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Q13868

- EXOS2_HUMAN

UniProt

Q13868 - EXOS2_HUMAN

Protein

Exosome complex component RRP4

Gene

EXOSC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (27 Apr 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. EXOSC2 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC4 and EXOSC7.1 Publication

    GO - Molecular functioni

    1. 3'-5'-exoribonuclease activity Source: ProtInc
    2. 7S RNA binding Source: ProtInc
    3. 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. positive regulation of cell growth Source: UniProtKB
    6. RNA metabolic process Source: Reactome
    7. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
    8. rRNA processing Source: ProtInc

    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 RRP4
    Alternative name(s):
    Exosome component 2
    Ribosomal RNA-processing protein 4
    Gene namesi
    Name:EXOSC2
    Synonyms:RRP4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:17097. EXOSC2.

    Subcellular locationi

    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

    PharmGKBiPA134876020.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 293293Exosome complex component RRP4PRO_0000087129Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei124 – 1241Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13868.
    PaxDbiQ13868.
    PRIDEiQ13868.

    PTM databases

    PhosphoSiteiQ13868.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13868.
    BgeeiQ13868.
    CleanExiHS_EXOSC2.
    GenevestigatoriQ13868.

    Organism-specific databases

    HPAiHPA021790.

    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 GTPBP1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DIS3LQ8TF46-12EBI-301735,EBI-3895807
    EXOSC3Q9NQT55EBI-301735,EBI-371866
    EXOSC4Q9NPD35EBI-301735,EBI-371823
    EXOSC7Q150245EBI-301735,EBI-371841
    MPHOSPH6Q995473EBI-301735,EBI-373187
    ZNF408Q9H9D43EBI-301735,EBI-347633

    Protein-protein interaction databases

    BioGridi116977. 29 interactions.
    IntActiQ13868. 34 interactions.
    MINTiMINT-2633872.
    STRINGi9606.ENSP00000361433.

    Structurei

    Secondary structure

    1
    293
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi45 – 473
    Beta strandi49 – 546
    Beta strandi56 – 638
    Beta strandi66 – 738
    Beta strandi80 – 823
    Beta strandi86 – 927
    Beta strandi95 – 995
    Beta strandi101 – 1044
    Beta strandi106 – 1116
    Helixi129 – 1346
    Beta strandi144 – 1496
    Turni150 – 1523
    Beta strandi153 – 1575
    Beta strandi171 – 1733
    Beta strandi193 – 1986
    Turni199 – 2013
    Beta strandi202 – 2065
    Helixi220 – 2223
    Helixi228 – 24619
    Helixi253 – 2619
    Turni262 – 2665
    Helixi275 – 28915
    Turni290 – 2923

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NN6X-ray3.35H1-293[»]
    ProteinModelPortaliQ13868.
    SMRiQ13868. Positions 25-293.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13868.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini79 – 15981S1 motifAdd
    BLAST

    Sequence similaritiesi

    Belongs to the RRP4 family.Curated
    Contains 1 S1 motif domain.Curated

    Phylogenomic databases

    eggNOGiCOG1097.
    HOGENOMiHOG000193685.
    HOVERGENiHBG051517.
    InParanoidiQ13868.
    KOiK03679.
    OMAiSRLRNCV.
    OrthoDBiEOG7JX34R.
    PhylomeDBiQ13868.
    TreeFamiTF105623.

    Family and domain databases

    InterProiIPR025721. Exosome_cplx_N_dom.
    IPR026699. Exosome_RNA_bind1/RRP40/RRP4.
    IPR004088. KH_dom_type_1.
    IPR012340. NA-bd_OB-fold.
    IPR022967. RNA-binding_domain_S1.
    [Graphical view]
    PANTHERiPTHR21321. PTHR21321. 1 hit.
    PfamiPF14382. ECR1_N. 1 hit.
    [Graphical view]
    SMARTiSM00316. S1. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.
    SSF54791. SSF54791. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13868-1) [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

    MAMEMRLPVA RKPLSERLGR DTKKHLVVPG DTITTDTGFM RGHGTYMGEE    50
    KLIASVAGSV ERVNKLICVK ALKTRYIGEV GDIVVGRITE VQQKRWKVET 100
    NSRLDSVLLL SSMNLPGGEL RRRSAEDELA MRGFLQEGDL ISAEVQAVFS 150
    DGAVSLHTRS LKYGKLGQGV LVQVSPSLVK RQKTHFHDLP CGASVILGNN 200
    GFIWIYPTPE HKEEEAGGFI ANLEPVSLAD REVISRLRNC IISLVTQRMM 250
    LYDTSILYCY EASLPHQIKD ILKPEIMEEI VMETRQRLLE QEG 293
    Length:293
    Mass (Da):32,789
    Last modified:April 27, 2001 - v2
    Checksum:i882033F50791643F
    GO
    Isoform 2 (identifier: Q13868-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         143-168: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:267
    Mass (Da):30,045
    Checksum:iFCBD02E381F5FAB9
    GO

    Sequence cautioni

    The sequence AAB60392.1 differs from that shown. Reason: Erroneous gene model prediction.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei143 – 16826Missing in isoform 2. 1 PublicationVSP_054921Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07561 Genomic DNA. Translation: AAB60392.1. Sequence problems.
    AK001916 mRNA. Translation: BAA91977.1.
    AK022460 mRNA. Translation: BAB14043.1.
    AK296605 mRNA. Translation: BAG59218.1.
    AL359092 Genomic DNA. Translation: CAM45748.1.
    CH471090 Genomic DNA. Translation: EAW87944.1.
    BC000747 mRNA. Translation: AAH00747.1.
    CCDSiCCDS65160.1. [Q13868-2]
    CCDS6935.1. [Q13868-1]
    RefSeqiNP_001269637.1. NM_001282708.1. [Q13868-2]
    NP_055100.2. NM_014285.6. [Q13868-1]
    UniGeneiHs.654643.

    Genome annotation databases

    EnsembliENST00000372358; ENSP00000361433; ENSG00000130713. [Q13868-1]
    ENST00000546165; ENSP00000444917; ENSG00000130713. [Q13868-2]
    GeneIDi23404.
    KEGGihsa:23404.
    UCSCiuc004bzu.2. human. [Q13868-1]

    Polymorphism databases

    DMDMi13878748.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07561 Genomic DNA. Translation: AAB60392.1 . Sequence problems.
    AK001916 mRNA. Translation: BAA91977.1 .
    AK022460 mRNA. Translation: BAB14043.1 .
    AK296605 mRNA. Translation: BAG59218.1 .
    AL359092 Genomic DNA. Translation: CAM45748.1 .
    CH471090 Genomic DNA. Translation: EAW87944.1 .
    BC000747 mRNA. Translation: AAH00747.1 .
    CCDSi CCDS65160.1. [Q13868-2 ]
    CCDS6935.1. [Q13868-1 ]
    RefSeqi NP_001269637.1. NM_001282708.1. [Q13868-2 ]
    NP_055100.2. NM_014285.6. [Q13868-1 ]
    UniGenei Hs.654643.

    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 H 1-293 [» ]
    ProteinModelPortali Q13868.
    SMRi Q13868. Positions 25-293.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116977. 29 interactions.
    IntActi Q13868. 34 interactions.
    MINTi MINT-2633872.
    STRINGi 9606.ENSP00000361433.

    PTM databases

    PhosphoSitei Q13868.

    Polymorphism databases

    DMDMi 13878748.

    Proteomic databases

    MaxQBi Q13868.
    PaxDbi Q13868.
    PRIDEi Q13868.

    Protocols and materials databases

    DNASUi 23404.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372358 ; ENSP00000361433 ; ENSG00000130713 . [Q13868-1 ]
    ENST00000546165 ; ENSP00000444917 ; ENSG00000130713 . [Q13868-2 ]
    GeneIDi 23404.
    KEGGi hsa:23404.
    UCSCi uc004bzu.2. human. [Q13868-1 ]

    Organism-specific databases

    CTDi 23404.
    GeneCardsi GC09P133569.
    H-InvDB HIX0008473.
    HGNCi HGNC:17097. EXOSC2.
    HPAi HPA021790.
    MIMi 602238. gene.
    neXtProti NX_Q13868.
    PharmGKBi PA134876020.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1097.
    HOGENOMi HOG000193685.
    HOVERGENi HBG051517.
    InParanoidi Q13868.
    KOi K03679.
    OMAi SRLRNCV.
    OrthoDBi EOG7JX34R.
    PhylomeDBi Q13868.
    TreeFami TF105623.

    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 EXOSC2. human.
    EvolutionaryTracei Q13868.
    GeneWikii Exosome_component_2.
    GenomeRNAii 23404.
    NextBioi 35472812.
    PROi Q13868.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13868.
    Bgeei Q13868.
    CleanExi HS_EXOSC2.
    Genevestigatori Q13868.

    Family and domain databases

    InterProi IPR025721. Exosome_cplx_N_dom.
    IPR026699. Exosome_RNA_bind1/RRP40/RRP4.
    IPR004088. KH_dom_type_1.
    IPR012340. NA-bd_OB-fold.
    IPR022967. RNA-binding_domain_S1.
    [Graphical view ]
    PANTHERi PTHR21321. PTHR21321. 1 hit.
    Pfami PF14382. ECR1_N. 1 hit.
    [Graphical view ]
    SMARTi SM00316. S1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    SSF54791. SSF54791. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the human abl and bcr genes."
      Chissoe S.L.
      Thesis (1994), University of Oklahoma, United States
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Lung carcinoma.
    2. "The exosome: a conserved eukaryotic RNA processing complex containing multiple 3'-->5' exoribonucleases."
      Mitchell P., Petfalski E., Shevchenko A., Mann M., Tollervey D.
      Cell 91:457-466(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION.
      Tissue: Cervix adenocarcinoma.
    3. "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: Colon, Mammary gland and Placenta.
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Lung.
    7. "The 3' end of yeast 5.8S rRNA is generated by an exonuclease processing mechanism."
      Mitchell P., Petfalski E., Tollervey D.
      Genes Dev. 10:502-513(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    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, PROTEIN INTERACTION.
    10. "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.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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 DIS3.
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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.
    18. "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.
    19. Erratum
      Liu Q., Greimann J.C., Lima C.D.
      Cell 131:188-189(2007)

    Entry informationi

    Entry nameiEXOS2_HUMAN
    AccessioniPrimary (citable) accession number: Q13868
    Secondary accession number(s): A3KFL3, B4DKK6, Q9NUY4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: April 27, 2001
    Last modified: October 1, 2014
    This is version 144 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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