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Q06265

- EXOS9_HUMAN

UniProt

Q06265 - EXOS9_HUMAN

Protein

Exosome complex component RRP45

Gene

EXOSC9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (15 May 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. EXOSC9 binds to ARE-containing RNAs.4 Publications

    GO - Molecular functioni

    1. 3'-5'-exoribonuclease activity Source: UniProtKB
    2. AU-rich element binding Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. RNA binding Source: UniProtKB

    GO - Biological processi

    1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: UniProtKB
    2. gene expression Source: Reactome
    3. immune response Source: UniProtKB
    4. mRNA metabolic process Source: Reactome
    5. nuclear mRNA surveillance Source: UniProtKB
    6. nuclear polyadenylation-dependent rRNA catabolic process Source: UniProtKB
    7. nuclear-transcribed mRNA catabolic process Source: UniProtKB
    8. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    9. positive regulation of cell growth Source: UniProtKB
    10. RNA metabolic process Source: Reactome
    11. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
    12. 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 RRP45
    Alternative name(s):
    Autoantigen PM/Scl 1
    Exosome component 9
    P75 polymyositis-scleroderma overlap syndrome-associated autoantigen
    Polymyositis/scleroderma autoantigen 1
    Polymyositis/scleroderma autoantigen 75 kDa
    Short name:
    PM/Scl-75
    Gene namesi
    Name:EXOSC9
    Synonyms:PMSCL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:9137. EXOSC9.

    Subcellular locationi

    Isoform 3 : Nucleus
    Note: Excluded from the nucleolus.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. exosome (RNase complex) Source: UniProtKB
    4. intermediate filament cytoskeleton Source: HPA
    5. nuclear exosome (RNase complex) Source: UniProtKB
    6. nucleolus Source: HPA
    7. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Exosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33463.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 439439Exosome complex component RRP45PRO_0000139971Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei297 – 2971N6-acetyllysine1 Publication
    Modified residuei306 – 3061Phosphoserine4 Publications
    Modified residuei392 – 3921Phosphoserine2 Publications
    Modified residuei394 – 3941Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ06265.
    PaxDbiQ06265.
    PRIDEiQ06265.

    PTM databases

    PhosphoSiteiQ06265.

    Expressioni

    Gene expression databases

    ArrayExpressiQ06265.
    BgeeiQ06265.
    CleanExiHS_EXOSC9.
    GenevestigatoriQ06265.

    Organism-specific databases

    HPAiHPA041838.
    HPA048257.

    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.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EXOSC4Q9NPD33EBI-347966,EBI-371823

    Protein-protein interaction databases

    BioGridi111402. 17 interactions.
    IntActiQ06265. 15 interactions.
    MINTiMINT-1036055.
    STRINGi9606.ENSP00000368984.

    Structurei

    Secondary structure

    1
    439
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 1912
    Beta strandi36 – 394
    Beta strandi45 – 528
    Beta strandi54 – 596
    Beta strandi62 – 643
    Turni69 – 724
    Beta strandi76 – 827
    Turni84 – 863
    Beta strandi92 – 943
    Helixi96 – 994
    Helixi101 – 11313
    Beta strandi118 – 1214
    Turni125 – 1273
    Beta strandi128 – 13811
    Helixi146 – 15914
    Helixi176 – 1794
    Beta strandi191 – 1988
    Turni200 – 2023
    Beta strandi203 – 2086
    Helixi211 – 2166
    Beta strandi220 – 2267
    Turni227 – 2293
    Beta strandi230 – 2389
    Helixi244 – 27734
    Helixi287 – 2904
    Beta strandi291 – 2988

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NN6X-ray3.35A1-302[»]
    ProteinModelPortaliQ06265.
    SMRiQ06265. Positions 2-278.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ06265.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 268268ARE bindingAdd
    BLAST

    Sequence similaritiesi

    Belongs to the RNase PH family.Curated

    Phylogenomic databases

    eggNOGiCOG2123.
    HOGENOMiHOG000229504.
    HOVERGENiHBG051523.
    KOiK03678.
    OMAiKMDTGVE.
    OrthoDBiEOG7X9G70.
    PhylomeDBiQ06265.
    TreeFamiTF300092.

    Family and domain databases

    InterProiIPR001247. ExoRNase_PH_dom1.
    IPR015847. ExoRNase_PH_dom2.
    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.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q06265-1) [UniParc]FASTAAdd to Basket

    Also known as: PM/SCL-75c-alpha

    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

    MKETPLSNCE RRFLLRAIEE KKRLDGRQTY DYRNIRISFG TDYGCCIVEL    50
    GKTRVLGQVS CELVSPKLNR ATEGILFFNL ELSQMAAPAF EPGRQSDLLV 100
    KLNRLMERCL RNSKCIDTES LCVVAGEKVW QIRVDLHLLN HDGNIIDAAS 150
    IAAIVALCHF RRPDVSVQGD EVTLYTPEER DPVPLSIHHM PICVSFAFFQ 200
    QGTYLLVDPN EREERVMDGL LVIAMNKHRE ICTIQSSGGI MLLKDQVLRC 250
    SKIAGVKVAE ITELILKALE NDQKVRKEGG KFGFAESIAN QRITAFKMEK 300
    APIDTSDVEE KAEEIIAEAE PPSEVVSTPV LWTPGTAQIG EGVENSWGDL 350
    EDSEKEDDEG GGDQAIILDG IKMDTGVEVS DIGSQDAPII LSDSEEEEMI 400
    ILEPDKNPKK IRTQTTSAKQ EKAPSKKPVK RRKKKRAAN 439
    Length:439
    Mass (Da):48,949
    Last modified:May 15, 2007 - v3
    Checksum:i7E27322F094ED3F3
    GO
    Isoform 2 (identifier: Q06265-2) [UniParc]FASTAAdd to Basket

    Also known as: PM/SCL-75c-beta

    The sequence of this isoform differs from the canonical sequence as follows:
         385-385: Q → QELGFHHVGQTGLEFLTS

    Show »
    Length:456
    Mass (Da):50,803
    Checksum:i693B31BE41C55545
    GO
    Isoform 3 (identifier: Q06265-3) [UniParc]FASTAAdd to Basket

    Also known as: PM/SCL-75a-alpha

    The sequence of this isoform differs from the canonical sequence as follows:
         1-84: Missing.

    Show »
    Length:355
    Mass (Da):39,235
    Checksum:iDC37BB31767B6621
    GO
    Isoform 4 (identifier: Q06265-4) [UniParc]FASTAAdd to Basket

    Also known as: PM/SCL-75a-beta

    The sequence of this isoform differs from the canonical sequence as follows:
         1-84: Missing.
         385-385: Q → QELGFHHVGQTGLEFLTS

    Show »
    Length:372
    Mass (Da):41,089
    Checksum:iDB666F47B5422E7E
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti366 – 3661I → V.
    Corresponds to variant rs1803183 [ dbSNP | Ensembl ].
    VAR_051867
    Natural varianti425 – 4251S → T.
    Corresponds to variant rs1051881 [ dbSNP | Ensembl ].
    VAR_014924

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8484Missing in isoform 3 and isoform 4. 2 PublicationsVSP_025555Add
    BLAST
    Alternative sequencei385 – 3851Q → QELGFHHVGQTGLEFLTS in isoform 2 and isoform 4. 2 PublicationsVSP_025556

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58460 mRNA. Translation: AAA58384.1.
    U09215 mRNA. Translation: AAA18832.1.
    AJ505989 mRNA. Translation: CAD44530.1.
    AJ517294 mRNA. Translation: CAD56889.1.
    AC079341 Genomic DNA. Translation: AAY40968.1.
    CCDSiCCDS34057.1. [Q06265-2]
    CCDS3722.2. [Q06265-1]
    PIRiG01425.
    RefSeqiNP_001029366.1. NM_001034194.1. [Q06265-2]
    NP_005024.2. NM_005033.2. [Q06265-1]
    UniGeneiHs.91728.

    Genome annotation databases

    EnsembliENST00000243498; ENSP00000243498; ENSG00000123737. [Q06265-1]
    ENST00000379663; ENSP00000368984; ENSG00000123737. [Q06265-2]
    GeneIDi5393.
    KEGGihsa:5393.
    UCSCiuc003idz.3. human. [Q06265-2]
    uc003iea.3. human. [Q06265-1]

    Polymorphism databases

    DMDMi147744559.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58460 mRNA. Translation: AAA58384.1 .
    U09215 mRNA. Translation: AAA18832.1 .
    AJ505989 mRNA. Translation: CAD44530.1 .
    AJ517294 mRNA. Translation: CAD56889.1 .
    AC079341 Genomic DNA. Translation: AAY40968.1 .
    CCDSi CCDS34057.1. [Q06265-2 ]
    CCDS3722.2. [Q06265-1 ]
    PIRi G01425.
    RefSeqi NP_001029366.1. NM_001034194.1. [Q06265-2 ]
    NP_005024.2. NM_005033.2. [Q06265-1 ]
    UniGenei Hs.91728.

    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 A 1-302 [» ]
    ProteinModelPortali Q06265.
    SMRi Q06265. Positions 2-278.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111402. 17 interactions.
    IntActi Q06265. 15 interactions.
    MINTi MINT-1036055.
    STRINGi 9606.ENSP00000368984.

    PTM databases

    PhosphoSitei Q06265.

    Polymorphism databases

    DMDMi 147744559.

    Proteomic databases

    MaxQBi Q06265.
    PaxDbi Q06265.
    PRIDEi Q06265.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000243498 ; ENSP00000243498 ; ENSG00000123737 . [Q06265-1 ]
    ENST00000379663 ; ENSP00000368984 ; ENSG00000123737 . [Q06265-2 ]
    GeneIDi 5393.
    KEGGi hsa:5393.
    UCSCi uc003idz.3. human. [Q06265-2 ]
    uc003iea.3. human. [Q06265-1 ]

    Organism-specific databases

    CTDi 5393.
    GeneCardsi GC04P122722.
    HGNCi HGNC:9137. EXOSC9.
    HPAi HPA041838.
    HPA048257.
    MIMi 606180. gene.
    neXtProti NX_Q06265.
    PharmGKBi PA33463.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2123.
    HOGENOMi HOG000229504.
    HOVERGENi HBG051523.
    KOi K03678.
    OMAi KMDTGVE.
    OrthoDBi EOG7X9G70.
    PhylomeDBi Q06265.
    TreeFami TF300092.

    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 Q06265.
    GeneWikii Exosome_component_9.
    GenomeRNAii 5393.
    NextBioi 20906.
    PROi Q06265.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q06265.
    Bgeei Q06265.
    CleanExi HS_EXOSC9.
    Genevestigatori Q06265.

    Family and domain databases

    InterProi IPR001247. ExoRNase_PH_dom1.
    IPR015847. ExoRNase_PH_dom2.
    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. "Molecular characterization of an autoantigen of PM-Scl in the polymyositis/scleroderma overlap syndrome: a unique and complete human cDNA encoding an apparent 75-kD acidic protein of the nucleolar complex."
      Alderuccio F., Chan E.K.L., Tan E.M.
      J. Exp. Med. 173:941-952(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Lymphoblastoma.
    2. "Nucleotide sequence of an alternatively spliced cDNA coding for PM-Scl-75, an autoantigen of the Polymyositis/Scleroderma overlap syndrome."
      Stahnke G., Haubruck H.
      Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    3. "The association of the human PM/Scl-75 autoantigen with the exosome is dependent on a newly identified N terminus."
      Raijmakers R., Egberts W.V., van Venrooij W.J., Pruijn G.J.
      J. Biol. Chem. 278:30698-30704(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, IDENTIFICATION IN THE RNA EXOSOME COMPLEX.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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.
    6. "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.
    7. "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, ARE BINDING.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Adenylation and exosome-mediated degradation of cotranscriptionally cleaved pre-messenger RNA in human cells."
      West S., Gromak N., Norbury C.J., Proudfoot N.J.
      Mol. Cell 21:437-443(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NUCLEAR PRE-MRNA DEGRADATION.
    10. "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.
    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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-392 AND SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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].
    14. "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-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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.
    17. "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-306; SER-392 AND SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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.
    22. Erratum
      Liu Q., Greimann J.C., Lima C.D.
      Cell 131:188-189(2007)

    Entry informationi

    Entry nameiEXOS9_HUMAN
    AccessioniPrimary (citable) accession number: Q06265
    Secondary accession number(s): Q12883
    , Q4W5P5, Q86Y41, Q86Y48
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: May 15, 2007
    Last modified: October 1, 2014
    This is version 139 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, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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