ETT1_YEAST
ID ETT1_YEAST Reviewed; 412 AA.
AC Q08421; D6W2B6; O00016; Q6Q5I2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Enhancer of translation termination 1;
GN Name=ETT1; OrderedLocusNames=YOR051C; ORFNames=YOR29-02;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9133743;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT presence of two tRNAs and 24 new open reading frames.";
RL Yeast 13:379-390(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [6]
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 [7]
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 [8]
RP FUNCTION.
RX PubMed=14671320; DOI=10.1073/pnas.2536857100;
RA Kushner D.B., Lindenbach B.D., Grdzelishvili V.Z., Noueiry A.O., Paul S.M.,
RA Ahlquist P.;
RT "Systematic, genome-wide identification of host genes affecting replication
RT of a positive-strand RNA virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15764-15769(2003).
RN [9]
RP INTERACTION WITH STM1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15044472; DOI=10.1074/jbc.m401981200;
RA Van Dyke M.W., Nelson L.D., Weilbaecher R.G., Mehta D.V.;
RT "Stm1p, a G4 quadruplex and purine motif triplex nucleic acid-binding
RT protein, interacts with ribosomes and subtelomeric Y' DNA in Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 279:24323-24333(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [11]
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 [12]
RP FUNCTION.
RX PubMed=20630870; DOI=10.1074/jbc.m110.106864;
RA Henri J., Rispal D., Bayart E., van Tilbeurgh H., Seraphin B., Graille M.;
RT "Structural and functional insights into Saccharomyces cerevisiae Tpa1, a
RT putative prolylhydroxylase influencing translation termination and
RT transcription.";
RL J. Biol. Chem. 285:30767-30778(2010).
CC -!- FUNCTION: Required for correct translation termination and probably
CC involved in regulation of hypoxic gene expression in association TPA1.
CC Inhibits replication of Brome mosaic virus.
CC {ECO:0000269|PubMed:14671320, ECO:0000269|PubMed:20630870}.
CC -!- SUBUNIT: Interacts with STM1. {ECO:0000269|PubMed:15044472}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 10800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ETT1 family. {ECO:0000305}.
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DR EMBL; Z70678; CAA94536.1; -; Genomic_DNA.
DR EMBL; Z74959; CAA99243.1; -; Genomic_DNA.
DR EMBL; AY558045; AAS56371.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10832.1; -; Genomic_DNA.
DR PIR; S66925; S66925.
DR RefSeq; NP_014694.1; NM_001183470.1.
DR AlphaFoldDB; Q08421; -.
DR SMR; Q08421; -.
DR BioGRID; 34451; 65.
DR DIP; DIP-2852N; -.
DR IntAct; Q08421; 3.
DR MINT; Q08421; -.
DR STRING; 4932.YOR051C; -.
DR iPTMnet; Q08421; -.
DR MaxQB; Q08421; -.
DR PaxDb; Q08421; -.
DR PRIDE; Q08421; -.
DR EnsemblFungi; YOR051C_mRNA; YOR051C; YOR051C.
DR GeneID; 854216; -.
DR KEGG; sce:YOR051C; -.
DR SGD; S000005577; ETT1.
DR VEuPathDB; FungiDB:YOR051C; -.
DR eggNOG; ENOG502QPHX; Eukaryota.
DR HOGENOM; CLU_050427_0_0_1; -.
DR InParanoid; Q08421; -.
DR OMA; GIVHECD; -.
DR BioCyc; YEAST:G3O-33594-MON; -.
DR PRO; PR:Q08421; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08421; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:2000640; P:positive regulation of SREBP signaling pathway; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0006415; P:translational termination; IMP:SGD.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR024318; Nro1/ETT1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR28290; PTHR28290; 1.
DR Pfam; PF12753; Nro1; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Translation regulation.
FT CHAIN 1..412
FT /note="Enhancer of translation termination 1"
FT /id="PRO_0000245279"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 338
FT /note="K -> E (in Ref. 4; AAS56371)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 47352 MW; DE8EDE32B80A5D60 CRC64;
MAKRPLGLGK QSREKKRKVE SVEKKSDEPS RESTPVRSQM SVELDDDADL DDELAQLKGL
WSKYFHSDRD DEYVLNGIVH ECDRLLRLSE EDKEIKKTLN DIFHGIYALA LSELTIFKAG
DEEATEEKRK KDVSSFFESA IERVELGLSH FPESQFLKLV LAKIIFQRIP LEYISNLHLK
SKDKKLDLVG QLEHGKKHFS IYENDTEFTF EILQMVNDLL DIVENFGREQ SIQEGIDSDN
EEEEELIDIE LEPEHPVYPL QQSLEANYEW LRNHFDKLLD NTNTDVKIYA SIANTLGELY
LKKAEEPSKV FLSLQYDDGG SEKVSDKEAK NAQETALKHT KKALEYLEKA KLEDDPDTWV
QVAEAYIDLG NLLDNESAEQ EEAYKTAEEI LGKANKASHG KFQDVLDNFL QG