ESF1_YEAST
ID ESF1_YEAST Reviewed; 628 AA.
AC Q06344; D6VSZ4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Pre-rRNA-processing protein ESF1;
DE AltName: Full=18S rRNA factor 1;
GN Name=ESF1; OrderedLocusNames=YDR365C;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION
RP [LARGE SCALE ANALYSIS].
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND INTERACTION WITH NSR1; KRR1; NOP1; UTP22; PUF6; RPS1; RPS2;
RP RPS3; RPS6; RPS11; RPL2; RPL3; RPL4; RPL7; RPL10; RPL20; RPP0 AND THE
RP SNORNAS U3 AND U14.
RX PubMed=15056729; DOI=10.1093/nar/gkh518;
RA Peng W.-T., Krogan N.J., Richards D.P., Greenblatt J.F., Hughes T.R.;
RT "ESF1 is required for 18S rRNA synthesis in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 32:1993-1999(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-223; SER-225;
RP SER-367; SER-369; SER-372 AND THR-542, AND IDENTIFICATION BY MASS
RP 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 THR-220 AND SER-225, AND
RP IDENTIFICATION BY 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-86; SER-223; SER-225;
RP SER-369; SER-372 AND THR-542, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-223; SER-225;
RP SER-367; SER-369; SER-372 AND THR-542, AND IDENTIFICATION BY MASS
RP 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
CC -!- FUNCTION: Involved in the 18S rRNA synthesis. Required for the early
CC cleavages at sites A0, A1 and A2. {ECO:0000269|PubMed:14690591,
CC ECO:0000269|PubMed:15056729}.
CC -!- SUBUNIT: Interacts with KRR1, NOP1, NSR1, PUF6 and UTP22, proteins
CC involved in 18S rRNA synthesis. Interacts also with ribosomal proteins
CC RPS1, RPS3, RPS4, RPS6, RPS11, RPL2, RPL3, RPL4, RPL7, RPL10, RPL20 and
CC RPP0 as well as with the snoRNAs U3 and U14.
CC {ECO:0000269|PubMed:15056729}.
CC -!- INTERACTION:
CC Q06344; P53743: ESF2; NbExp=6; IntAct=EBI-34121, EBI-28537;
CC Q06344; P20448: HCA4; NbExp=3; IntAct=EBI-34121, EBI-5612;
CC Q06344; P53254: UTP22; NbExp=2; IntAct=EBI-34121, EBI-1878;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14690591}.
CC -!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ESF1 family. {ECO:0000305}.
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DR EMBL; U28373; AAB64801.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12204.1; -; Genomic_DNA.
DR PIR; S61160; S61160.
DR RefSeq; NP_010653.1; NM_001180673.1.
DR AlphaFoldDB; Q06344; -.
DR BioGRID; 32422; 220.
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-5248N; -.
DR IntAct; Q06344; 57.
DR MINT; Q06344; -.
DR STRING; 4932.YDR365C; -.
DR iPTMnet; Q06344; -.
DR MaxQB; Q06344; -.
DR PaxDb; Q06344; -.
DR PRIDE; Q06344; -.
DR EnsemblFungi; YDR365C_mRNA; YDR365C; YDR365C.
DR GeneID; 851969; -.
DR KEGG; sce:YDR365C; -.
DR SGD; S000002773; ESF1.
DR VEuPathDB; FungiDB:YDR365C; -.
DR eggNOG; KOG2318; Eukaryota.
DR GeneTree; ENSGT00390000004881; -.
DR HOGENOM; CLU_010564_0_1_1; -.
DR InParanoid; Q06344; -.
DR OMA; LTWDETA; -.
DR BioCyc; YEAST:G3O-29915-MON; -.
DR PRO; PR:Q06344; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06344; protein.
DR GO; GO:0005730; C:nucleolus; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR InterPro; IPR039754; Esf1.
DR InterPro; IPR012580; NUC153.
DR PANTHER; PTHR12202; PTHR12202; 1.
DR Pfam; PF08159; NUC153; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..628
FT /note="Pre-rRNA-processing protein ESF1"
FT /id="PRO_0000228158"
FT REGION 78..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 426..495
FT /evidence="ECO:0000255"
FT COMPBIAS 78..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 542
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 628 AA; 72410 MW; A16FB043D0ED86B7 CRC64;
MAGENPKKEG VDARFAGIYS DPKFKNTKTK DHKIKLDSRF SKKDLEVQHK SKVDKYGRKI
KNAQNNRELE DFDKYFEKEA ENDEDSEVNA KTVVDRARGE VPDDYVSSSD EFTSSDSESS
GESEVESEEE NEVEIENAKP ESGDISKNLA VVNLDWDHVK SEDLMITFSS FVPKGGKIER
VAIYPSEFGK ERMQREEVEG PPKELFQKKN KNKTSKKKKT DDSDSDMDIG IKDLYEEGDA
DKDVDSRALR QYQLDRLRYY YAIVYCSDTT TSKAIYDNCD GTEYESTANM FDLRYVPDGM
TFDDDVRDEC SILPKNYRPH QFSTDALQHS SVKLTWDETP ADRVEVAKRA FTQKEIDDMD
FKAYLASDSD ESDGQVDEEA KNKLKSLVGD FGFNSKKETP NDEDEEVDME ITFTPALEGG
NEKSSEDKEE TTIEKIRRKE KERRKARKQK VKELKQQSEK DKKSKLKSVN KKHTNDEEEI
EKNAKSKAEL ELLMDDDDDT ETQGTINNKA HFNMNEILRS EKEKHKKGRY QKKERIVEDT
FTPDLEDPRF KEVFEDHDFA IDPTQPEFKG TQAMSKILKE RSKRVKNKKR KLGGSENNMT
NNADDNEDIG NLVNKLKKKS KSSKKVKV
