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Index > Protein center > EXOSC6(Gene name) > Human
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  • EXOSC6 (Gene name),
  • Exosome complex component MTR3 (Protein name ),  EXOS6_HUMAN from NCBI database.
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  • General Annotation
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  • Antigen Annotation
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  • Gene name:
    EXOSC6(MTR3);
    Protein name:
    Exosome complex component MTR3;
    Alternative:
    mRNA transport regulator 3 homolog(hMtr3);Exosome component 6;p11;
    Organism:
    Human (Homo sapiens). 
    General Annotation
    Sub Unit:
    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.
    Function:
    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 anti-sense 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.
    Subcellular Location:
    Cytoplasm Nucleus nucleolus Nucleus
    Protein Attributes:
    Sequence length:
    272
    Sequence:
    50:
    MPGDHRRIRG | PEESQPPQLY | AADEEEAPGT | RDPTRLRPVY | ARAGLLSQAK | 
    100:
    GSAYLEAGGT | KVLCAVSGPR | QAEGGERGGG | PAGAGGEAPA | ALRGRLLCDF | 
    150:
    RRAPFAGRRR | RAPPGGCEER | ELALALQEAL | EPAVRLGRYP | RAQLEVSALL | 
    200:
    LEDGGSALAA | ALTAAALALA | DAGVEMYDLV | VGCGLSLAPG | PAPTWLLDPT | 
    250:
    RLEEERAAAG | LTVALMPVLN | QVAGLLGSGE | GGLTESWAEA | VRLGLEGCQR | 
    272:
    LYPVLQQSLV | RAARRRGAAA | QP
    3D Structure:
    N/A
    Predicted Eptitope:
    Please Sign in.
    EIAab Sequence  Vaild Sequence:
    Please Sign in.
    Related Databases
    UniGene:
    String:
    Pfam:
    MIM:
    SMR:
    Uniprot:
     
    FOR
    ELISA Kit for Human Exosome complex component MTR3
    ELISA Kit for Human Exosome complex component MTR3
    CLIA Kit for Human Exosome complex component MTR3
    CLIA Kit for Human Exosome complex component MTR3
    Polyclonal Antibody for Human Exosome complex component MTR3
    Polyclonal Antibody for Human Exosome complex component MTR3
    Monoclonal Antibody for Human Exosome complex component MTR3
    Monoclonal Antibody for Human Exosome complex component MTR3
    Protein for Human Exosome complex component MTR3
    Protein for Human Exosome complex component MTR3

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    Recovery
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    Linearity
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    References
    1. 1.
      "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J. , Han C. , Gordon L.A. , Terry A. , Prabhakar S. , She X. , Xie G. , Hellsten U. , Chan Y.M. , Altherr M. , Couronne O. , Aerts A. , Bajorek E. , Black S. , Blumer H. , Branscomb E. , Brown N.C. , Bruno W.J. , more...
      Nature432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
      tissue: Salivary gland.
    2. 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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
      tissue: Salivary gland.
    3. 3.
      "AU binding proteins recruit the exosome to degrade ARE-containing mRNAs."
      Chen C.-Y. , Gherzi R. , Ong S.-E. , Chan E.L. , Raijmakers R. , Pruijn G.J.M. , Stoecklin G. , Moroni C. , Mann M. , Karin M.
      Cell107:451-464(2001) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION BY MASS SPECTROMETRY;IDENTIFICATION IN THE RNA EXOSOME CORE COMPLEX
    4. 4.
      "Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring."
      Raijmakers R. , Vree Egberts W. , van Venrooij W.J. , Pruijn G.J.M.
      J. Mol. Biol.323:653-663(2002) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PROTEIN INTERACTION
    5. 5.
      "A protein interaction framework for human mRNA degradation."
      Lehner B. , Sanderson C.M.
      Genome Res.14:1315-1323(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PROTEIN INTERACTION
    6. 6.
      "Dis3-like 1: a novel exoribonuclease associated with the human exosome."
      Staals R.H. , Bronkhorst A.W. , Schilders G. , Slomovic S. , Schuster G. , Heck A.J. , Raijmakers R. , Pruijn G.J.
      EMBO J.29:2358-2367(2010) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION IN THE RNA EXOSOME COMPLEX;IDENTIFICATION BY MASS SPECTROMETRY
    7. 7.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
    8. 8.
      "The RNA exosome targets the AID cytidine deaminase to both strands of transcribed duplex DNA substrates."
      Basu U. , Meng F.L. , Keim C. , Grinstein V. , Pefanis E. , Eccleston J. , Zhang T. , Myers D. , Wasserman C.R. , Wesemann D.R. , Januszyk K. , Gregory R.I. , Deng H. , Lima C.D. , Alt F.W.
      Cell144:353-363(2011) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN DEAMINATION OF TRANSCRIBED DNA SUBSTRATE
    9. 9.
      "Reconstitution, activities, and structure of the eukaryotic RNA exosome."
      Liu Q. , Greimann J.C. , Lima C.D.
      Cell127:1223-1237(2006) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS);LACK OF CATALYTIC ACTIVITY;RECONSTITUTION OF THE RNA EXOSOME CORE COMPLEX
    10. 10.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: ERRATUM
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