Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 193 (16 Oct 2019)
Sequence version 1 (01 Aug 1991)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

5'-3' exoribonuclease 1

Gene

XRN1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Miscellaneous

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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionExonuclease, Hydrolase, Nuclease, RNA-binding
Biological processKaryogamy, Nonsense-mediated mRNA decay, rRNA processing
LigandMagnesium

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-30661-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-450385 Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-SCE-450513 Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:XRN1
Synonyms:DST2, KEM1, RAR5, SEP1, SKI1
Ordered Locus Names:YGL173C
ORF Names:G1645
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome VII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YGL173C

Saccharomyces Genome Database

More...
SGDi
S000003141 XRN1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Microtubule

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi37N → D: Reduces strongly exonuclease activity. 1 Publication1
Mutagenesisi41H → R or D: Reduces strongly exonuclease activity. 1 Publication1
Mutagenesisi86D → G: Reduces strongly exonuclease activity. 1 Publication1
Mutagenesisi87G → D: Reduces strongly exonuclease activity. 1 Publication1
Mutagenesisi93K → M: Reduces strongly exonuclease activity. 1 Publication1
Mutagenesisi97Q → E or R: Reduces strongly exonuclease activity. 1 Publication1
Mutagenesisi101R → G: Reduces strongly exonuclease activity. 1 Publication1
Mutagenesisi176E → G: Reduces strongly exonuclease activity. 1
Mutagenesisi178E → D or G: Reduces strongly exonuclease activity. 1 Publication1
Mutagenesisi201C → Y or R: Reduces strongly exonuclease activity. 1 Publication1
Mutagenesisi206D → A: Abolishes exonuclease activity in vitro. 1 Publication1
Mutagenesisi208D → A: Abolishes exonuclease activity in vitro. 1 Publication1
Mutagenesisi592L → P: Reduces strongly exonuclease activity; when associated with Y-710. 1 Publication1
Mutagenesisi710Y → C: Reduces strongly exonuclease activity; when associated with P-592. 1 Publication1
Mutagenesisi798W → R: Reduces strongly exonuclease activity; when associated with D-1024; F-1043 and P-1197. 1 Publication1
Mutagenesisi1024E → D: Reduces strongly exonuclease activity; when associated with R-798; F-1043 and P-1197. 1 Publication1
Mutagenesisi1043Y → F: Reduces strongly exonuclease activity; when associated with R-798; D-1024 and P-1197. 1 Publication1
Mutagenesisi1197S → P: Reduces strongly exonuclease activity; when associated with R-798; D-1024 and F-1043. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000713951 – 15285'-3' exoribonuclease 1Add BLAST1528

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1506PhosphothreonineCombined sources1
Modified residuei1510PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P22147

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P22147

PRoteomics IDEntifications database

More...
PRIDEi
P22147

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P22147

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33080, 835 interactors

Database of interacting proteins

More...
DIPi
DIP-656N

Protein interaction database and analysis system

More...
IntActi
P22147, 119 interactors

Molecular INTeraction database

More...
MINTi
P22147

STRING: functional protein association networks

More...
STRINGi
4932.YGL173C

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P22147

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000160331

KEGG Orthology (KO)

More...
KOi
K12618

Identification of Orthologs from Complete Genome Data

More...
OMAi
YPAISQL

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.30.30, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027073 5_3_exoribonuclease
IPR016494 5_3_exoribonuclease_1
IPR004859 Put_53exo
IPR014722 Rib_L2_dom2
IPR041385 SH3_12
IPR040992 XRN1_D1
IPR041106 XRN1_D2_D3
IPR040486 Xrn1_D3
IPR041412 Xrn1_helical

The PANTHER Classification System

More...
PANTHERi
PTHR12341 PTHR12341, 1 hit
PTHR12341:SF7 PTHR12341:SF7, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18129 SH3_12, 1 hit
PF18332 XRN1_D1, 1 hit
PF18334 XRN1_D2_D3, 1 hit
PF18194 Xrn1_D3, 1 hit
PF17846 XRN_M, 1 hit
PF03159 XRN_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF006743 Exonuclease_Xnr1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i49C2EDAF73D3EB92
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
S13743

NCBI Reference Sequences

More...
RefSeqi
NP_011342.1, NM_001181038.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YGL173C_mRNA; YGL173C; YGL173C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852702

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGL173C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
PIRiS13743
RefSeqiNP_011342.1, NM_001181038.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6Q8Yelectron microscopy3.10z3-918[»]
SMRiP22147
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi33080, 835 interactors
DIPiDIP-656N
IntActiP22147, 119 interactors
MINTiP22147
STRINGi4932.YGL173C

PTM databases

iPTMnetiP22147

Proteomic databases

MaxQBiP22147
PaxDbiP22147
PRIDEiP22147

Genome annotation databases

EnsemblFungiiYGL173C_mRNA; YGL173C; YGL173C
GeneIDi852702
KEGGisce:YGL173C

Organism-specific databases

EuPathDBiFungiDB:YGL173C
SGDiS000003141 XRN1

Phylogenomic databases

HOGENOMiHOG000160331
KOiK12618
OMAiYPAISQL

Enzyme and pathway databases

BioCyciYEAST:G3O-30661-MONOMER
ReactomeiR-SCE-450385 Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-SCE-450513 Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P22147

Family and domain databases

Gene3Di2.30.30.30, 1 hit
InterProiView protein in InterPro
IPR027073 5_3_exoribonuclease
IPR016494 5_3_exoribonuclease_1
IPR004859 Put_53exo
IPR014722 Rib_L2_dom2
IPR041385 SH3_12
IPR040992 XRN1_D1
IPR041106 XRN1_D2_D3
IPR040486 Xrn1_D3
IPR041412 Xrn1_helical
PANTHERiPTHR12341 PTHR12341, 1 hit
PTHR12341:SF7 PTHR12341:SF7, 1 hit
PfamiView protein in Pfam
PF18129 SH3_12, 1 hit
PF18332 XRN1_D1, 1 hit
PF18334 XRN1_D2_D3, 1 hit
PF18194 Xrn1_D3, 1 hit
PF17846 XRN_M, 1 hit
PF03159 XRN_N, 1 hit
PIRSFiPIRSF006743 Exonuclease_Xnr1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiXRN1_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P22147
Secondary accession number(s): D6VTX9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: October 16, 2019
This is version 193 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again