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Q9CRA8

- EXOS5_MOUSE

UniProt

Q9CRA8 - EXOS5_MOUSE

Protein

Exosome complex component RRP46

Gene

Exosc5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes By similarity.By similarity

    GO - Molecular functioni

    1. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. defense response to virus Source: Ensembl
    2. DNA deamination Source: Ensembl
    3. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Ensembl
    4. RNA catabolic process Source: MGI
    5. rRNA processing Source: UniProtKB-KW

    Keywords - Biological processi

    rRNA processing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198696. KSRP destabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exosome complex component RRP46
    Alternative name(s):
    Exosome component 5
    Ribosomal RNA-processing protein 46
    Gene namesi
    Name:Exosc5
    Synonyms:D7Wsu180e, Rrp46
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:107889. Exosc5.

    Subcellular locationi

    Nucleusnucleolus By similarity. Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. exosome (RNase complex) Source: UniProtKB
    3. nucleolus Source: UniProtKB-SubCell
    4. transcriptionally active chromatin Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Exosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 235235Exosome complex component RRP46PRO_0000139976Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9CRA8.
    PRIDEiQ9CRA8.

    PTM databases

    PhosphoSiteiQ9CRA8.

    Expressioni

    Gene expression databases

    BgeeiQ9CRA8.
    CleanExiMM_EXOSC5.
    GenevestigatoriQ9CRA8.

    Interactioni

    Subunit structurei

    Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure. Interacts with EXOSC1. Interacts with GTPBP1 By similarity. Interacts with ZC3HAV1 By similarity. Interacts with DDX17 only in the presence of ZC3HAV1 in an RNA-independent manner By similarity.By similarity

    Protein-protein interaction databases

    BioGridi205707. 1 interaction.
    IntActiQ9CRA8. 3 interactions.
    MINTiMINT-1765755.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CRA8.
    SMRiQ9CRA8. Positions 26-234.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RNase PH family.Curated

    Phylogenomic databases

    eggNOGiCOG0689.
    GeneTreeiENSGT00550000075002.
    HOGENOMiHOG000229515.
    HOVERGENiHBG051520.
    InParanoidiQ9CRA8.
    KOiK12590.
    OMAiTCEASLL.
    OrthoDBiEOG7P8P90.
    PhylomeDBiQ9CRA8.
    TreeFamiTF315920.

    Family and domain databases

    Gene3Di3.30.230.70. 1 hit.
    InterProiIPR001247. ExoRNase_PH_dom1.
    IPR015847. ExoRNase_PH_dom2.
    IPR027408. PNPase/RNase_PH_dom.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view]
    PfamiPF01138. RNase_PH. 1 hit.
    PF03725. RNase_PH_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55666. SSF55666. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9CRA8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGAKRADAN LLTDTGTESS PRSPVCSLRH FACEQNLLSR PDGSASFLQG    50
    DTSVLAGVYG PAEVKVSKEI FNKATLEVIL RPKIGLPGVA EKSRERLVRN 100
    TCEAVVLGAL HPRTSITVVL QVVSDAGSLL ACCLNAACMA LVDAGVPMRA 150
    LFCGVTCALD SDGNLVLDPT TKQEKEARAI LTFALDSAEQ KLLMSTTKGL 200
    YSDAELQQCL AAAQAASQHI FRFYRESLQR RYSKS 235
    Length:235
    Mass (Da):25,194
    Last modified:June 1, 2001 - v1
    Checksum:i08752915141CF65D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111L → V in AAH34358. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK007372 mRNA. Translation: BAB24993.1.
    AK006475 mRNA. Translation: BAB24607.1.
    BC034358 mRNA. Translation: AAH34358.1.
    CCDSiCCDS20990.1.
    RefSeqiNP_613052.1. NM_138586.3.
    UniGeneiMm.207484.
    Mm.27853.

    Genome annotation databases

    EnsembliENSMUST00000079634; ENSMUSP00000078580; ENSMUSG00000061286.
    GeneIDi27998.
    KEGGimmu:27998.
    UCSCiuc009fti.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK007372 mRNA. Translation: BAB24993.1 .
    AK006475 mRNA. Translation: BAB24607.1 .
    BC034358 mRNA. Translation: AAH34358.1 .
    CCDSi CCDS20990.1.
    RefSeqi NP_613052.1. NM_138586.3.
    UniGenei Mm.207484.
    Mm.27853.

    3D structure databases

    ProteinModelPortali Q9CRA8.
    SMRi Q9CRA8. Positions 26-234.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 205707. 1 interaction.
    IntActi Q9CRA8. 3 interactions.
    MINTi MINT-1765755.

    PTM databases

    PhosphoSitei Q9CRA8.

    Proteomic databases

    PaxDbi Q9CRA8.
    PRIDEi Q9CRA8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000079634 ; ENSMUSP00000078580 ; ENSMUSG00000061286 .
    GeneIDi 27998.
    KEGGi mmu:27998.
    UCSCi uc009fti.2. mouse.

    Organism-specific databases

    CTDi 56915.
    MGIi MGI:107889. Exosc5.

    Phylogenomic databases

    eggNOGi COG0689.
    GeneTreei ENSGT00550000075002.
    HOGENOMi HOG000229515.
    HOVERGENi HBG051520.
    InParanoidi Q9CRA8.
    KOi K12590.
    OMAi TCEASLL.
    OrthoDBi EOG7P8P90.
    PhylomeDBi Q9CRA8.
    TreeFami TF315920.

    Enzyme and pathway databases

    Reactomei REACT_198696. KSRP destabilizes mRNA.

    Miscellaneous databases

    NextBioi 306496.
    PROi Q9CRA8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9CRA8.
    CleanExi MM_EXOSC5.
    Genevestigatori Q9CRA8.

    Family and domain databases

    Gene3Di 3.30.230.70. 1 hit.
    InterProi IPR001247. ExoRNase_PH_dom1.
    IPR015847. ExoRNase_PH_dom2.
    IPR027408. PNPase/RNase_PH_dom.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view ]
    Pfami PF01138. RNase_PH. 1 hit.
    PF03725. RNase_PH_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    SSF55666. SSF55666. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Pancreas and Testis.
    2. "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].
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiEXOS5_MOUSE
    AccessioniPrimary (citable) accession number: Q9CRA8
    Secondary accession number(s): Q8K1J2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3