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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
 
 
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