYMKPAKM RQILTRFGEV DRLFLKKEDD QKYKQRVKGG GNKKNKYEEG WAEFIRKRDA
KLCAETLNGN IIGGKKGTFY HDDILNVKYL PGFKWADLTE QIARENDIRQ AKLEMEISQA
NKLNAEFIRN VEQSKMIQNI KNSRKRAGKE GESADSHPHR EFKQRRVETS RANAPSDIKQ
QSSGSKDLGN VLTNLL
