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Q9DAA6

- EXOS1_MOUSE

UniProt

Q9DAA6 - EXOS1_MOUSE

Protein

Exosome complex component CSL4

Gene

Exosc1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 100 (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. EXOSC1 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC6 and EXOSC8 By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: MGI
    2. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. 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 CSL4
    Alternative name(s):
    Exosome component 1
    Gene namesi
    Name:Exosc1
    Synonyms:Csl4
    OrganismiMus musculus (Mouse)Imported
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1913833. Exosc1.

    Subcellular locationi

    Nucleusnucleolus. Nucleus By similarity. Cytoplasm By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Exosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 195195Exosome complex component CSL4PRO_0000087128Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9DAA6.
    PaxDbiQ9DAA6.
    PRIDEiQ9DAA6.

    PTM databases

    PhosphoSiteiQ9DAA6.

    Expressioni

    Gene expression databases

    BgeeiQ9DAA6.
    CleanExiMM_EXOSC1.
    GenevestigatoriQ9DAA6.

    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 EXOSC5, EXOSC7 and EXOSC10 By similarity. Interacts with DDX60 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi211569. 2 interactions.
    STRINGi10090.ENSMUSP00000074756.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DAA6.
    SMRiQ9DAA6. Positions 6-185.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini66 – 14782S1 motifAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CSL4 family.Curated
    Contains 1 S1 motif domain.Curated

    Phylogenomic databases

    eggNOGiCOG1096.
    GeneTreeiENSGT00390000015287.
    HOGENOMiHOG000177330.
    HOVERGENiHBG051516.
    InParanoidiQ9DAA6.
    KOiK07573.
    OMAiFTHESSA.
    OrthoDBiEOG7V4B0J.
    PhylomeDBiQ9DAA6.
    TreeFamiTF316607.

    Family and domain databases

    InterProiIPR019495. EXOSC1.
    IPR025721. Exosome_cplx_N_dom.
    IPR012340. NA-bd_OB-fold.
    IPR022967. RNA-binding_domain_S1.
    [Graphical view]
    PfamiPF14382. ECR1_N. 1 hit.
    PF10447. EXOSC1. 1 hit.
    [Graphical view]
    SMARTiSM00316. S1. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9DAA6-1) [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

    MAPPVRYCIP GERLCNLEEG SPGSGTYTRH GYIFSSLAGC LMKTSENGAV    50
    PVVSVMRETE SQLLPDVGAV VTCKVSSINS RFAKVHILYV GSTPLKNAFR 100
    GTIRKEDIRA TEKDKVEIYK SFRPGDIVLA KVISLGDAQS NYLLTTAENE 150
    LGVVVAHSES GVQMVPISWC EMQCPKTHTK EFRKVARVQP EFLQT 195
    Length:195
    Mass (Da):21,424
    Last modified:June 1, 2001 - v1
    Checksum:i2F8D214B2B6A2953
    GO
    Isoform 2 (identifier: Q9DAA6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         76-116: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:154
    Mass (Da):16,794
    Checksum:i7FA6B8509060F16C
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei76 – 11641Missing in isoform 2. 1 PublicationVSP_004176Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002930 mRNA. Translation: BAB22465.1.
    AK006018 mRNA. Translation: BAB24368.1.
    BC024423 mRNA. Translation: AAH24423.1.
    CCDSiCCDS29816.1. [Q9DAA6-1]
    CCDS50436.1. [Q9DAA6-2]
    RefSeqiNP_001158033.1. NM_001164561.1. [Q9DAA6-2]
    NP_079920.1. NM_025644.4. [Q9DAA6-1]
    UniGeneiMm.289086.

    Genome annotation databases

    EnsembliENSMUST00000075280; ENSMUSP00000074756; ENSMUSG00000034321. [Q9DAA6-1]
    ENSMUST00000112123; ENSMUSP00000107751; ENSMUSG00000034321. [Q9DAA6-2]
    GeneIDi66583.
    KEGGimmu:66583.
    UCSCiuc008hmm.2. mouse. [Q9DAA6-1]
    uc008hmn.2. mouse. [Q9DAA6-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002930 mRNA. Translation: BAB22465.1 .
    AK006018 mRNA. Translation: BAB24368.1 .
    BC024423 mRNA. Translation: AAH24423.1 .
    CCDSi CCDS29816.1. [Q9DAA6-1 ]
    CCDS50436.1. [Q9DAA6-2 ]
    RefSeqi NP_001158033.1. NM_001164561.1. [Q9DAA6-2 ]
    NP_079920.1. NM_025644.4. [Q9DAA6-1 ]
    UniGenei Mm.289086.

    3D structure databases

    ProteinModelPortali Q9DAA6.
    SMRi Q9DAA6. Positions 6-185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211569. 2 interactions.
    STRINGi 10090.ENSMUSP00000074756.

    PTM databases

    PhosphoSitei Q9DAA6.

    Proteomic databases

    MaxQBi Q9DAA6.
    PaxDbi Q9DAA6.
    PRIDEi Q9DAA6.

    Protocols and materials databases

    DNASUi 66583.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000075280 ; ENSMUSP00000074756 ; ENSMUSG00000034321 . [Q9DAA6-1 ]
    ENSMUST00000112123 ; ENSMUSP00000107751 ; ENSMUSG00000034321 . [Q9DAA6-2 ]
    GeneIDi 66583.
    KEGGi mmu:66583.
    UCSCi uc008hmm.2. mouse. [Q9DAA6-1 ]
    uc008hmn.2. mouse. [Q9DAA6-2 ]

    Organism-specific databases

    CTDi 51013.
    MGIi MGI:1913833. Exosc1.

    Phylogenomic databases

    eggNOGi COG1096.
    GeneTreei ENSGT00390000015287.
    HOGENOMi HOG000177330.
    HOVERGENi HBG051516.
    InParanoidi Q9DAA6.
    KOi K07573.
    OMAi FTHESSA.
    OrthoDBi EOG7V4B0J.
    PhylomeDBi Q9DAA6.
    TreeFami TF316607.

    Enzyme and pathway databases

    Reactomei REACT_198696. KSRP destabilizes mRNA.

    Miscellaneous databases

    NextBioi 322064.
    PROi Q9DAA6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9DAA6.
    CleanExi MM_EXOSC1.
    Genevestigatori Q9DAA6.

    Family and domain databases

    InterProi IPR019495. EXOSC1.
    IPR025721. Exosome_cplx_N_dom.
    IPR012340. NA-bd_OB-fold.
    IPR022967. RNA-binding_domain_S1.
    [Graphical view ]
    Pfami PF14382. ECR1_N. 1 hit.
    PF10447. EXOSC1. 1 hit.
    [Graphical view ]
    SMARTi SM00316. S1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: 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] (ISOFORM 1).

    Entry informationi

    Entry nameiEXOS1_MOUSE
    AccessioniPrimary (citable) accession number: Q9DAA6
    Secondary accession number(s): Q9DCB9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 12, 2003
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 100 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