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Q9NPD3

- EXOS4_HUMAN

UniProt

Q9NPD3 - EXOS4_HUMAN

Protein

Exosome complex component RRP41

Gene

EXOSC4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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. EXOSC4 binds to ARE-containing RNAs.5 Publications

    GO - Molecular functioni

    1. 3'-5'-exoribonuclease activity Source: UniProtKB
    2. AU-rich element binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. defense response to virus Source: MGI
    2. DNA deamination Source: UniProtKB
    3. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
    4. gene expression Source: Reactome
    5. histone mRNA catabolic process Source: UniProtKB
    6. maturation of 5.8S rRNA Source: UniProtKB
    7. mRNA metabolic process Source: Reactome
    8. nuclear mRNA surveillance Source: UniProtKB
    9. nuclear-transcribed mRNA catabolic process Source: UniProtKB
    10. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    11. positive regulation of cell growth Source: UniProtKB
    12. RNA metabolic process Source: Reactome
    13. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
    14. rRNA processing Source: UniProtKB

    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 RRP41
    Alternative name(s):
    Exosome component 4
    Ribosomal RNA-processing protein 41
    p12A
    Gene namesi
    Name:EXOSC4
    Synonyms:RRP41, SKI6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:18189. EXOSC4.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleusnucleolus 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. exosome (RNase complex) Source: UniProtKB
    4. nucleolus Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. transcriptionally active chromatin Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Exosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134867931.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 245244Exosome complex component RRP41PRO_0000139958Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NPD3.
    PaxDbiQ9NPD3.
    PRIDEiQ9NPD3.

    2D gel databases

    SWISS-2DPAGEQ9NPD3.

    PTM databases

    PhosphoSiteiQ9NPD3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NPD3.
    BgeeiQ9NPD3.
    CleanExiHS_EXOSC4.
    GenevestigatoriQ9NPD3.

    Organism-specific databases

    HPAiHPA024792.

    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 DDX60.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EXOSC1Q9Y3B24EBI-371823,EBI-371892
    EXOSC10Q017803EBI-371823,EBI-358236
    EXOSC2Q138685EBI-371823,EBI-301735
    EXOSC3Q9NQT54EBI-371823,EBI-371866
    EXOSC9Q062653EBI-371823,EBI-347966

    Protein-protein interaction databases

    BioGridi120007. 39 interactions.
    IntActiQ9NPD3. 29 interactions.
    MINTiMINT-2818708.
    STRINGi9606.ENSP00000315476.

    Structurei

    Secondary structure

    1
    245
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 174
    Beta strandi25 – 306
    Beta strandi32 – 4514
    Beta strandi47 – 5711
    Beta strandi60 – 623
    Beta strandi72 – 787
    Turni80 – 823
    Beta strandi83 – 853
    Turni89 – 913
    Helixi94 – 10916
    Helixi113 – 1153
    Beta strandi119 – 12911
    Helixi134 – 14815
    Beta strandi158 – 1658
    Beta strandi168 – 1725
    Helixi175 – 1784
    Beta strandi185 – 1895
    Turni191 – 1933
    Beta strandi198 – 2014
    Helixi210 – 23930

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NN6X-ray3.35B2-245[»]
    ProteinModelPortaliQ9NPD3.
    SMRiQ9NPD3. Positions 7-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NPD3.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RNase PH family.Curated

    Phylogenomic databases

    eggNOGiCOG0689.
    HOGENOMiHOG000229515.
    HOVERGENiHBG051519.
    InParanoidiQ9NPD3.
    KOiK11600.
    OMAiDYVCACT.
    PhylomeDBiQ9NPD3.
    TreeFamiTF313915.

    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.

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

    Q9NPD3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGLELLSDQ GYRVDGRRAG ELRKIQARMG VFAQADGSAY IEQGNTKALA    50
    VVYGPHEIRG SRARALPDRA LVNCQYSSAT FSTGERKRRP HGDRKSCEMG 100
    LQLRQTFEAA ILTQLHPRSQ IDIYVQVLQA DGGTYAACVN AATLAVLDAG 150
    IPMRDFVCAC SAGFVDGTAL ADLSHVEEAA GGPQLALALL PASGQIALLE 200
    MDARLHEDHL ERVLEAAAQA ARDVHTLLDR VVRQHVREAS ILLGD 245
    Length:245
    Mass (Da):26,383
    Last modified:January 23, 2007 - v3
    Checksum:i7A24E97897DAF313
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF281133 mRNA. Translation: AAF82134.1.
    AK000598 mRNA. Translation: BAA91279.1.
    AC109322 Genomic DNA. No translation available.
    BC002777 mRNA. Translation: AAH02777.1.
    CCDSiCCDS6414.1.
    RefSeqiNP_061910.1. NM_019037.2.
    UniGeneiHs.632041.

    Genome annotation databases

    EnsembliENST00000316052; ENSP00000315476; ENSG00000178896.
    GeneIDi54512.
    KEGGihsa:54512.
    UCSCiuc003zau.3. human.

    Polymorphism databases

    DMDMi14285756.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF281133 mRNA. Translation: AAF82134.1 .
    AK000598 mRNA. Translation: BAA91279.1 .
    AC109322 Genomic DNA. No translation available.
    BC002777 mRNA. Translation: AAH02777.1 .
    CCDSi CCDS6414.1.
    RefSeqi NP_061910.1. NM_019037.2.
    UniGenei Hs.632041.

    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 B 2-245 [» ]
    ProteinModelPortali Q9NPD3.
    SMRi Q9NPD3. Positions 7-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120007. 39 interactions.
    IntActi Q9NPD3. 29 interactions.
    MINTi MINT-2818708.
    STRINGi 9606.ENSP00000315476.

    PTM databases

    PhosphoSitei Q9NPD3.

    Polymorphism databases

    DMDMi 14285756.

    2D gel databases

    SWISS-2DPAGE Q9NPD3.

    Proteomic databases

    MaxQBi Q9NPD3.
    PaxDbi Q9NPD3.
    PRIDEi Q9NPD3.

    Protocols and materials databases

    DNASUi 54512.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000316052 ; ENSP00000315476 ; ENSG00000178896 .
    GeneIDi 54512.
    KEGGi hsa:54512.
    UCSCi uc003zau.3. human.

    Organism-specific databases

    CTDi 54512.
    GeneCardsi GC08P145133.
    HGNCi HGNC:18189. EXOSC4.
    HPAi HPA024792.
    MIMi 606491. gene.
    neXtProti NX_Q9NPD3.
    PharmGKBi PA134867931.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0689.
    HOGENOMi HOG000229515.
    HOVERGENi HBG051519.
    InParanoidi Q9NPD3.
    KOi K11600.
    OMAi DYVCACT.
    PhylomeDBi Q9NPD3.
    TreeFami TF313915.

    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 Q9NPD3.
    GeneWikii Exosome_component_4.
    GenomeRNAii 54512.
    NextBioi 56896.
    PROi Q9NPD3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NPD3.
    Bgeei Q9NPD3.
    CleanExi HS_EXOSC4.
    Genevestigatori Q9NPD3.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Skin.
    5. Bienvenut W.V.
      Submitted (OCT-2004) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    6. "The yeast exosome and human PM-Scl are related complexes of 3'-->5' exonucleases."
      Allmang C., Petfalski E., Podtelejnikov A., Mann M., Tollervey D., Mitchell P.
      Genes Dev. 13:2148-2158(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. "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.
    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. "Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'."
      Mullen T.E., Marzluff W.F.
      Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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.
    13. "Addition of poly(A) and poly(A)-rich tails during RNA degradation in the cytoplasm of human cells."
      Slomovic S., Fremder E., Staals R.H., Pruijn G.J., Schuster G.
      Proc. Natl. Acad. Sci. U.S.A. 107:7407-7412(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RRNA MATURATION.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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.
      Cell 144:353-363(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEAMINATION OF TRANSCRIBED DNA SUBSTRATE.
    16. "DDX60, a DEXD/H box helicase, is a novel antiviral factor promoting RIG-I-like receptor-mediated signaling."
      Miyashita M., Oshiumi H., Matsumoto M., Seya T.
      Mol. Cell. Biol. 31:3802-3819(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX60.
    17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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.
    20. Erratum
      Liu Q., Greimann J.C., Lima C.D.
      Cell 131:188-189(2007)

    Entry informationi

    Entry nameiEXOS4_HUMAN
    AccessioniPrimary (citable) accession number: Q9NPD3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 134 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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