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Q8IZH2

- XRN1_HUMAN

UniProt

Q8IZH2 - XRN1_HUMAN

Protein

5'-3' exoribonuclease 1

Gene

XRN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Major 5'-3' exoribonuclease involved in mRNA decay. Required for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA By similarity. Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS).By similarity1 Publication

    GO - Molecular functioni

    1. 5'-3' exonuclease activity Source: InterPro
    2. DNA binding Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
    2. gene expression Source: Reactome
    3. histone mRNA catabolic process Source: UniProtKB
    4. mRNA metabolic process Source: Reactome
    5. nuclear mRNA surveillance Source: UniProtKB
    6. nuclear-transcribed mRNA catabolic process Source: UniProtKB
    7. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    8. RNA metabolic process Source: Reactome
    9. rRNA catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Exonuclease, Hydrolase, Nuclease

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_20518. mRNA decay by 5' to 3' exoribonuclease.
    REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
    REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5'-3' exoribonuclease 1 (EC:3.1.13.-)
    Alternative name(s):
    Strand-exchange protein 1 homolog
    Gene namesi
    Name:XRN1
    Synonyms:SEP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:30654. XRN1.

    Subcellular locationi

    Cytoplasm 3 Publications
    Note: Discrete foci at the inner surface of the cell membrane.

    GO - Cellular componenti

    1. cytoplasmic mRNA processing body Source: Ensembl
    2. cytosol Source: Reactome
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA134878471.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 170617065'-3' exoribonuclease 1PRO_0000071392Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1348 – 13481PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8IZH2.
    PaxDbiQ8IZH2.
    PRIDEiQ8IZH2.

    PTM databases

    PhosphoSiteiQ8IZH2.

    Expressioni

    Tissue specificityi

    Expressed in heart, brain, pancreas, spleen, testis, osteogenic sarcoma (OGS) biopsy and primary cell lines.1 Publication

    Inductioni

    By GDNF/glial cell line-derived neurotrophic factor.1 Publication

    Gene expression databases

    ArrayExpressiQ8IZH2.
    BgeeiQ8IZH2.
    CleanExiHS_XRN1.
    GenevestigatoriQ8IZH2.

    Organism-specific databases

    HPAiHPA035005.
    HPA035006.

    Interactioni

    Subunit structurei

    Associates with alpha and beta tubulins By similarity. Found in a mRNP complex with UPF1, UPF2, UPF3B and XRN1. Interacts with ZC3HAV1 in an RNA-dependent manner. Interacts with DIS3L2.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi119970. 72 interactions.
    DIPiDIP-31174N.
    IntActiQ8IZH2. 25 interactions.
    STRINGi9606.ENSP00000264951.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IZH2.
    SMRiQ8IZH2. Positions 1-600.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5049.
    HOVERGENiHBG094164.
    InParanoidiQ8IZH2.
    KOiK12618.
    OMAiCKQRKSN.
    OrthoDBiEOG7S7SCW.
    PhylomeDBiQ8IZH2.
    TreeFamiTF105757.

    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.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IZH2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGVPKFYRWI SERYPCLSEV VKEHQIPEFD NLYLDMNGII HQCSHPNDDD     50
    VHFRISDDKI FTDIFHYLEV LFRIIKPRKV FFMAVDGVAP RAKMNQQRGR 100
    RFRSAKEAED KIKKAIEKGE TLPTEARFDS NCITPGTEFM ARLHEHLKYF 150
    VNMKISTDKS WQGVTIYFSG HETPGEGEHK IMEFIRSEKA KPDHDPNTRH 200
    CLYGLDADLI MLGLTSHEAH FSLLREEVRF GGKKTQRVCA PEETTFHLLH 250
    LSLMREYIDY EFSVLKEKIT FKYDIERIID DWILMGFLVG NDFIPHLPHL 300
    HINHDALPLL YGTYVTILPE LGGYINESGH LNLPRFEKYL VKLSDFDREH 350
    FSEVFVDLKW FESKVGNKYL NEAAGVAAEE ARNYKEKKKL KGQENSLCWT 400
    ALDKNEGEMI TSKDNLEDET EDDDLFETEF RQYKRTYYMT KMGVDVVSDD 450
    FLADQAACYV QAIQWILHYY YHGVQSWSWY YPYHYAPFLS DIHNISTLKI 500
    HFELGKPFKP FEQLLAVLPA ASKNLLPACY QHLMTNEDSP IIEYYPPDFK 550
    TDLNGKQQEW EAVVLIPFID EKRLLEAMET CNHSLKKEER KRNQHSECLM 600
    CWYDRDTEFI YPSPWPEKFP AIERCCTRYK IISLDAWRVD INKNKITRID 650
    QKALYFCGFP TLKHIRHKFF LKKSGVQVFQ QSSRGENMML EILVDAESDE 700
    LTVENVASSV LGKSVFVNWP HLEEARVVAV SDGETKFYLE EPPGTQKLYS 750
    GRTAPPSKVV HLGDKEQSNW AKEVQGISEH YLRRKGIIIN ETSAVVYAQL 800
    LTGRKYQINQ NGEVRLEKQW SKQVVPFVYQ TIVKDIRAFD SRFSNIKTLD 850
    DLFPLRSMVF MLGTPYYGCT GEVQDSGDVI TEGRIRVIFS IPCEPNLDAL 900
    IQNQHKYSIK YNPGYVLASR LGVSGYLVSR FTGSIFIGRG SRRNPHGDHK 950
    ANVGLNLKFN KKNEEVPGYT KKVGSEWMYS SAAEQLLAEY LERAPELFSY 1000
    IAKNSQEDVF YEDDIWPGEN ENGAEKVQEI ITWLKGHPVS TLSRSSCDLQ 1050
    ILDAAIVEKI EEEVEKCKQR KNNKKVRVTV KPHLLYRPLE QQHGVIPDRD 1100
    AEFCLFDRVV NVRENFSVPV GLRGTIIGIK GANREADVLF EVLFDEEFPG 1150
    GLTIRCSPGR GYRLPTSALV NLSHGSRSET GNQKLTAIVK PQPAVHQHSS 1200
    SSSVSSGHLG ALNHSPQSLF VPTQVPTKDD DEFCNIWQSL QGSGKMQYFQ 1250
    PTIQEKGAVL PQEISQVNQH HKSGFNDNSV KYQQRKHDPH RKFKEECKSP 1300
    KAECWSQKMS NKQPNSGIEN FLASLNISKE NEVQSSHHGE PPSEEHLSPQ 1350
    SFAMGTRMLK EILKIDGSNT VDHKNEIKQI ANEIPVSSNR RDEYGLPSQP 1400
    KQNKKLASYM NKPHSANEYH NVQSMDNMCW PAPSQIPPVS TPVTELSRIC 1450
    SLVGMPQPDF SFLRMPQTMT VCQVKLSNGL LVHGPQCHSE NEAKEKAALF 1500
    ALQQLGSLGM NFPLPSQVFA NYPSAVPPGT IPPAFPPPTG WDHYGSNYAL 1550
    GAANIMPSSS HLFGSMPWGP SVPVPGKPFH HTLYSGTMPM AGGIPGGVHN 1600
    QFIPLQVTKK RVANKKNFEN KEAQSSQATP VQTSQPDSSN IVKVSPRESS 1650
    SASLKSSPIA QPASSFQVET ASQGHSISHH KSTPISSSRR KSRKLAVNFG 1700
    VSKPSE 1706
    Length:1,706
    Mass (Da):194,107
    Last modified:March 1, 2003 - v1
    Checksum:iD06A76208DE78698
    GO
    Isoform 2 (identifier: Q8IZH2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1354-1354: M → MK
         1540-1552: Missing.

    Show »
    Length:1,694
    Mass (Da):192,843
    Checksum:i25AD7CD0191A4E05
    GO
    Isoform 3 (identifier: Q8IZH2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         449-459: DDFLADQAACY → EYVFANAFILK
         460-1706: Missing.

    Show »
    Length:459
    Mass (Da):53,818
    Checksum:i2C546FA5EDB81BC3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 481D → G in CAE45950. (PubMed:17974005)Curated
    Sequence conflicti55 – 551I → T in BAC04718. (PubMed:14702039)Curated
    Sequence conflicti113 – 1131K → E in CAH18332. (PubMed:17974005)Curated
    Sequence conflicti142 – 1421R → K in AAH48104. (PubMed:15489334)Curated
    Sequence conflicti148 – 1481K → E in CAH18332. (PubMed:17974005)Curated
    Sequence conflicti572 – 5721Missing in CAB63749. (PubMed:17974005)Curated
    Sequence conflicti722 – 7221L → I in CAE45950. (PubMed:17974005)Curated
    Sequence conflicti834 – 8341K → R in CAH18332. (PubMed:17974005)Curated
    Sequence conflicti1250 – 12501Q → R in CAH18332. (PubMed:17974005)Curated
    Sequence conflicti1463 – 14631L → F in CAE45950. (PubMed:17974005)Curated
    Sequence conflicti1686 – 16861S → P in CAH18332. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti674 – 6741S → G.
    Corresponds to variant rs35214510 [ dbSNP | Ensembl ].
    VAR_053000
    Natural varianti1259 – 12591V → A.
    Corresponds to variant rs35902661 [ dbSNP | Ensembl ].
    VAR_053001

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei449 – 45911DDFLADQAACY → EYVFANAFILK in isoform 3. 1 PublicationVSP_016692Add
    BLAST
    Alternative sequencei460 – 17061247Missing in isoform 3. 1 PublicationVSP_016693Add
    BLAST
    Alternative sequencei1354 – 13541M → MK in isoform 2. 1 PublicationVSP_016694
    Alternative sequencei1540 – 155213Missing in isoform 2. 1 PublicationVSP_016695Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY137776 mRNA. Translation: AAN11306.1.
    AL133623 mRNA. Translation: CAB63749.1.
    BX640905 mRNA. Translation: CAE45950.1.
    CR627396 mRNA. Translation: CAH10490.1.
    CR749518 mRNA. Translation: CAH18332.1.
    BC039314 mRNA. Translation: AAH39314.1.
    BC048104 mRNA. Translation: AAH48104.1.
    AK096177 mRNA. Translation: BAC04718.1.
    CCDSiCCDS3123.1. [Q8IZH2-1]
    CCDS63801.1. [Q8IZH2-2]
    PIRiT43461.
    RefSeqiNP_001269786.1. NM_001282857.1. [Q8IZH2-2]
    NP_001269788.1. NM_001282859.1. [Q8IZH2-3]
    NP_061874.3. NM_019001.4. [Q8IZH2-1]
    UniGeneiHs.435103.

    Genome annotation databases

    EnsembliENST00000264951; ENSP00000264951; ENSG00000114127. [Q8IZH2-1]
    ENST00000392981; ENSP00000376707; ENSG00000114127. [Q8IZH2-2]
    ENST00000463916; ENSP00000418404; ENSG00000114127. [Q8IZH2-3]
    GeneIDi54464.
    KEGGihsa:54464.
    UCSCiuc003eus.3. human. [Q8IZH2-1]
    uc003euu.3. human. [Q8IZH2-2]
    uc003euw.3. human. [Q8IZH2-3]

    Polymorphism databases

    DMDMi74714582.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY137776 mRNA. Translation: AAN11306.1 .
    AL133623 mRNA. Translation: CAB63749.1 .
    BX640905 mRNA. Translation: CAE45950.1 .
    CR627396 mRNA. Translation: CAH10490.1 .
    CR749518 mRNA. Translation: CAH18332.1 .
    BC039314 mRNA. Translation: AAH39314.1 .
    BC048104 mRNA. Translation: AAH48104.1 .
    AK096177 mRNA. Translation: BAC04718.1 .
    CCDSi CCDS3123.1. [Q8IZH2-1 ]
    CCDS63801.1. [Q8IZH2-2 ]
    PIRi T43461.
    RefSeqi NP_001269786.1. NM_001282857.1. [Q8IZH2-2 ]
    NP_001269788.1. NM_001282859.1. [Q8IZH2-3 ]
    NP_061874.3. NM_019001.4. [Q8IZH2-1 ]
    UniGenei Hs.435103.

    3D structure databases

    ProteinModelPortali Q8IZH2.
    SMRi Q8IZH2. Positions 1-600.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119970. 72 interactions.
    DIPi DIP-31174N.
    IntActi Q8IZH2. 25 interactions.
    STRINGi 9606.ENSP00000264951.

    PTM databases

    PhosphoSitei Q8IZH2.

    Polymorphism databases

    DMDMi 74714582.

    Proteomic databases

    MaxQBi Q8IZH2.
    PaxDbi Q8IZH2.
    PRIDEi Q8IZH2.

    Protocols and materials databases

    DNASUi 54464.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264951 ; ENSP00000264951 ; ENSG00000114127 . [Q8IZH2-1 ]
    ENST00000392981 ; ENSP00000376707 ; ENSG00000114127 . [Q8IZH2-2 ]
    ENST00000463916 ; ENSP00000418404 ; ENSG00000114127 . [Q8IZH2-3 ]
    GeneIDi 54464.
    KEGGi hsa:54464.
    UCSCi uc003eus.3. human. [Q8IZH2-1 ]
    uc003euu.3. human. [Q8IZH2-2 ]
    uc003euw.3. human. [Q8IZH2-3 ]

    Organism-specific databases

    CTDi 54464.
    GeneCardsi GC03M142025.
    HGNCi HGNC:30654. XRN1.
    HPAi HPA035005.
    HPA035006.
    MIMi 607994. gene.
    neXtProti NX_Q8IZH2.
    PharmGKBi PA134878471.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5049.
    HOVERGENi HBG094164.
    InParanoidi Q8IZH2.
    KOi K12618.
    OMAi CKQRKSN.
    OrthoDBi EOG7S7SCW.
    PhylomeDBi Q8IZH2.
    TreeFami TF105757.

    Enzyme and pathway databases

    Reactomei REACT_20518. mRNA decay by 5' to 3' exoribonuclease.
    REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
    REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

    Miscellaneous databases

    ChiTaRSi XRN1. human.
    GenomeRNAii 54464.
    NextBioi 56731.
    PROi Q8IZH2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IZH2.
    Bgeei Q8IZH2.
    CleanExi HS_XRN1.
    Genevestigatori Q8IZH2.

    Family and domain databases

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

    Publicationsi

    1. "Identification of human SEP1 as a glial cell line-derived neurotrophic factor-inducible protein and its expression in the nervous system."
      Shimoyama Y., Morikawa Y., Ichihara M., Kodama Y., Fukuda N., Hayashi H., Morinaga T., Iwashita T., Murakumo Y., Takahashi M.
      Neuroscience 121:899-906(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION BY GDNF, SUBCELLULAR LOCATION.
      Tissue: Neuroblastoma.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Fetal kidney, Small intestine and Testis.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain and Testis.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-473 (ISOFORMS 1/2).
      Tissue: Mesangial cell.
    5. "Cloning and characterization of human Sep1 (hSEP1) gene and cytoplasmic localization of its product."
      Sato Y., Shimamoto A., Shobuike T., Sugimoto M., Ikeda H., Kuroda S., Furuichi Y.
      DNA Res. 5:241-246(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 2), SUBCELLULAR LOCATION.
    6. "Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities."
      Lejeune F., Li X., Maquat L.E.
      Mol. Cell 12:675-687(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH UPF1; UPF2 AND UPF3B.
    7. "The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci."
      Ingelfinger D., Arndt-Jovin D.J., Luehrmann R., Achsel T.
      RNA 8:1489-1501(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. "The human homolog of yeast SEP1 is a novel candidate tumor suppressor gene in osteogenic sarcoma."
      Zhang K., Dion N., Fuchs B., Damron T., Gitelis S., Irwin R., O'Connor M., Schwartz H., Scully S.P., Rock M.G., Bolander M.E., Sarkar G.
      Gene 298:121-127(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: POTENTIAL TUMOR SUPPRESSION ROLE IN OSTEOGENIC SARCOMA, TISSUE SPECIFICITY.
    9. "Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'."
      Mullen T.E., Marzluff W.F.
      Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation."
      Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T., Gao G.
      Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZC3HAV1.
    13. "Exonuclease hDIS3L2 specifies an exosome-independent 3'-5' degradation pathway of human cytoplasmic mRNA."
      Lubas M., Damgaard C.K., Tomecki R., Cysewski D., Jensen T.H., Dziembowski A.
      EMBO J. 32:1855-1868(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DIS3L2.

    Entry informationi

    Entry nameiXRN1_HUMAN
    AccessioniPrimary (citable) accession number: Q8IZH2
    Secondary accession number(s): Q4G0S3
    , Q68D88, Q6AI24, Q6MZS8, Q86WS7, Q8N8U4, Q9UF39
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Down-regulated in OGS biopsy.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3