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P22147 (XRN1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:XRN1
Synonyms:DST2, KEM1, RAR5, SEP1, SKI1
Ordered Locus Names:YGL173C
ORF Names:G1645
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1528 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.11 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.32 Ref.33 Ref.34 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.44 Ref.45 Ref.46 Ref.47 Ref.49 Ref.53 Ref.54 Ref.56 Ref.57 Ref.58 Ref.60 Ref.61

Cofactor

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 regulation

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. Ref.43

Subcellular location

Cytoplasm. Cytoplasmperinuclear region. CytoplasmP-body Ref.18 Ref.35 Ref.46 Ref.51 Ref.55 Ref.58.

Disruption phenotype

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. Ref.5 Ref.17 Ref.48

Miscellaneous

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

Sequence similarities

Belongs to the 5'-3' exonuclease family.

Ontologies

Keywords
   Biological processKaryogamy
Nonsense-mediated mRNA decay
rRNA processing
   Cellular componentCytoplasm
Microtubule
   LigandMagnesium
RNA-binding
   Molecular functionExonuclease
Hydrolase
Nuclease
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA phosphodiester bond hydrolysis, exonucleolytic

Inferred from direct assay PubMed 3545079. Source: GOC

karyogamy

Inferred from electronic annotation. Source: UniProtKB-KW

nonfunctional rRNA decay

Inferred from mutant phenotype PubMed 19481524. Source: SGD

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from mutant phenotype PubMed 10848586. Source: SGD

positive regulation of transcription elongation from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 23706738. Source: SGD

positive regulation of transcription initiation from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 23706738. Source: SGD

rRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

traversing start control point of mitotic cell cycle

Inferred from mutant phenotype Ref.39. Source: SGD

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 23706738. Source: SGD

cytoplasmic mRNA processing body

Inferred from direct assay Ref.35. Source: SGD

cytoplasmic stress granule

Inferred from direct assay PubMed 23222640. Source: SGD

cytosol

Traceable author statement. Source: Reactome

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from direct assay PubMed 23706738. Source: SGD

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function5'-3' exoribonuclease activity

Inferred from direct assay PubMed 3545079. Source: SGD

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from direct assay PubMed 23706738. Source: SGD

protein binding

Inferred from physical interaction PubMed 10900456PubMed 16429126. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LSM4P400703EBI-9642,EBI-188

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152815285'-3' exoribonuclease 1
PRO_0000071395

Amino acid modifications

Modified residue15061Phosphothreonine Ref.62
Modified residue15101Phosphoserine Ref.52 Ref.59 Ref.62

Experimental info

Mutagenesis371N → D: Reduces strongly exonuclease activity. Ref.23
Mutagenesis411H → R or D: Reduces strongly exonuclease activity. Ref.23
Mutagenesis861D → G: Reduces strongly exonuclease activity. Ref.23
Mutagenesis871G → D: Reduces strongly exonuclease activity. Ref.23
Mutagenesis931K → M: Reduces strongly exonuclease activity. Ref.23
Mutagenesis971Q → E or R: Reduces strongly exonuclease activity. Ref.23
Mutagenesis1011R → G: Reduces strongly exonuclease activity. Ref.23
Mutagenesis1761E → G: Reduces strongly exonuclease activity.
Mutagenesis1781E → D or G: Reduces strongly exonuclease activity. Ref.23
Mutagenesis2011C → Y or R: Reduces strongly exonuclease activity. Ref.23
Mutagenesis2061D → A: Abolishes exonuclease activity in vitro. Ref.25
Mutagenesis2081D → A: Abolishes exonuclease activity in vitro. Ref.25
Mutagenesis5921L → P: Reduces strongly exonuclease activity; when associated with Y-710. Ref.23
Mutagenesis7101Y → C: Reduces strongly exonuclease activity; when associated with P-592. Ref.23
Mutagenesis7981W → R: Reduces strongly exonuclease activity; when associated with D-1024; F-1043 and P-1197. Ref.23
Mutagenesis10241E → D: Reduces strongly exonuclease activity; when associated with R-798; F-1043 and P-1197. Ref.23
Mutagenesis10431Y → F: Reduces strongly exonuclease activity; when associated with R-798; D-1024 and P-1197. Ref.23
Mutagenesis11971S → P: Reduces strongly exonuclease activity; when associated with R-798; D-1024 and F-1043. Ref.23

Sequences

Sequence LengthMass (Da)Tools
P22147 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 49C2EDAF73D3EB92

FASTA1,528175,460
        10         20         30         40         50         60 
MGIPKFFRYI SERWPMILQL IEGTQIPEFD NLYLDMNSIL HNCTHGNDDD VTKRLTEEEV 

        70         80         90        100        110        120 
FAKICTYIDH LFQTIKPKKI FYMAIDGVAP RAKMNQQRAR RFRTAMDAEK ALKKAIENGD 

       130        140        150        160        170        180 
EIPKGEPFDS NSITPGTEFM AKLTKNLQYF IHDKISNDSK WREVQIIFSG HEVPGEGEHK 

       190        200        210        220        230        240 
IMNFIRHLKS QKDFNQNTRH CIYGLDADLI MLGLSTHGPH FALLREEVTF GRRNSEKKSL 

       250        260        270        280        290        300 
EHQNFYLLHL SLLREYMELE FKEIADEMQF EYNFERILDD FILVMFVIGN DFLPNLPDLH 

       310        320        330        340        350        360 
LNKGAFPVLL QTFKEALLHT DGYINEHGKI NLKRLGVWLN YLSQFELLNF EKDDIDVEWF 

       370        380        390        400        410        420 
NKQLENISLE GERKRQRVGK KLLVKQQKKL IGSIKPWLME QLQEKLSPDL PDEEIPTLEL 

       430        440        450        460        470        480 
PKDLDMKDHL EFLKEFAFDL GLFITHSKSK GSYSLKMDLD SINPDETEEE FQNRVNSIRK 

       490        500        510        520        530        540 
TIKKYQNAII VEDKEELETE KTIYNERFER WKHEYYHDKL KFTTDSEEKV RDLAKDYVEG 

       550        560        570        580        590        600 
LQWVLYYYYR GCPSWSWYYP HHYAPRISDL AKGLDQDIEF DLSKPFTPFQ QLMAVLPERS 

       610        620        630        640        650        660 
KNLIPPAFRP LMYDEQSPIH DFYPAEVQLD KNGKTADWEA VVLISFVDEK RLIEAMQPYL 

       670        680        690        700        710        720 
RKLSPEEKTR NQFGKDLIYS FNPQVDNLYK SPLGGIFSDI EHNHCVEKEY ITIPLDSSEI 

       730        740        750        760        770        780 
RYGLLPNAKL GAEMLAGFPT LLSLPFTSSL EYNETMVFQQ PSKQQSMVLQ ITDIYKTNNV 

       790        800        810        820        830        840 
TLEDFSKRHL NKVIYTRWPY LRESKLVSLT DGKTIYEYQE SNDKKKFGFI TKPAETQDKK 

       850        860        870        880        890        900 
LFNSLKNSML RMYAKQKAVK IGPMEAIATV FPVTGLVRDS DGGYIKTFSP TPDYYPLQLV 

       910        920        930        940        950        960 
VESVVNEDER YKERGPIPIE EEFPLNSKVI FLGDYAYGGE TTIDGYSSDR RLKITVEKKF 

       970        980        990       1000       1010       1020 
LDSEPTIGKE RLQMDHQAVK YYPSYIVSKN MHLHPLFLSK ITSKFMITDA TGKHINVGIP 

      1030       1040       1050       1060       1070       1080 
VKFEARHQKV LGYARRNPRG WEYSNLTLNL LKEYRQTFPD FFFRLSKVGN DIPVLEDLFP 

      1090       1100       1110       1120       1130       1140 
DTSTKDAMNL LDGIKQWLKY VSSKFIAVSL ESDSLTKTSI AAVEDHIMKY AANIEGHERK 

      1150       1160       1170       1180       1190       1200 
QLAKVPREAV LNPRSSFALL RSQKFDLGDR VVYIQDSGKV PIFSKGTVVG YTTLSSSLSI 

      1210       1220       1230       1240       1250       1260 
QVLFDHEIVA GNNFGGRLRT NRGLGLDASF LLNITNRQFI YHSKASKKAL EKKKQSNNRN 

      1270       1280       1290       1300       1310       1320 
NNTKTAHKTP SKQQSEEKLR KERAHDLLNF IKKDTNEKNS ESVDNKSMGS QKDSKPAKKV 

      1330       1340       1350       1360       1370       1380 
LLKRPAQKSS ENVQVDLANF EKAPLDNPTV AGSIFNAVAN QYSDGIGSNL NIPTPPHPMN 

      1390       1400       1410       1420       1430       1440 
VVGGPIPGAN DVADVGLPYN IPPGFMTHPN GLHPLHPHQM PYPNMNGMSI PPPAPHGFGQ 

      1450       1460       1470       1480       1490       1500 
PISFPPPPPM TNVSDQGSRI VVNEKESQDL KKFINGKQHS NGSTIGGETK NSRKGEIKPS 

      1510       1520 
SGTNSTECQS PKSQSNAADR DNKKDEST 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS13743.
RefSeqNP_011342.1. NM_001181038.1.

3D structure databases

ProteinModelPortalP22147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33080. 456 interactions.
DIPDIP-656N.
IntActP22147. 76 interactions.
MINTMINT-414332.
STRING4932.YGL173C.

Proteomic databases

MaxQBP22147.
PaxDbP22147.
PeptideAtlasP22147.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL173C; YGL173C; YGL173C.
GeneID852702.
KEGGsce:YGL173C.

Organism-specific databases

CYGDYGL173c.
SGDS000003141. XRN1.

Phylogenomic databases

eggNOGCOG5049.
GeneTreeENSGT00670000098080.
HOGENOMHOG000160331.
KOK12618.
OMANIFAYIE.
OrthoDBEOG71RXT2.

Enzyme and pathway databases

BioCycYEAST:G3O-30661-MONOMER.

Gene expression databases

GenevestigatorP22147.

Family and domain databases

InterProIPR027073. 5_3_exoribonuclease.
IPR016494. 5_3_exoribonuclease_1.
IPR004859. Put_53exo.
[Graphical view]
PANTHERPTHR12341. PTHR12341. 1 hit.
PfamPF03159. XRN_N. 1 hit.
[Graphical view]
PIRSFPIRSF006743. Exonuclease_Xnr1. 1 hit.
ProtoNetSearch...

Other

NextBio972050.
PROP22147.

Entry information

Entry nameXRN1_YEAST
AccessionPrimary (citable) accession number: P22147
Secondary accession number(s): D6VTX9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: July 9, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families