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Q96B26

- EXOS8_HUMAN

UniProt

Q96B26 - EXOS8_HUMAN

Protein

Exosome complex component RRP43

Gene

EXOSC8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Dec 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. EXOSC8 binds to ARE-containing RNAs.2 Publications

    GO - Molecular functioni

    1. AU-rich element binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

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

    Keywords - Biological processi

    rRNA processing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_18355. ATF4 activates genes.
    REACT_20619. mRNA decay by 3' to 5' exoribonuclease.
    REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
    REACT_25042. KSRP destabilizes mRNA.
    REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exosome complex component RRP43
    Alternative name(s):
    Exosome component 8
    Opa-interacting protein 2
    Short name:
    OIP-2
    Ribosomal RNA-processing protein 43
    p9
    Gene namesi
    Name:EXOSC8
    Synonyms:OIP2, RRP43
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:17035. EXOSC8.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication. Nucleusnucleolus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. exosome (RNase complex) Source: UniProtKB
    4. nucleolus Source: UniProtKB-SubCell
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Exosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134922251.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 276275Exosome complex component RRP43PRO_0000139967Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ96B26.
    PaxDbiQ96B26.
    PeptideAtlasiQ96B26.
    PRIDEiQ96B26.

    2D gel databases

    SWISS-2DPAGEQ96B26.

    PTM databases

    PhosphoSiteiQ96B26.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96B26.
    BgeeiQ96B26.
    CleanExiHS_EXOSC8.
    GenevestigatoriQ96B26.

    Organism-specific databases

    HPAiCAB034240.
    HPA039702.
    HPA043942.

    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. Binds outer membrane protein opap from Neisseria gonorrhoeae.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EXOSC3Q9NQT53EBI-371922,EBI-371866
    EXOSC5Q9NQT44EBI-371922,EBI-371876

    Protein-protein interaction databases

    BioGridi116468. 29 interactions.
    IntActiQ96B26. 24 interactions.
    MINTiMINT-4536555.
    STRINGi9606.ENSP00000374354.

    Structurei

    Secondary structure

    1
    276
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 199
    Beta strandi37 – 393
    Beta strandi43 – 5311
    Beta strandi56 – 6611
    Beta strandi71 – 733
    Beta strandi80 – 845
    Beta strandi87 – 893
    Beta strandi95 – 973
    Helixi100 – 11617
    Helixi121 – 1244
    Beta strandi126 – 1283
    Beta strandi133 – 14311
    Helixi150 – 16112
    Beta strandi172 – 1754
    Beta strandi194 – 2007
    Turni202 – 2043
    Beta strandi207 – 2093
    Turni212 – 2165
    Beta strandi219 – 2268
    Beta strandi232 – 2387
    Helixi245 – 26723
    Turni268 – 2736

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NN6X-ray3.35C1-276[»]
    ProteinModelPortaliQ96B26.
    SMRiQ96B26. Positions 7-275.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96B26.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RNase PH family.Curated

    Phylogenomic databases

    eggNOGiCOG2123.
    HOGENOMiHOG000229504.
    HOVERGENiHBG051522.
    InParanoidiQ96B26.
    KOiK12586.
    OMAiQAASQFI.
    OrthoDBiEOG7D59PC.
    PhylomeDBiQ96B26.
    TreeFamiTF320415.

    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. 2 hits.
    SSF55666. SSF55666. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q96B26-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAGFKTVEP LEYYRRFLKE NCRPDGRELG EFRTTTVNIG SISTADGSAL    50
    VKLGNTTVIC GVKAEFAAPS TDAPDKGYVV PNVDLPPLCS SRFRSGPPGE 100
    EAQVASQFIA DVIENSQIIQ KEDLCISPGK LVWVLYCDLI CLDYDGNILD 150
    ACTFALLAAL KNVQLPEVTI NEETALAEVN LKKKSYLNIR THPVATSFAV 200
    FDDTLLIVDP TGEEEHLATG TLTIVMDEEG KLCCLHKPGG SGLTGAKLQD 250
    CMSRAVTRHK EVKKLMDEVI KSMKPK 276
    Length:276
    Mass (Da):30,040
    Last modified:December 1, 2001 - v1
    Checksum:iFC8F5BAE74A1FF55
    GO

    Sequence cautioni

    The sequence CAI14013.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence EAX08581.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti265 – 27612LMDEV…SMKPK → TDG in AAC39558. (PubMed:9466265)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL138706 Genomic DNA. Translation: CAI14013.1. Sequence problems.
    CH471075 Genomic DNA. Translation: EAX08581.1. Sequence problems.
    BC020773 mRNA. Translation: AAH20773.1.
    AF025438 mRNA. Translation: AAC39558.1.
    CCDSiCCDS31958.1.
    RefSeqiNP_852480.1. NM_181503.2.
    UniGeneiHs.294041.

    Genome annotation databases

    EnsembliENST00000389704; ENSP00000374354; ENSG00000120699.
    GeneIDi11340.
    KEGGihsa:11340.
    UCSCiuc001uwa.3. human.

    Polymorphism databases

    DMDMi21759409.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL138706 Genomic DNA. Translation: CAI14013.1 . Sequence problems.
    CH471075 Genomic DNA. Translation: EAX08581.1 . Sequence problems.
    BC020773 mRNA. Translation: AAH20773.1 .
    AF025438 mRNA. Translation: AAC39558.1 .
    CCDSi CCDS31958.1.
    RefSeqi NP_852480.1. NM_181503.2.
    UniGenei Hs.294041.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2NN6 X-ray 3.35 C 1-276 [» ]
    ProteinModelPortali Q96B26.
    SMRi Q96B26. Positions 7-275.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116468. 29 interactions.
    IntActi Q96B26. 24 interactions.
    MINTi MINT-4536555.
    STRINGi 9606.ENSP00000374354.

    PTM databases

    PhosphoSitei Q96B26.

    Polymorphism databases

    DMDMi 21759409.

    2D gel databases

    SWISS-2DPAGE Q96B26.

    Proteomic databases

    MaxQBi Q96B26.
    PaxDbi Q96B26.
    PeptideAtlasi Q96B26.
    PRIDEi Q96B26.

    Protocols and materials databases

    DNASUi 11340.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389704 ; ENSP00000374354 ; ENSG00000120699 .
    GeneIDi 11340.
    KEGGi hsa:11340.
    UCSCi uc001uwa.3. human.

    Organism-specific databases

    CTDi 11340.
    GeneCardsi GC13P037572.
    HGNCi HGNC:17035. EXOSC8.
    HPAi CAB034240.
    HPA039702.
    HPA043942.
    MIMi 606019. gene.
    neXtProti NX_Q96B26.
    PharmGKBi PA134922251.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2123.
    HOGENOMi HOG000229504.
    HOVERGENi HBG051522.
    InParanoidi Q96B26.
    KOi K12586.
    OMAi QAASQFI.
    OrthoDBi EOG7D59PC.
    PhylomeDBi Q96B26.
    TreeFami TF320415.

    Enzyme and pathway databases

    Reactomei REACT_18355. ATF4 activates genes.
    REACT_20619. mRNA decay by 3' to 5' exoribonuclease.
    REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
    REACT_25042. KSRP destabilizes mRNA.
    REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

    Miscellaneous databases

    EvolutionaryTracei Q96B26.
    GeneWikii Exosome_component_8.
    GenomeRNAii 11340.
    NextBioi 43089.
    PROi Q96B26.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96B26.
    Bgeei Q96B26.
    CleanExi HS_EXOSC8.
    Genevestigatori Q96B26.

    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. 2 hits.
    SSF55666. SSF55666. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Uterus.
    4. "Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth."
      Williams J.M., Chen G.-C., Zhu L., Rest R.F.
      Mol. Microbiol. 27:171-186(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-276.
    5. "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.
      Cell 107:451-464(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE RNA EXOSOME CORE COMPLEX.
    6. "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]
      Cited for: PROTEIN INTERACTION.
    7. "A protein interaction framework for human mRNA degradation."
      Lehner B., Sanderson C.M.
      Genome Res. 14:1315-1323(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN INTERACTION.
    8. "Sequence-specific RNA binding mediated by the RNase PH domain of components of the exosome."
      Anderson J.R., Mukherjee D., Muthukumaraswamy K., Moraes K.C., Wilusz C.J., Wilusz J.
      RNA 12:1810-1816(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ARE-CONTAINING MRNA-BINDING.
    9. "Human cell growth requires a functional cytoplasmic exosome, which is involved in various mRNA decay pathways."
      van Dijk E.L., Schilders G., Pruijn G.J.
      RNA 13:1027-1035(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA DEGRADATION, SUBCELLULAR LOCATION.
    10. "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]
      Cited for: IDENTIFICATION IN THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    13. "Reconstitution, activities, and structure of the eukaryotic RNA exosome."
      Liu Q., Greimann J.C., Lima C.D.
      Cell 127:1223-1237(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS), LACK OF CATALYTIC ACTIVITY, RECONSTITUTION OF THE RNA EXOSOME CORE COMPLEX.
    14. Erratum
      Liu Q., Greimann J.C., Lima C.D.
      Cell 131:188-189(2007)

    Entry informationi

    Entry nameiEXOS8_HUMAN
    AccessioniPrimary (citable) accession number: Q96B26
    Secondary accession number(s): O43480, Q5TBA5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2002
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 126 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

    Caution

    The six exosome core subunits containing a RNase PH-domain are not phosphorolytically active.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3