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P22147

- XRN1_YEAST

UniProt

P22147 - XRN1_YEAST

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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

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

Mg2+Note: 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. 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
Complete GO annotation...

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.
ReactomeiREACT_249345. mRNA decay by 5' to 3' exoribonuclease.

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
Complete GO annotation...

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. 459 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

        10         20         30         40         50
MGIPKFFRYI SERWPMILQL IEGTQIPEFD NLYLDMNSIL HNCTHGNDDD
60 70 80 90 100
VTKRLTEEEV FAKICTYIDH LFQTIKPKKI FYMAIDGVAP RAKMNQQRAR
110 120 130 140 150
RFRTAMDAEK ALKKAIENGD EIPKGEPFDS NSITPGTEFM AKLTKNLQYF
160 170 180 190 200
IHDKISNDSK WREVQIIFSG HEVPGEGEHK IMNFIRHLKS QKDFNQNTRH
210 220 230 240 250
CIYGLDADLI MLGLSTHGPH FALLREEVTF GRRNSEKKSL EHQNFYLLHL
260 270 280 290 300
SLLREYMELE FKEIADEMQF EYNFERILDD FILVMFVIGN DFLPNLPDLH
310 320 330 340 350
LNKGAFPVLL QTFKEALLHT DGYINEHGKI NLKRLGVWLN YLSQFELLNF
360 370 380 390 400
EKDDIDVEWF NKQLENISLE GERKRQRVGK KLLVKQQKKL IGSIKPWLME
410 420 430 440 450
QLQEKLSPDL PDEEIPTLEL PKDLDMKDHL EFLKEFAFDL GLFITHSKSK
460 470 480 490 500
GSYSLKMDLD SINPDETEEE FQNRVNSIRK TIKKYQNAII VEDKEELETE
510 520 530 540 550
KTIYNERFER WKHEYYHDKL KFTTDSEEKV RDLAKDYVEG LQWVLYYYYR
560 570 580 590 600
GCPSWSWYYP HHYAPRISDL AKGLDQDIEF DLSKPFTPFQ QLMAVLPERS
610 620 630 640 650
KNLIPPAFRP LMYDEQSPIH DFYPAEVQLD KNGKTADWEA VVLISFVDEK
660 670 680 690 700
RLIEAMQPYL RKLSPEEKTR NQFGKDLIYS FNPQVDNLYK SPLGGIFSDI
710 720 730 740 750
EHNHCVEKEY ITIPLDSSEI RYGLLPNAKL GAEMLAGFPT LLSLPFTSSL
760 770 780 790 800
EYNETMVFQQ PSKQQSMVLQ ITDIYKTNNV TLEDFSKRHL NKVIYTRWPY
810 820 830 840 850
LRESKLVSLT DGKTIYEYQE SNDKKKFGFI TKPAETQDKK LFNSLKNSML
860 870 880 890 900
RMYAKQKAVK IGPMEAIATV FPVTGLVRDS DGGYIKTFSP TPDYYPLQLV
910 920 930 940 950
VESVVNEDER YKERGPIPIE EEFPLNSKVI FLGDYAYGGE TTIDGYSSDR
960 970 980 990 1000
RLKITVEKKF LDSEPTIGKE RLQMDHQAVK YYPSYIVSKN MHLHPLFLSK
1010 1020 1030 1040 1050
ITSKFMITDA TGKHINVGIP VKFEARHQKV LGYARRNPRG WEYSNLTLNL
1060 1070 1080 1090 1100
LKEYRQTFPD FFFRLSKVGN DIPVLEDLFP DTSTKDAMNL LDGIKQWLKY
1110 1120 1130 1140 1150
VSSKFIAVSL ESDSLTKTSI AAVEDHIMKY AANIEGHERK QLAKVPREAV
1160 1170 1180 1190 1200
LNPRSSFALL RSQKFDLGDR VVYIQDSGKV PIFSKGTVVG YTTLSSSLSI
1210 1220 1230 1240 1250
QVLFDHEIVA GNNFGGRLRT NRGLGLDASF LLNITNRQFI YHSKASKKAL
1260 1270 1280 1290 1300
EKKKQSNNRN NNTKTAHKTP SKQQSEEKLR KERAHDLLNF IKKDTNEKNS
1310 1320 1330 1340 1350
ESVDNKSMGS QKDSKPAKKV LLKRPAQKSS ENVQVDLANF EKAPLDNPTV
1360 1370 1380 1390 1400
AGSIFNAVAN QYSDGIGSNL NIPTPPHPMN VVGGPIPGAN DVADVGLPYN
1410 1420 1430 1440 1450
IPPGFMTHPN GLHPLHPHQM PYPNMNGMSI PPPAPHGFGQ PISFPPPPPM
1460 1470 1480 1490 1500
TNVSDQGSRI VVNEKESQDL KKFINGKQHS NGSTIGGETK NSRKGEIKPS
1510 1520
SGTNSTECQS PKSQSNAADR DNKKDEST
Length:1,528
Mass (Da):175,460
Last modified:August 1, 1991 - v1
Checksum:i49C2EDAF73D3EB92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 459 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.
Reactomei REACT_249345. mRNA decay by 5' to 3' exoribonuclease.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 144 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