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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
 
 
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