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Q9Y3B2

- EXOS1_HUMAN

UniProt

Q9Y3B2 - EXOS1_HUMAN

Protein

Exosome complex component CSL4

Gene

EXOSC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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. EXOSC1 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC6 and EXOSC8.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. RNA binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Biological processi

    rRNA processing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exosome complex component CSL4
    Alternative name(s):
    Exosome component 1
    Gene namesi
    Name:EXOSC1
    Synonyms:CSL4
    ORF Names:CGI-108
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:17286. EXOSC1.

    Subcellular locationi

    Nucleusnucleolus 1 Publication. Nucleus 1 Publication. Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. exosome (RNase complex) Source: UniProtKB
    3. nucleolus Source: UniProtKB
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Exosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134900737.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 195195Exosome complex component CSL4PRO_0000087127Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y3B2.
    PaxDbiQ9Y3B2.
    PRIDEiQ9Y3B2.

    PTM databases

    PhosphoSiteiQ9Y3B2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y3B2.
    BgeeiQ9Y3B2.
    CleanExiHS_EXOSC1.
    GenevestigatoriQ9Y3B2.

    Organism-specific databases

    HPAiHPA038370.

    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 EXOSC5, EXOSC7 and EXOSC10. Interacts with DDX60.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EXOSC4Q9NPD34EBI-371892,EBI-371823
    EXOSC5Q9NQT410EBI-371892,EBI-371876
    EXOSC7Q150246EBI-371892,EBI-371841

    Protein-protein interaction databases

    BioGridi119220. 27 interactions.
    IntActiQ9Y3B2. 25 interactions.
    MINTiMINT-3085607.
    STRINGi9606.ENSP00000359939.

    Structurei

    Secondary structure

    1
    195
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 164
    Turni17 – 193
    Beta strandi23 – 253
    Beta strandi27 – 293
    Beta strandi32 – 343
    Beta strandi41 – 455
    Beta strandi49 – 524
    Beta strandi70 – 789
    Beta strandi80 – 9314
    Beta strandi103 – 1064
    Helixi107 – 1093
    Helixi118 – 1203
    Beta strandi124 – 13512
    Beta strandi142 – 1454
    Beta strandi148 – 1503
    Beta strandi159 – 1613
    Beta strandi165 – 1684
    Beta strandi171 – 1733
    Turni175 – 1784

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NN6X-ray3.35I1-195[»]
    ProteinModelPortaliQ9Y3B2.
    SMRiQ9Y3B2. Positions 6-185.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y3B2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini66 – 14782S1 motifAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CSL4 family.Curated
    Contains 1 S1 motif domain.Curated

    Phylogenomic databases

    eggNOGiCOG1096.
    HOGENOMiHOG000177330.
    HOVERGENiHBG051516.
    InParanoidiQ9Y3B2.
    KOiK07573.
    OMAiVTSINPR.
    OrthoDBiEOG7V4B0J.
    PhylomeDBiQ9Y3B2.
    TreeFamiTF316607.

    Family and domain databases

    InterProiIPR019495. EXOSC1.
    IPR025721. Exosome_cplx_N_dom.
    IPR012340. NA-bd_OB-fold.
    IPR022967. RNA-binding_domain_S1.
    [Graphical view]
    PfamiPF14382. ECR1_N. 1 hit.
    PF10447. EXOSC1. 1 hit.
    [Graphical view]
    SMARTiSM00316. S1. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9Y3B2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPPVRYCIP GERLCNLEEG SPGSGTYTRH GYIFSSLAGC LMKSSENGAL    50
    PVVSVVRETE SQLLPDVGAI VTCKVSSINS RFAKVHILYV GSMPLKNSFR 100
    GTIRKEDVRA TEKDKVEIYK SFRPGDIVLA KVISLGDAQS NYLLTTAENE 150
    LGVVVAHSES GIQMVPISWC EMQCPKTHTK EFRKVARVQP EFLQT 195
    Length:195
    Mass (Da):21,452
    Last modified:November 1, 1999 - v1
    Checksum:iE9C3B0A66F911195
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF151866 mRNA. Translation: AAD34103.1.
    AK313717 mRNA. Translation: BAG36460.1.
    AL355490 Genomic DNA. Translation: CAI40782.1.
    CH471066 Genomic DNA. Translation: EAW49936.1.
    BC022067 mRNA. Translation: AAH22067.1.
    CCDSiCCDS7459.1.
    RefSeqiNP_057130.1. NM_016046.3.
    UniGeneiHs.632089.

    Genome annotation databases

    EnsembliENST00000370902; ENSP00000359939; ENSG00000171311.
    GeneIDi51013.
    KEGGihsa:51013.
    UCSCiuc001kni.3. human.

    Polymorphism databases

    DMDMi14285410.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF151866 mRNA. Translation: AAD34103.1 .
    AK313717 mRNA. Translation: BAG36460.1 .
    AL355490 Genomic DNA. Translation: CAI40782.1 .
    CH471066 Genomic DNA. Translation: EAW49936.1 .
    BC022067 mRNA. Translation: AAH22067.1 .
    CCDSi CCDS7459.1.
    RefSeqi NP_057130.1. NM_016046.3.
    UniGenei Hs.632089.

    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 I 1-195 [» ]
    ProteinModelPortali Q9Y3B2.
    SMRi Q9Y3B2. Positions 6-185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119220. 27 interactions.
    IntActi Q9Y3B2. 25 interactions.
    MINTi MINT-3085607.
    STRINGi 9606.ENSP00000359939.

    PTM databases

    PhosphoSitei Q9Y3B2.

    Polymorphism databases

    DMDMi 14285410.

    Proteomic databases

    MaxQBi Q9Y3B2.
    PaxDbi Q9Y3B2.
    PRIDEi Q9Y3B2.

    Protocols and materials databases

    DNASUi 51013.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370902 ; ENSP00000359939 ; ENSG00000171311 .
    GeneIDi 51013.
    KEGGi hsa:51013.
    UCSCi uc001kni.3. human.

    Organism-specific databases

    CTDi 51013.
    GeneCardsi GC10M099198.
    HGNCi HGNC:17286. EXOSC1.
    HPAi HPA038370.
    MIMi 606493. gene.
    neXtProti NX_Q9Y3B2.
    PharmGKBi PA134900737.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1096.
    HOGENOMi HOG000177330.
    HOVERGENi HBG051516.
    InParanoidi Q9Y3B2.
    KOi K07573.
    OMAi VTSINPR.
    OrthoDBi EOG7V4B0J.
    PhylomeDBi Q9Y3B2.
    TreeFami TF316607.

    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 Q9Y3B2.
    GeneWikii Exosome_component_1.
    GenomeRNAii 51013.
    NextBioi 53508.
    PROi Q9Y3B2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y3B2.
    Bgeei Q9Y3B2.
    CleanExi HS_EXOSC1.
    Genevestigatori Q9Y3B2.

    Family and domain databases

    InterProi IPR019495. EXOSC1.
    IPR025721. Exosome_cplx_N_dom.
    IPR012340. NA-bd_OB-fold.
    IPR022967. RNA-binding_domain_S1.
    [Graphical view ]
    Pfami PF14382. ECR1_N. 1 hit.
    PF10447. EXOSC1. 1 hit.
    [Graphical view ]
    SMARTi SM00316. S1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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].
    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. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(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].
      Tissue: Brain.
    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. "Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring."
      Raijmakers R., Vree Egberts W., van Venrooij W.J., Pruijn G.J.M.
      J. Mol. Biol. 323:653-663(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN INTERACTION.
    8. "Protein-protein interactions of hCsl4p with other human exosome subunits."
      Raijmakers R., Noordman Y.E., van Venrooij W.J., Pruijn G.J.M.
      J. Mol. Biol. 315:809-818(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EXOSC5; EXOSC7 AND EXOSC10.
    9. "A protein interaction framework for human mRNA degradation."
      Lehner B., Sanderson C.M.
      Genome Res. 14:1315-1323(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN INTERACTION.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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. "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-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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.
    16. "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.
    17. Erratum
      Liu Q., Greimann J.C., Lima C.D.
      Cell 131:188-189(2007)

    Entry informationi

    Entry nameiEXOS1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y3B2
    Secondary accession number(s): B2R9B3, Q5JTH3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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