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Q9NQT5

- EXOS3_HUMAN

UniProt

Q9NQT5 - EXOS3_HUMAN

Protein

Exosome complex component RRP40

Gene

EXOSC3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (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. EXOSC3 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC9 and EXOSC5.4 Publications

    GO - Molecular functioni

    1. 3'-5'-exoribonuclease activity Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. CUT catabolic process Source: UniProtKB
    2. DNA deamination Source: UniProtKB
    3. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: UniProtKB
    4. gene expression Source: Reactome
    5. isotype switching Source: UniProtKB
    6. mRNA metabolic process Source: Reactome
    7. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    8. positive regulation of isotype switching Source: Ensembl
    9. RNA metabolic process Source: Reactome
    10. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
    11. 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 RRP40
    Alternative name(s):
    Exosome component 3
    Ribosomal RNA-processing protein 40
    p10
    Gene namesi
    Name:EXOSC3
    Synonyms:RRP40
    ORF Names:CGI-102
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:17944. EXOSC3.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Exosome, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Pontocerebellar hypoplasia 1B (PCH1B) [MIM:614678]: A severe autosomal recessive neurologic disorder characterized by a combination of cerebellar and spinal motor neuron degeneration beginning at birth. There is diffuse muscle weakness, progressive microcephaly, global developmental delay, and brainstem involvement.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311G → A in PCH1B. 1 Publication
    VAR_068505
    Natural varianti132 – 1321D → A in PCH1B. 1 Publication
    Corresponds to variant rs141138948 [ dbSNP | Ensembl ].
    VAR_068506
    Natural varianti139 – 1391A → P in PCH1B. 1 Publication
    VAR_068507
    Natural varianti238 – 2381W → R in PCH1B. 1 Publication
    VAR_068508

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614678. phenotype.
    Orphaneti2254. Pontocerebellar hypoplasia type 1.
    PharmGKBiPA134926550.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 275274Exosome complex component RRP40PRO_0000087131Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NQT5.
    PaxDbiQ9NQT5.
    PeptideAtlasiQ9NQT5.
    PRIDEiQ9NQT5.

    PTM databases

    PhosphoSiteiQ9NQT5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NQT5.
    BgeeiQ9NQT5.
    CleanExiHS_EXOSC3.
    GenevestigatoriQ9NQT5.

    Organism-specific databases

    HPAiHPA020485.

    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 GTPBP1. Interacts with ZC3HAV1. Interacts with DDX17 only in the presence of ZC3HAV1 in an RNA-independent manner.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DIS3Q9Y2L13EBI-371866,EBI-373539
    DIS3LQ8TF463EBI-371866,EBI-3672244
    EXOSC2Q138685EBI-371866,EBI-301735
    EXOSC4Q9NPD34EBI-371866,EBI-371823
    EXOSC5Q9NQT47EBI-371866,EBI-371876
    EXOSC8Q96B263EBI-371866,EBI-371922

    Protein-protein interaction databases

    BioGridi119217. 19 interactions.
    DIPiDIP-29847N.
    IntActiQ9NQT5. 19 interactions.
    MINTiMINT-3072286.
    STRINGi9606.ENSP00000323046.

    Structurei

    Secondary structure

    1
    275
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 243
    Beta strandi25 – 273
    Beta strandi30 – 345
    Beta strandi45 – 495
    Beta strandi78 – 803
    Beta strandi85 – 895
    Turni92 – 943
    Beta strandi99 – 1035
    Beta strandi113 – 12513
    Beta strandi128 – 1325
    Beta strandi134 – 1374
    Beta strandi141 – 1433
    Beta strandi145 – 1473
    Beta strandi153 – 1575
    Beta strandi162 – 1698
    Beta strandi177 – 1793
    Turni183 – 1853
    Beta strandi198 – 2003
    Helixi204 – 2118
    Helixi217 – 2204
    Beta strandi224 – 2263
    Beta strandi230 – 2323
    Turni233 – 2353
    Beta strandi236 – 2394
    Helixi244 – 25613
    Turni262 – 2643
    Helixi265 – 27410

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NN6X-ray3.35G1-275[»]
    ProteinModelPortaliQ9NQT5.
    SMRiQ9NQT5. Positions 17-275.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NQT5.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RRP40 family.Curated

    Phylogenomic databases

    eggNOGiCOG1097.
    HOGENOMiHOG000184644.
    HOVERGENiHBG051518.
    InParanoidiQ9NQT5.
    KOiK03681.
    OMAiVNGRVWI.
    OrthoDBiEOG76HQ2F.
    PhylomeDBiQ9NQT5.
    TreeFamiTF314927.

    Family and domain databases

    InterProiIPR026699. Exosome_RNA_bind1/RRP40/RRP4.
    IPR004088. KH_dom_type_1.
    IPR012340. NA-bd_OB-fold.
    [Graphical view]
    PANTHERiPTHR21321. PTHR21321. 1 hit.
    SUPFAMiSSF50249. SSF50249. 1 hit.
    SSF54791. SSF54791. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NQT5-1) [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

    MAEPASVAAE SLAGSRARAA RTVLGQVVLP GEELLLPEQE DAEGPGGAVE    50
    RPLSLNARAC SRVRVVCGPG LRRCGDRLLV TKCGRLRHKE PGSGSGGGVY 100
    WVDSQQKRYV PVKGDHVIGI VTAKSGDIFK VDVGGSEPAS LSYLSFEGAT 150
    KRNRPNVQVG DLIYGQFVVA NKDMEPEMVC IDSCGRANGM GVIGQDGLLF 200
    KVTLGLIRKL LAPDCEIIQE VGKLYPLEIV FGMNGRIWVK AKTIQQTLIL 250
    ANILEACEHM TSDQRKQIFS RLAES 275
    Length:275
    Mass (Da):29,572
    Last modified:January 23, 2007 - v3
    Checksum:i264322144A199166
    GO
    Isoform 2 (identifier: Q9NQT5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         159-275: VGDLIYGQFV...KQIFSRLAES → AISSRL

    Note: No experimental confirmation available.

    Show »
    Length:164
    Mass (Da):17,248
    Checksum:i51C07B44337D0076
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 6510NARACSRVRV → MLERARGCAF in AAD34097. (PubMed:10810093)Curated
    Sequence conflicti95 – 951S → G in AAD34097. (PubMed:10810093)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311G → A in PCH1B. 1 Publication
    VAR_068505
    Natural varianti132 – 1321D → A in PCH1B. 1 Publication
    Corresponds to variant rs141138948 [ dbSNP | Ensembl ].
    VAR_068506
    Natural varianti139 – 1391A → P in PCH1B. 1 Publication
    VAR_068507
    Natural varianti225 – 2251Y → H.
    Corresponds to variant rs3208406 [ dbSNP | Ensembl ].
    VAR_054098
    Natural varianti238 – 2381W → R in PCH1B. 1 Publication
    VAR_068508

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei159 – 275117VGDLI…RLAES → AISSRL in isoform 2. 1 PublicationVSP_043457Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF281132 mRNA. Translation: AAF82133.1.
    AK289571 mRNA. Translation: BAF82260.1.
    AK290864 mRNA. Translation: BAF83553.1.
    AL138752 Genomic DNA. Translation: CAI13880.1.
    CH471071 Genomic DNA. Translation: EAW58264.1.
    BC002437 mRNA. Translation: AAH02437.1.
    BC008880 mRNA. Translation: AAH08880.1.
    AF151860 mRNA. Translation: AAD34097.1.
    CCDSiCCDS35016.1. [Q9NQT5-1]
    CCDS43805.1. [Q9NQT5-2]
    RefSeqiNP_001002269.1. NM_001002269.2. [Q9NQT5-2]
    NP_057126.2. NM_016042.3. [Q9NQT5-1]
    UniGeneiHs.602571.
    Hs.713483.

    Genome annotation databases

    EnsembliENST00000327304; ENSP00000323046; ENSG00000107371. [Q9NQT5-1]
    ENST00000396521; ENSP00000379775; ENSG00000107371. [Q9NQT5-2]
    ENST00000465229; ENSP00000418422; ENSG00000107371. [Q9NQT5-2]
    GeneIDi51010.
    KEGGihsa:51010.
    UCSCiuc004aal.3. human. [Q9NQT5-1]
    uc004aam.3. human. [Q9NQT5-2]

    Polymorphism databases

    DMDMi14285758.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF281132 mRNA. Translation: AAF82133.1 .
    AK289571 mRNA. Translation: BAF82260.1 .
    AK290864 mRNA. Translation: BAF83553.1 .
    AL138752 Genomic DNA. Translation: CAI13880.1 .
    CH471071 Genomic DNA. Translation: EAW58264.1 .
    BC002437 mRNA. Translation: AAH02437.1 .
    BC008880 mRNA. Translation: AAH08880.1 .
    AF151860 mRNA. Translation: AAD34097.1 .
    CCDSi CCDS35016.1. [Q9NQT5-1 ]
    CCDS43805.1. [Q9NQT5-2 ]
    RefSeqi NP_001002269.1. NM_001002269.2. [Q9NQT5-2 ]
    NP_057126.2. NM_016042.3. [Q9NQT5-1 ]
    UniGenei Hs.602571.
    Hs.713483.

    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 G 1-275 [» ]
    ProteinModelPortali Q9NQT5.
    SMRi Q9NQT5. Positions 17-275.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119217. 19 interactions.
    DIPi DIP-29847N.
    IntActi Q9NQT5. 19 interactions.
    MINTi MINT-3072286.
    STRINGi 9606.ENSP00000323046.

    PTM databases

    PhosphoSitei Q9NQT5.

    Polymorphism databases

    DMDMi 14285758.

    Proteomic databases

    MaxQBi Q9NQT5.
    PaxDbi Q9NQT5.
    PeptideAtlasi Q9NQT5.
    PRIDEi Q9NQT5.

    Protocols and materials databases

    DNASUi 51010.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327304 ; ENSP00000323046 ; ENSG00000107371 . [Q9NQT5-1 ]
    ENST00000396521 ; ENSP00000379775 ; ENSG00000107371 . [Q9NQT5-2 ]
    ENST00000465229 ; ENSP00000418422 ; ENSG00000107371 . [Q9NQT5-2 ]
    GeneIDi 51010.
    KEGGi hsa:51010.
    UCSCi uc004aal.3. human. [Q9NQT5-1 ]
    uc004aam.3. human. [Q9NQT5-2 ]

    Organism-specific databases

    CTDi 51010.
    GeneCardsi GC09M037772.
    HGNCi HGNC:17944. EXOSC3.
    HPAi HPA020485.
    MIMi 606489. gene.
    614678. phenotype.
    neXtProti NX_Q9NQT5.
    Orphaneti 2254. Pontocerebellar hypoplasia type 1.
    PharmGKBi PA134926550.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1097.
    HOGENOMi HOG000184644.
    HOVERGENi HBG051518.
    InParanoidi Q9NQT5.
    KOi K03681.
    OMAi VNGRVWI.
    OrthoDBi EOG76HQ2F.
    PhylomeDBi Q9NQT5.
    TreeFami TF314927.

    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

    ChiTaRSi EXOSC3. human.
    EvolutionaryTracei Q9NQT5.
    GeneWikii Exosome_component_3.
    GenomeRNAii 51010.
    NextBioi 53494.
    PROi Q9NQT5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NQT5.
    Bgeei Q9NQT5.
    CleanExi HS_EXOSC3.
    Genevestigatori Q9NQT5.

    Family and domain databases

    InterProi IPR026699. Exosome_RNA_bind1/RRP40/RRP4.
    IPR004088. KH_dom_type_1.
    IPR012340. NA-bd_OB-fold.
    [Graphical view ]
    PANTHERi PTHR21321. PTHR21321. 1 hit.
    SUPFAMi SSF50249. SSF50249. 1 hit.
    SSF54791. SSF54791. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] (ISOFORMS 1 AND 2).
      Tissue: Cerebellum.
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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).
      Tissue: Skin and Uterus.
    6. Bienvenut W.V.
      Submitted (AUG-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-16 AND 202-208, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    7. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-275 (ISOFORM 1).
    8. "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.
    9. "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.
    10. "The mammalian exosome mediates the efficient degradation of mRNAs that contain AU-rich elements."
      Mukherjee D., Gao M., O'Connor J.P., Raijmakers R., Pruijn G., Lutz C.S., Wilusz J.
      EMBO J. 21:165-174(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CYTOPLASMIC MRNA DEGRADATION.
    11. "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.
    12. "p72 DEAD box RNA helicase is required for optimal function of the zinc-finger antiviral protein."
      Chen G., Guo X., Lv F., Xu Y., Gao G.
      Proc. Natl. Acad. Sci. U.S.A. 105:4352-4357(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX17.
    13. "RNA exosome depletion reveals transcription upstream of active human promoters."
      Preker P., Nielsen J., Kammler S., Lykke-Andersen S., Christensen M.S., Mapendano C.K., Schierup M.H., Jensen T.H.
      Science 322:1851-1854(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROMPT DEGRADATION.
    14. "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].
    15. "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, SUBCELLULAR LOCATION, INTERACTION WITH DIS3L.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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.
    18. "Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding protein 1 (GTPBP1) with its target mRNAs."
      Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J., Chung S.J., Senju S., Nishimura Y., Kim K.T.
      FASEB J. 25:2757-2769(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GTPBP1.
    19. "Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation."
      Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T., Gao G.
      Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZC3HAV1.
    20. "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].
    21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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), RECONSTITUTION OF THE RNA EXOSOME CORE COMPLEX.
    23. Erratum
      Liu Q., Greimann J.C., Lima C.D.
      Cell 131:188-189(2007)
    24. Cited for: VARIANTS PCH1B ALA-31; ALA-132; PRO-139 AND ARG-238.

    Entry informationi

    Entry nameiEXOS3_HUMAN
    AccessioniPrimary (citable) accession number: Q9NQT5
    Secondary accession number(s): A8K0K6, Q5QP85, Q9Y3A8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 137 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3