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P22147

- XRN1_YEAST

UniProt

P22147 - XRN1_YEAST

Protein

5'-3' exoribonuclease 1

Gene

XRN1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
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    Functioni

    Multifunctional protein that exhibits several independent functions at different levels of the cellular processes. 5'-3' exonuclease component of the nonsense-mediated mRNA decay (NMD) which is a highly conserved mRNA degradation pathway, an RNA surveillance system whose role is to identify and rid cells of mRNA with premature termination codons and thus prevents accumulation of potentially harmful truncated proteins. The NMD pathway has a second role regulating the decay of wild-type mRNAs, and especially mRNAs that are important for telomere functions. Participate in CTH2-mediated and VTS1-mediated mRNA turnover. Involved in the degradation of several hypomodified mature tRNA species and participates in the 5'-processing or the degradation of the snoRNA precursors and rRNA processing. Involved in defense against virus and suppresses viral RNA recombination by rapidly removing the 5'-truncated RNAs, the substrates of recombination, and thus reducing the chance for recombination to occur in the parental strain. Required for the assembly of the virus-like particles of the Ty3 retrotransposon and contributes to the efficient generation of narnavirus 20S RNA by playing a major role in the elimination of the non-viral upstream sequences from the primary transcripts. Degrades single-stranded DNA (ss-DNA) and can renature complementary ss-DNA as well as catalyzes the formation of heteroduplex DNA from circular ss-DNA and homologous linear ds-DNA in vitro. Acts as a microtubule-associated protein which interacts with cytoplasmic microtubules through beta-tubulin and promotes in vitro assembly of tubulin into microtubules. Associates with microtubule functions such as chromosome transmission, nuclear migration, and SPB duplication. Has also a role in G1 to S transition and is involved in nuclear fusion during karyogamy. Required for the expression of ROK1 at the post-transcriptional level and for the alpha-factor induction of the karyogamy genes KAR3 and KAR4. Plays a role in filamentous growth.35 Publications

    Cofactori

    Magnesium. Both strand exchange and nuclease activities require magnesium, for the strand exchange activity, calcium can replace magnesium when the linear ds-DNA has been first resected with an exogenous endonuclease.

    Enzyme regulationi

    3'-phosphoadenosine 5'-phosphate (pAp) is an inhibitor of KEM1. Sodium-induced GCN4 expression reduces pAp accumulation by activating HAL2 expression, and therefore maintains mRNA degradation capacity which is likely to be important for the accurate and rapid adaptation of gene expression to salt stress.1 Publication

    GO - Molecular functioni

    1. 5'-3' exoribonuclease activity Source: SGD
    2. chromatin binding Source: SGD
    3. protein binding Source: IntAct
    4. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. karyogamy Source: UniProtKB-KW
    2. nonfunctional rRNA decay Source: SGD
    3. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: SGD
    4. positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD
    5. positive regulation of transcription initiation from RNA polymerase II promoter Source: SGD
    6. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
    7. rRNA processing Source: UniProtKB-KW
    8. traversing start control point of mitotic cell cycle Source: SGD

    Keywords - Molecular functioni

    Exonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    Karyogamy, Nonsense-mediated mRNA decay, rRNA processing

    Keywords - Ligandi

    Magnesium, RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30661-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5'-3' exoribonuclease 1 (EC:3.1.13.-)
    Alternative name(s):
    DNA strand transfer protein beta
    Short name:
    STP-beta
    KAR(-)-enhancing mutation protein
    Strand exchange protein 1
    p175
    Gene namesi
    Name:XRN1
    Synonyms:DST2, KEM1, RAR5, SEP1, SKI1
    Ordered Locus Names:YGL173C
    ORF Names:G1645
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGL173c.
    SGDiS000003141. XRN1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. cytoplasmic mRNA processing body Source: SGD
    3. cytoplasmic stress granule Source: SGD
    4. cytosol Source: Reactome
    5. microtubule Source: UniProtKB-KW
    6. nucleus Source: SGD
    7. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Microtubule

    Pathology & Biotechi

    Disruption phenotypei

    Mutations affect nuclear fusion, leed to reduced chromosome stability and defects in spindle pole body duplication and/or separation as well as loss of viability under conditions of nitrogen starvation. Homozygous diploids are unable to sporulate. Leads also to arrest in pachytene and deficiency in meiotic recombination and sensitivity to oleate.3 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi37 – 371N → D: Reduces strongly exonuclease activity. 1 Publication
    Mutagenesisi41 – 411H → R or D: Reduces strongly exonuclease activity. 1 Publication
    Mutagenesisi86 – 861D → G: Reduces strongly exonuclease activity. 1 Publication
    Mutagenesisi87 – 871G → D: Reduces strongly exonuclease activity. 1 Publication
    Mutagenesisi93 – 931K → M: Reduces strongly exonuclease activity. 1 Publication
    Mutagenesisi97 – 971Q → E or R: Reduces strongly exonuclease activity. 1 Publication
    Mutagenesisi101 – 1011R → G: Reduces strongly exonuclease activity. 1 Publication
    Mutagenesisi176 – 1761E → G: Reduces strongly exonuclease activity.
    Mutagenesisi178 – 1781E → D or G: Reduces strongly exonuclease activity. 1 Publication
    Mutagenesisi201 – 2011C → Y or R: Reduces strongly exonuclease activity. 1 Publication
    Mutagenesisi206 – 2061D → A: Abolishes exonuclease activity in vitro. 1 Publication
    Mutagenesisi208 – 2081D → A: Abolishes exonuclease activity in vitro. 1 Publication
    Mutagenesisi592 – 5921L → P: Reduces strongly exonuclease activity; when associated with Y-710. 1 Publication
    Mutagenesisi710 – 7101Y → C: Reduces strongly exonuclease activity; when associated with P-592. 1 Publication
    Mutagenesisi798 – 7981W → R: Reduces strongly exonuclease activity; when associated with D-1024; F-1043 and P-1197. 1 Publication
    Mutagenesisi1024 – 10241E → D: Reduces strongly exonuclease activity; when associated with R-798; F-1043 and P-1197. 1 Publication
    Mutagenesisi1043 – 10431Y → F: Reduces strongly exonuclease activity; when associated with R-798; D-1024 and P-1197. 1 Publication
    Mutagenesisi1197 – 11971S → P: Reduces strongly exonuclease activity; when associated with R-798; D-1024 and F-1043. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 152815285'-3' exoribonuclease 1PRO_0000071395Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1506 – 15061Phosphothreonine1 Publication
    Modified residuei1510 – 15101Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP22147.
    PaxDbiP22147.
    PeptideAtlasiP22147.

    Expressioni

    Gene expression databases

    GenevestigatoriP22147.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LSM4P400703EBI-9642,EBI-188

    Protein-protein interaction databases

    BioGridi33080. 456 interactions.
    DIPiDIP-656N.
    IntActiP22147. 76 interactions.
    MINTiMINT-414332.
    STRINGi4932.YGL173C.

    Structurei

    3D structure databases

    ProteinModelPortaliP22147.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 5'-3' exonuclease family.Curated

    Phylogenomic databases

    eggNOGiCOG5049.
    GeneTreeiENSGT00670000098080.
    HOGENOMiHOG000160331.
    KOiK12618.
    OMAiNIFAYIE.
    OrthoDBiEOG71RXT2.

    Family and domain databases

    InterProiIPR027073. 5_3_exoribonuclease.
    IPR016494. 5_3_exoribonuclease_1.
    IPR004859. Put_53exo.
    [Graphical view]
    PANTHERiPTHR12341. PTHR12341. 1 hit.
    PfamiPF03159. XRN_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006743. Exonuclease_Xnr1. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P22147-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGIPKFFRYI SERWPMILQL IEGTQIPEFD NLYLDMNSIL HNCTHGNDDD     50
    VTKRLTEEEV FAKICTYIDH LFQTIKPKKI FYMAIDGVAP RAKMNQQRAR 100
    RFRTAMDAEK ALKKAIENGD EIPKGEPFDS NSITPGTEFM AKLTKNLQYF 150
    IHDKISNDSK WREVQIIFSG HEVPGEGEHK IMNFIRHLKS QKDFNQNTRH 200
    CIYGLDADLI MLGLSTHGPH FALLREEVTF GRRNSEKKSL EHQNFYLLHL 250
    SLLREYMELE FKEIADEMQF EYNFERILDD FILVMFVIGN DFLPNLPDLH 300
    LNKGAFPVLL QTFKEALLHT DGYINEHGKI NLKRLGVWLN YLSQFELLNF 350
    EKDDIDVEWF NKQLENISLE GERKRQRVGK KLLVKQQKKL IGSIKPWLME 400
    QLQEKLSPDL PDEEIPTLEL PKDLDMKDHL EFLKEFAFDL GLFITHSKSK 450
    GSYSLKMDLD SINPDETEEE FQNRVNSIRK TIKKYQNAII VEDKEELETE 500
    KTIYNERFER WKHEYYHDKL KFTTDSEEKV RDLAKDYVEG LQWVLYYYYR 550
    GCPSWSWYYP HHYAPRISDL AKGLDQDIEF DLSKPFTPFQ QLMAVLPERS 600
    KNLIPPAFRP LMYDEQSPIH DFYPAEVQLD KNGKTADWEA VVLISFVDEK 650
    RLIEAMQPYL RKLSPEEKTR NQFGKDLIYS FNPQVDNLYK SPLGGIFSDI 700
    EHNHCVEKEY ITIPLDSSEI RYGLLPNAKL GAEMLAGFPT LLSLPFTSSL 750
    EYNETMVFQQ PSKQQSMVLQ ITDIYKTNNV TLEDFSKRHL NKVIYTRWPY 800
    LRESKLVSLT DGKTIYEYQE SNDKKKFGFI TKPAETQDKK LFNSLKNSML 850
    RMYAKQKAVK IGPMEAIATV FPVTGLVRDS DGGYIKTFSP TPDYYPLQLV 900
    VESVVNEDER YKERGPIPIE EEFPLNSKVI FLGDYAYGGE TTIDGYSSDR 950
    RLKITVEKKF LDSEPTIGKE RLQMDHQAVK YYPSYIVSKN MHLHPLFLSK 1000
    ITSKFMITDA TGKHINVGIP VKFEARHQKV LGYARRNPRG WEYSNLTLNL 1050
    LKEYRQTFPD FFFRLSKVGN DIPVLEDLFP DTSTKDAMNL LDGIKQWLKY 1100
    VSSKFIAVSL ESDSLTKTSI AAVEDHIMKY AANIEGHERK QLAKVPREAV 1150
    LNPRSSFALL RSQKFDLGDR VVYIQDSGKV PIFSKGTVVG YTTLSSSLSI 1200
    QVLFDHEIVA GNNFGGRLRT NRGLGLDASF LLNITNRQFI YHSKASKKAL 1250
    EKKKQSNNRN NNTKTAHKTP SKQQSEEKLR KERAHDLLNF IKKDTNEKNS 1300
    ESVDNKSMGS QKDSKPAKKV LLKRPAQKSS ENVQVDLANF EKAPLDNPTV 1350
    AGSIFNAVAN QYSDGIGSNL NIPTPPHPMN VVGGPIPGAN DVADVGLPYN 1400
    IPPGFMTHPN GLHPLHPHQM PYPNMNGMSI PPPAPHGFGQ PISFPPPPPM 1450
    TNVSDQGSRI VVNEKESQDL KKFINGKQHS NGSTIGGETK NSRKGEIKPS 1500
    SGTNSTECQS PKSQSNAADR DNKKDEST 1528
    Length:1,528
    Mass (Da):175,460
    Last modified:August 1, 1991 - v1
    Checksum:i49C2EDAF73D3EB92
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M90097 Genomic DNA. Translation: AAA35219.1.
    X54717 Genomic DNA. Translation: CAA38520.1.
    M58367 Genomic DNA. Translation: AAA35036.1.
    M36725 Genomic DNA. Translation: AAA35125.1.
    X61181 Genomic DNA. Translation: CAA43487.1.
    X84705 Genomic DNA. Translation: CAA59180.1.
    Z72695 Genomic DNA. Translation: CAA96885.1.
    BK006941 Genomic DNA. Translation: DAA07940.1.
    PIRiS13743.
    RefSeqiNP_011342.1. NM_001181038.1.

    Genome annotation databases

    EnsemblFungiiYGL173C; YGL173C; YGL173C.
    GeneIDi852702.
    KEGGisce:YGL173C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M90097 Genomic DNA. Translation: AAA35219.1 .
    X54717 Genomic DNA. Translation: CAA38520.1 .
    M58367 Genomic DNA. Translation: AAA35036.1 .
    M36725 Genomic DNA. Translation: AAA35125.1 .
    X61181 Genomic DNA. Translation: CAA43487.1 .
    X84705 Genomic DNA. Translation: CAA59180.1 .
    Z72695 Genomic DNA. Translation: CAA96885.1 .
    BK006941 Genomic DNA. Translation: DAA07940.1 .
    PIRi S13743.
    RefSeqi NP_011342.1. NM_001181038.1.

    3D structure databases

    ProteinModelPortali P22147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33080. 456 interactions.
    DIPi DIP-656N.
    IntActi P22147. 76 interactions.
    MINTi MINT-414332.
    STRINGi 4932.YGL173C.

    Proteomic databases

    MaxQBi P22147.
    PaxDbi P22147.
    PeptideAtlasi P22147.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGL173C ; YGL173C ; YGL173C .
    GeneIDi 852702.
    KEGGi sce:YGL173C.

    Organism-specific databases

    CYGDi YGL173c.
    SGDi S000003141. XRN1.

    Phylogenomic databases

    eggNOGi COG5049.
    GeneTreei ENSGT00670000098080.
    HOGENOMi HOG000160331.
    KOi K12618.
    OMAi NIFAYIE.
    OrthoDBi EOG71RXT2.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30661-MONOMER.

    Miscellaneous databases

    NextBioi 972050.
    PROi P22147.

    Gene expression databases

    Genevestigatori P22147.

    Family and domain databases

    InterProi IPR027073. 5_3_exoribonuclease.
    IPR016494. 5_3_exoribonuclease_1.
    IPR004859. Put_53exo.
    [Graphical view ]
    PANTHERi PTHR12341. PTHR12341. 1 hit.
    Pfami PF03159. XRN_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006743. Exonuclease_Xnr1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "kem mutations affect nuclear fusion in Saccharomyces cerevisiae."
      Kim J., Ljungdahl P.O., Fink G.R.
      Genetics 126:799-812(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    2. "Molecular and genetic analysis of the gene encoding the Saccharomyces cerevisiae strand exchange protein Sep1."
      Tishkoff D., Johnson A.W., Kolodner R.D.
      Mol. Cell. Biol. 11:2593-2608(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    3. "Cloning and characterization of DST2, the gene for DNA strand transfer protein beta from Saccharomyces cerevisiae."
      Dykstra C.C., Kitada K., Clark A.B., Hamatake R.K., Sugino A.
      Mol. Cell. Biol. 11:2583-2592(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204626 / S288c / A364A.
    4. "Disruption of the gene XRN1, coding for a 5'-->3' exoribonuclease, restricts yeast cell growth."
      Larimer F.W., Stevens A.
      Gene 95:85-90(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "rar mutations which increase artificial chromosome stability in Saccharomyces cerevisiae identify transcription and recombination proteins."
      Kipling D., Tambini C., Kearsey S.E.
      Nucleic Acids Res. 19:1385-1391(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE.
    6. "The sequence of an 11.1 kb fragment on the left arm of Saccharomyces cerevisiae chromosome VII reveals six open reading frames including NSP49, KEM1 and four putative new genes."
      Bertani I., Coglievina M., Zaccaria P., Klima R., Bruschi C.V.
      Yeast 11:1187-1194(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    7. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    8. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    9. "Strand exchange protein 1 from Saccharomyces cerevisiae. A novel multifunctional protein that contains DNA strand exchange and exonuclease activities."
      Johnson A.W., Kolodner R.D.
      J. Biol. Chem. 266:14046-14054(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF EXONUCLEASE ACTIVITY.
    10. "Characterization of the XRN1 gene encoding a 5'-->3' exoribonuclease: sequence data and analysis of disparate protein and mRNA levels of gene-disrupted yeast cells."
      Larimer F.W., Hsu C.L., Maupin M.K., Stevens A.
      Gene 120:51-57(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF EXORIBONUCLEASE ACTIVITY.
    11. "The Sep1 strand exchange protein from Saccharomyces cerevisiae promotes a paranemic joint between homologous DNA molecules."
      Chen J., Kanaar R., Cozzarelli N.R.
      Genes Dev. 8:1356-1366(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "The activity of the Saccharomyces cerevisiae strand exchange protein 1 intrinsic exonuclease during joint molecule formation."
      Johnson A.W., Kolodner R.D.
      J. Biol. Chem. 269:3664-3672(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF EXONUCLEASE ACTIVITY DURING STRAND EXCHANGE.
    13. "Characterization of the interaction of Saccharomyces cerevisiae strand exchange protein 1 with DNA."
      Johnson A.W., Kolodner R.D.
      J. Biol. Chem. 269:3673-3681(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING PROPERTIES.
    14. "A multifunctional exonuclease from vegetative Schizosaccharomyces pombe cells exhibiting in vitro strand exchange activity."
      Kaeslin E., Heyer W.-D.
      J. Biol. Chem. 269:14094-14102(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF EXONUCLEASE AND STRAND EXCHANGE ACTIVITIES.
    15. "The yeast KEM1 gene encodes a nuclease specific for G4 tetraplex DNA: implication of in vivo functions for this novel DNA structure."
      Liu Z., Gilbert W.
      Cell 77:1083-1092(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF SPECIFICITY FOR G4 TETRAPLEX DNA.
    16. "A role of Sep1 (= Kem1, Xrn1) as a microtubule-associated protein in Saccharomyces cerevisiae."
      Interthal H., Bellocq C., Baehler J., Bashkirov V.I., Edelstein S.J., Heyer W.-D.
      EMBO J. 14:1057-1066(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH MICROTUBULES.
    17. "The sep1 mutant of Saccharomyces cerevisiae arrests in pachytene and is deficient in meiotic recombination."
      Tishkoff D.X., Rockmill B., Roeder G.S., Kolodner R.D.
      Genetics 139:495-509(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    18. "Regulation and intracellular localization of Saccharomyces cerevisiae strand exchange protein 1 (Sep1/Xrn1/Kem1), a multifunctional exonuclease."
      Heyer W.-D., Johnson A.W., Reinhart U., Kolodner R.D.
      Mol. Cell. Biol. 15:2728-2736(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    19. "Gene disruption of a G4-DNA-dependent nuclease in yeast leads to cellular senescence and telomere shortening."
      Liu Z., Lee A., Gilbert W.
      Proc. Natl. Acad. Sci. U.S.A. 92:6002-6006(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "Rat1p and Xrn1p are functionally interchangeable exoribonucleases that are restricted to and required in the nucleus and cytoplasm, respectively."
      Johnson A.W.
      Mol. Cell. Biol. 17:6122-6130(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Processing of the precursors to small nucleolar RNAs and rRNAs requires common components."
      Petfalski E., Dandekar T., Henry Y., Tollervey D.
      Mol. Cell. Biol. 18:1181-1189(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "Telomere length regulation and telomeric chromatin require the nonsense-mediated mRNA decay pathway."
      Lew J.E., Enomoto S., Berman J.
      Mol. Cell. Biol. 18:6121-6130(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "Mutational analysis of exoribonuclease I from Saccharomyces cerevisiae."
      Page A.M., Davis K., Molineux C., Kolodner R.D., Johnson A.W.
      Nucleic Acids Res. 26:3707-3716(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASN-37; HIS-41; ASP-86; GLY-87; LYS-93; GLN-97; ARG-101; GLU-178; CYS-201; LEU-592; TYR-710; TRP-798; GLU-1024; TYR-1043 AND SER-1197.
    24. "The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases of the exosome complex."
      Anderson J.S.J., Parker R.P.
      EMBO J. 17:1497-1506(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    25. "Active-site mutations in the Xrn1p exoribonuclease of Saccharomyces cerevisiae reveal a specific role in meiosis."
      Solinger J.A., Pascolini D., Heyer W.-D.
      Mol. Cell. Biol. 19:5930-5942(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-206 AND ASP-208.
    26. "The final step in the formation of 25S rRNA in Saccharomyces cerevisiae is performed by 5'->3' exonucleases."
      Geerlings T.H., Vos J.C., Raue H.A.
      RNA 6:1698-1703(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    27. "Upf1p, Nmd2p, and Upf3p regulate the decapping and exonucleolytic degradation of both nonsense-containing mRNAs and wild-type mRNAs."
      He F., Jacobson A.
      Mol. Cell. Biol. 21:1515-1530(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    28. "KEM1 is involved in filamentous growth of Saccharomyces cerevisiae."
      Kim J., Kim J.
      FEMS Microbiol. Lett. 216:33-38(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    29. "An mRNA surveillance mechanism that eliminates transcripts lacking termination codons."
      Frischmeyer P.A., van Hoof A., O'Donnell K., Guerrerio A.L., Parker R., Dietz H.C.
      Science 295:2258-2261(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    30. "Genome-wide analysis of mRNAs regulated by the nonsense-mediated and 5' to 3' mRNA decay pathways in yeast."
      He F., Li X., Spatrick P., Casillo R., Dong S., Jacobson A.
      Mol. Cell 12:1439-1452(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    31. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    32. "The Upf-dependent decay of wild-type PPR1 mRNA depends on its 5'-UTR and first 92 ORF nucleotides."
      Kebaara B., Nazarenus T., Taylor R., Forch A., Atkin A.L.
      Nucleic Acids Res. 31:3157-3165(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    33. "Initiation-mediated mRNA decay in yeast affects heat-shock mRNAs, and works through decapping and 5'-to-3' hydrolysis."
      Heikkinen H.L., Llewellyn S.A., Barnes C.A.
      Nucleic Acids Res. 31:4006-4016(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    34. "The roles of endonucleolytic cleavage and exonucleolytic digestion in the 5'-end processing of S. cerevisiae box C/D snoRNAs."
      Lee C.Y., Lee A., Chanfreau G.
      RNA 9:1362-1370(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    35. "Decapping and decay of messenger RNA occur in cytoplasmic processing bodies."
      Sheth U., Parker R.
      Science 300:805-808(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    36. "Deletion of OSH3 gene confers resistance against ISP-1 in Saccharomyces cerevisiae."
      Yano T., Inukai M., Isono F.
      Biochem. Biophys. Res. Commun. 315:228-234(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    37. "Posttranscriptional regulation of the karyogamy gene by Kem1p/Xrn1p exoribonuclease and Rok1p RNA helicase of Saccharomyces cerevisiae."
      Kim J., Jeon S., Yang Y.-S., Kim J.
      Biochem. Biophys. Res. Commun. 321:1032-1039(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    38. "RNase MRP cleaves the CLB2 mRNA to promote cell cycle progression: novel method of mRNA degradation."
      Gill T., Cai T., Aulds J., Wierzbicki S., Schmitt M.E.
      Mol. Cell. Biol. 24:945-953(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    39. "A role for KEM1 at the START of the cell cycle in Saccharomyces cerevisiae."
      Pathak R., Bogomolnaya L.M., Guo J., Polymenis M.
      Curr. Genet. 48:300-309(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    40. "Regulation and surveillance of normal and 3'-extended forms of the yeast aci-reductone dioxygenase mRNA by RNase III cleavage and exonucleolytic degradation."
      Zer C., Chanfreau G.
      J. Biol. Chem. 280:28997-29003(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    41. "Multiple RNA surveillance pathways limit aberrant expression of iron uptake mRNAs and prevent iron toxicity in S. cerevisiae."
      Lee A., Henras A.K., Chanfreau G.
      Mol. Cell 19:39-51(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    42. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    43. "Sodium-induced GCN4 expression controls the accumulation of the 5' to 3' RNA degradation inhibitor, 3'-phosphoadenosine 5'-phosphate."
      Todeschini A.-L., Condon C., Benard L.
      J. Biol. Chem. 281:3276-3282(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    44. "Determinants of Rbp1p localization in specific cytoplasmic mRNA-processing foci, P-bodies."
      Jang L.-T., Buu L.-M., Lee F.-J.S.
      J. Biol. Chem. 281:29379-29390(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    45. "Suppression of viral RNA recombination by a host exoribonuclease."
      Cheng C.-P., Serviene E., Nagy P.D.
      J. Virol. 80:2631-2640(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    46. "Virus-like particles of the Ty3 retrotransposon assemble in association with P-body components."
      Beliakova-Bethell N., Beckham C., Giddings T.H. Jr., Winey M., Parker R., Sandmeyer S.
      RNA 12:94-101(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    47. "Yeast transcripts cleaved by an internal ribozyme provide new insight into the role of the cap and poly(A) tail in translation and mRNA decay."
      Meaux S., Van Hoof A.
      RNA 12:1323-1337(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    48. "The sensitivity of yeast mutants to oleic acid implicates the peroxisome and other processes in membrane function."
      Lockshon D., Surface L.E., Kerr E.O., Kaeberlein M., Kennedy B.K.
      Genetics 175:77-91(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    49. "Respiratory deficiency mediates the regulation of CHO1-encoded phosphatidylserine synthase by mRNA stability in Saccharomyces cerevisiae."
      Choi H.-S., Carman G.M.
      J. Biol. Chem. 282:31217-31227(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    50. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    51. "Analysis of P-body assembly in Saccharomyces cerevisiae."
      Teixeira D., Parker R.
      Mol. Biol. Cell 18:2274-2287(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    52. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1510, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    53. "Degradation of several hypomodified mature tRNA species in Saccharomyces cerevisiae is mediated by Met22 and the 5'-3' exonucleases Rat1 and Xrn1."
      Chernyakov I., Whipple J.M., Kotelawala L., Grayhack E.J., Phizicky E.M.
      Genes Dev. 22:1369-1380(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    54. "Transcription in the nucleus and mRNA decay in the cytoplasm are coupled processes."
      Goler-Baron V., Selitrennik M., Barkai O., Haimovich G., Lotan R., Choder M.
      Genes Dev. 22:2022-2027(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    55. "Synthetic genetic array analysis in Saccharomyces cerevisiae provides evidence for an interaction between RAT8/DBP5 and genes encoding P-body components."
      Scarcelli J.J., Viggiano S., Hodge C.A., Heath C.V., Amberg D.C., Cole C.N.
      Genetics 179:1945-1955(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    56. "20S RNA narnavirus defies the antiviral activity of SKI1/XRN1 in Saccharomyces cerevisiae."
      Esteban R., Vega L., Fujimura T.
      J. Biol. Chem. 283:25812-25820(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    57. "The Cth2 ARE-binding protein recruits the Dhh1 helicase to promote the decay of succinate dehydrogenase SDH4 mRNA in response to iron deficiency."
      Pedro-Segura E., Vergara S.V., Rodriguez-Navarro S., Parker R., Thiele D.J., Puig S.
      J. Biol. Chem. 283:28527-28535(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    58. "The DEAD-box RNA helicase Ded1p affects and accumulates in Saccharomyces cerevisiae P-bodies."
      Beckham C., Hilliker A., Cziko A.-M., Noueiry A., Ramaswami M., Parker R.
      Mol. Biol. Cell 19:984-993(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    59. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1510, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    60. "S. cerevisiae Vts1p induces deadenylation-dependent transcript degradation and interacts with the Ccr4p-Pop2p-Not deadenylase complex."
      Rendl L.M., Bieman M.A., Smibert C.A.
      RNA 14:1328-1336(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    61. "Cordycepin interferes with 3' end formation in yeast independently of its potential to terminate RNA chain elongation."
      Holbein S., Wengi A., Decourty L., Freimoser F.M., Jacquier A., Dichtl B.
      RNA 15:837-849(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    62. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1506 AND SER-1510, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiXRN1_YEAST
    AccessioniPrimary (citable) accession number: P22147
    Secondary accession number(s): D6VTX9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 11700 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3