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Q9JHI7

- EXOS9_MOUSE

UniProt

Q9JHI7 - EXOS9_MOUSE

Protein

Exosome complex component RRP45

Gene

Exosc9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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. EXOSC9 binds to ARE-containing RNAs By similarity.By similarity

    GO - Molecular functioni

    1. AU-rich element binding Source: Ensembl
    2. exonuclease activity Source: UniProtKB-KW

    GO - Biological processi

    1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Ensembl
    2. nuclear mRNA surveillance Source: Ensembl
    3. nuclear polyadenylation-dependent rRNA catabolic process Source: Ensembl
    4. positive regulation of cell growth Source: Ensembl
    5. rRNA processing Source: UniProtKB-KW

    Keywords - Molecular functioni

    Exonuclease, Hydrolase, Nuclease

    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 RRP45
    Alternative name(s):
    Autoantigen PM/Scl 1
    Exosome component 9
    P75 polymyositis-scleroderma overlap syndrome-associated autoantigen
    Polymyositis/scleroderma autoantigen 1
    Polymyositis/scleroderma autoantigen 75 kDa
    Short name:
    PM/Scl-75
    Gene namesi
    Name:Exosc9
    Synonyms:Pmscl1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1355319. Exosc9.

    Subcellular locationi

    Cytoplasm By similarity. Nucleusnucleolus By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. exosome (RNase complex) Source: UniProtKB
    3. nucleolus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Exosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 438438Exosome complex component RRP45PRO_0000139972Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei297 – 2971N6-acetyllysineBy similarity
    Modified residuei306 – 3061PhosphoserineBy similarity
    Modified residuei393 – 3931PhosphoserineBy similarity
    Modified residuei395 – 3951PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9JHI7.
    PaxDbiQ9JHI7.
    PRIDEiQ9JHI7.

    PTM databases

    PhosphoSiteiQ9JHI7.

    Expressioni

    Gene expression databases

    BgeeiQ9JHI7.
    CleanExiMM_EXOSC9.
    GenevestigatoriQ9JHI7.

    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 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JHI7.
    SMRiQ9JHI7. Positions 2-278.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RNase PH family.Curated

    Phylogenomic databases

    eggNOGiCOG2123.
    GeneTreeiENSGT00530000063093.
    HOGENOMiHOG000229504.
    HOVERGENiHBG051523.
    InParanoidiQ9JHI7.
    KOiK03678.
    OMAiKMDTGVE.
    OrthoDBiEOG7X9G70.
    PhylomeDBiQ9JHI7.
    TreeFamiTF300092.

    Family and domain databases

    InterProiIPR001247. ExoRNase_PH_dom1.
    IPR015847. ExoRNase_PH_dom2.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view]
    PfamiPF01138. RNase_PH. 1 hit.
    PF03725. RNase_PH_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 2 hits.
    SSF55666. SSF55666. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9JHI7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKETPLSNCE RRFLLRAIEE KKRLDGRQTY DYRNIRISFG TDYGCCIVEL    50
    GKTRVLGQVS CELVSPKLNR ATEGILFFNL ELSQMAAPAF EPGRQSDLLV 100
    KLNRLLERCL RNSKCIDTES LCVVAGEKVW QIRVDLHLLN HDGNIIDAAS 150
    IAAIVALCHF RRPDVSVQGE EVTLYTPEER DPVPLSIHHM PICVSFAFFQ 200
    QGTYLLVDPN EREERVMDGL LVIAMNKHRE ICTIQSSGGI MLLKDQVFRC 250
    SKIAGVKVAE ITELIQKALE NDQRVRKEGG KFGFAESIAN QRITAFKMET 300
    APIDTSNIEE RAEEIIAEAE PPPEVVSQPV LWTPGTAQIG DGIENSWGDL 350
    EDSEKEEEEE EGGIDEAVIL DDTKMDTGEV SDIGSQGAPI VLSDSEEEEM 400
    IILEPEKNPK KIRAQTSANQ KAPSKGQGKR KKKKRTAN 438
    Length:438
    Mass (Da):48,937
    Last modified:October 1, 2000 - v1
    Checksum:i7AAE63DBF12F5149
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF152841 mRNA. Translation: AAF73218.1.
    AF152842 mRNA. Translation: AAF73219.1.
    BC005622 mRNA. Translation: AAH05622.1.
    BC052156 mRNA. Translation: AAH52156.1.
    AK011636 mRNA. Translation: BAB27749.1.
    CCDSiCCDS17312.1.
    RefSeqiNP_062266.1. NM_019393.2.
    UniGeneiMm.116711.

    Genome annotation databases

    EnsembliENSMUST00000029269; ENSMUSP00000029269; ENSMUSG00000027714.
    GeneIDi50911.
    KEGGimmu:50911.
    UCSCiuc008ozm.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF152841 mRNA. Translation: AAF73218.1 .
    AF152842 mRNA. Translation: AAF73219.1 .
    BC005622 mRNA. Translation: AAH05622.1 .
    BC052156 mRNA. Translation: AAH52156.1 .
    AK011636 mRNA. Translation: BAB27749.1 .
    CCDSi CCDS17312.1.
    RefSeqi NP_062266.1. NM_019393.2.
    UniGenei Mm.116711.

    3D structure databases

    ProteinModelPortali Q9JHI7.
    SMRi Q9JHI7. Positions 2-278.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9JHI7.

    Proteomic databases

    MaxQBi Q9JHI7.
    PaxDbi Q9JHI7.
    PRIDEi Q9JHI7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029269 ; ENSMUSP00000029269 ; ENSMUSG00000027714 .
    GeneIDi 50911.
    KEGGi mmu:50911.
    UCSCi uc008ozm.1. mouse.

    Organism-specific databases

    CTDi 5393.
    MGIi MGI:1355319. Exosc9.

    Phylogenomic databases

    eggNOGi COG2123.
    GeneTreei ENSGT00530000063093.
    HOGENOMi HOG000229504.
    HOVERGENi HBG051523.
    InParanoidi Q9JHI7.
    KOi K03678.
    OMAi KMDTGVE.
    OrthoDBi EOG7X9G70.
    PhylomeDBi Q9JHI7.
    TreeFami TF300092.

    Enzyme and pathway databases

    Reactomei REACT_198696. KSRP destabilizes mRNA.

    Miscellaneous databases

    NextBioi 307895.
    PROi Q9JHI7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9JHI7.
    CleanExi MM_EXOSC9.
    Genevestigatori Q9JHI7.

    Family and domain databases

    InterProi IPR001247. ExoRNase_PH_dom1.
    IPR015847. ExoRNase_PH_dom2.
    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. 2 hits.
    SSF55666. SSF55666. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Structure and localization of mouse Pmscl1 and Pmscl2 genes."
      Bliskovski V., Liddell R., Ramsay E.S., Miller M.J., Mock B.A.
      Genomics 64:106-110(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Brain and Spleen.
    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].
      Tissue: Embryo and Mammary gland.
    3. "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] OF 1-395.
      Strain: C57BL/6J.
      Tissue: Embryo.

    Entry informationi

    Entry nameiEXOS9_MOUSE
    AccessioniPrimary (citable) accession number: Q9JHI7
    Secondary accession number(s): Q9CSZ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 106 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