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Q9VUQ5

- AGO2_DROME

UniProt

Q9VUQ5 - AGO2_DROME

Protein

Protein argonaute-2

Gene

AGO2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 3 (16 Aug 2004)
      Previous versions | rss
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    Functioni

    Essential for RNA interference (RNAi); double-stranded RNA induces potent and specific gene silencing. RNAi is mediated by the RNA-induced silencing complex (RISC), a sequence-specific, multicomponent nuclease that destroys or silences messenger RNAs homologous to the silencing trigger.1 Publication

    Cofactori

    Magnesium or manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi965 – 9651Divalent metal cationBy similarity
    Metal bindingi1037 – 10371Divalent metal cationBy similarity
    Metal bindingi1173 – 11731Divalent metal cationBy similarity

    GO - Molecular functioni

    1. endoribonuclease activity Source: FlyBase
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. siRNA binding Source: FlyBase

    GO - Biological processi

    1. autophagic cell death Source: FlyBase
    2. cellularization Source: FlyBase
    3. defense response to virus Source: FlyBase
    4. dosage compensation by hyperactivation of X chromosome Source: FlyBase
    5. dsRNA transport Source: FlyBase
    6. heterochromatin organization involved in chromatin silencing Source: FlyBase
    7. negative regulation of viral genome replication Source: FlyBase
    8. pole cell formation Source: FlyBase
    9. production of siRNA involved in RNA interference Source: UniProtKB
    10. RNA interference Source: FlyBase
    11. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    12. salivary gland cell autophagic cell death Source: FlyBase
    13. segment polarity determination Source: FlyBase
    14. siRNA loading onto RISC involved in RNA interference Source: FlyBase
    15. syncytial nuclear migration Source: FlyBase
    16. targeting of mRNA for destruction involved in RNA interference Source: FlyBase
    17. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, RNA-mediated gene silencing

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein argonaute-2
    Gene namesi
    Name:AGO2Imported
    ORF Names:CG7439
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0087035. AGO2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: FlyBase
    2. RISC complex Source: FlyBase
    3. RISC-loading complex Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12141214Protein argonaute-2PRO_0000194071Add
    BLAST

    Proteomic databases

    PaxDbiQ9VUQ5.
    PRIDEiQ9VUQ5.

    Expressioni

    Gene expression databases

    BgeeiQ9VUQ5.

    Interactioni

    Subunit structurei

    Interacts with Fmr1 to form a ribonucleoprotein (RNP) complex involved in translation regulation, other components of the complex are mRpL5, mRpL11, Rm62 and Dcr-1. Interacts with Dcr-1 to form components of the RISC. Interacts with cricket paralysis virus protein 1A; this interaction may block the RISC activity.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Fmr1Q9NFU04EBI-442476,EBI-422631

    Protein-protein interaction databases

    BioGridi65002. 9 interactions.
    DIPiDIP-41570N.
    IntActiQ9VUQ5. 7 interactions.
    MINTiMINT-248245.

    Structurei

    Secondary structure

    1
    1214
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi601 – 6033
    Helixi604 – 6118
    Beta strandi618 – 6214
    Helixi623 – 6253
    Helixi627 – 6348
    Beta strandi638 – 6414
    Helixi645 – 6473
    Beta strandi652 – 6554
    Beta strandi658 – 6636
    Turni664 – 6663
    Beta strandi668 – 67710
    Helixi678 – 6836
    Turni684 – 6863
    Beta strandi692 – 6987
    Beta strandi705 – 7084
    Helixi710 – 7123
    Beta strandi713 – 7164
    Turni717 – 7193

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1R6ZX-ray2.80A/P/Z589-726[»]
    1T2RNMR-A602-720[»]
    1T2SNMR-A602-720[»]
    1VYNNMR-A602-740[»]
    3MJ0X-ray2.31A601-723[»]
    ProteinModelPortaliQ9VUQ5.
    SMRiQ9VUQ5. Positions 591-719.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9VUQ5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini608 – 717110PAZPROSITE-ProRule annotationAdd
    BLAST
    Domaini885 – 1186302PiwiPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni681 – 6866Interaction with guide RNASequence Analysis
    Regioni1075 – 10762Interaction with guide RNASequence Analysis
    Regioni1119 – 11279Interaction with guide RNASequence Analysis
    Regioni1156 – 117823Interaction with guide RNASequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi19 – 391373Gln/Gly-richAdd
    BLAST

    Domaini

    PAZ domain provides a major contribution for nucleic acid recognition. PAZ binds oligonucleotides of different lengths and has a strong preference for single-stranded nucleic acids (ssRNA or SSDNA) or RNA duplexes with single-stranded 3' overhangs. Can bind the characteristic two-base 3' overhangs of siRNAs, indicating that it may contribute to the specific and productive incorporation of siRNAs and miRNAs into the RNAi pathway.

    Sequence similaritiesi

    Belongs to the argonaute family. Ago subfamily.Curated
    Contains 1 PAZ domain.PROSITE-ProRule annotation
    Contains 1 Piwi domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG279895.
    GeneTreeiENSGT00640000091312.
    InParanoidiQ9VUQ5.
    KOiK11593.
    OMAiQGQEGGY.
    OrthoDBiEOG722J7S.
    PhylomeDBiQ9VUQ5.

    Family and domain databases

    Gene3Di3.30.420.10. 1 hit.
    InterProiIPR014811. DUF1785.
    IPR003100. PAZ_dom.
    IPR003165. Piwi.
    IPR012337. RNaseH-like_dom.
    [Graphical view]
    PfamiPF08699. DUF1785. 1 hit.
    PF02170. PAZ. 1 hit.
    PF02171. Piwi. 1 hit.
    [Graphical view]
    SMARTiSM00950. Piwi. 1 hit.
    [Graphical view]
    SUPFAMiSSF101690. SSF101690. 1 hit.
    SSF53098. SSF53098. 1 hit.
    PROSITEiPS50821. PAZ. 1 hit.
    PS50822. PIWI. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform B (identifier: Q9VUQ5-1) [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

    MGKKDKNKKG GQDSAAAPQP QQQQKQQQQR QQQPQQLQQP QQLQQPQQLQ     50
    QPQQQQQQQP HQQQQQSSRQ QPSTSSGGSR ASGFQQGGQQ QKSQDAEGWT 100
    AQKKQGKQQV QGWTKQGQQG GHQQGRQGQD GGYQQRPPGQ QQGGHQQGRQ 150
    GQEGGYQQRP PGQQQGGHQQ GRQGQEGGYQ QRPSGQQQGG HQQGRQGQEG 200
    GYQQRPPGQQ QGGHQQGRQG QEGGYQQRPS GQQQGGHQQG RQGQEGGYQQ 250
    RPPGQQQGGH QQGRQGQEGG YQQRPPGQQQ GGHEQGRQGQ EGGYQQRPSG 300
    QQQGGHQQGR QGQEGGYQQR PSGQQQGGHQ QGRQGQEGGY QQRPSGQQQG 350
    GHQQGRQGQE GGYQQRPPGQ QPNQTQSQGQ YQSRGPPQQQ QAAPLPLPPQ 400
    PAGSIKRGTI GKPGQVGINY LDLDLSKMPS VAYHYDVKIM PERPKKFYRQ 450
    AFEQFRVDQL GGAVLAYDGK ASCYSVDKLP LNSQNPEVTV TDRNGRTLRY 500
    TIEIKETGDS TIDLKSLTTY MNDRIFDKPM RAMQCVEVVL ASPCHNKAIR 550
    VGRSFFKMSD PNNRHELDDG YEALVGLYQA FMLGDRPFLN VDISHKSFPI 600
    SMPMIEYLER FSLKAKINNT TNLDYSRRFL EPFLRGINVV YTPPQSFQSA 650
    PRVYRVNGLS RAPASSETFE HDGKKVTIAS YFHSRNYPLK FPQLHCLNVG 700
    SSIKSILLPI ELCSIEEGQA LNRKDGATQV ANMIKYAATS TNVRKRKIMN 750
    LLQYFQHNLD PTISRFGIRI ANDFIVVSTR VLSPPQVEYH SKRFTMVKNG 800
    SWRMDGMKFL EPKPKAHKCA VLYCDPRSGR KMNYTQLNDF GNLIISQGKA 850
    VNISLDSDVT YRPFTDDERS LDTIFADLKR SQHDLAIVII PQFRISYDTI 900
    KQKAELQHGI LTQCIKQFTV ERKCNNQTIG NILLKINSKL NGINHKIKDD 950
    PRLPMMKNTM YIGADVTHPS PDQREIPSVV GVAASHDPYG ASYNMQYRLQ 1000
    RGALEEIEDM FSITLEHLRV YKEYRNAYPD HIIYYRDGVS DGQFPKIKNE 1050
    ELRCIKQACD KVGCKPKICC VIVVKRHHTR FFPSGDVTTS NKFNNVDPGT 1100
    VVDRTIVHPN EMQFFMVSHQ AIQGTAKPTR YNVIENTGNL DIDLLQQLTY 1150
    NLCHMFPRCN RSVSYPAPAY LAHLVAARGR VYLTGTNRFL DLKKEYAKRT 1200
    IVPEFMKKNP MYFV 1214
    Length:1,214
    Mass (Da):136,850
    Last modified:August 16, 2004 - v3
    Checksum:i0DC73AF09CC33F73
    GO
    Isoform C (identifier: Q9VUQ5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-6: MGKKDK → MHFPITTPE

    Note: No experimental confirmation available.

    Show »
    Length:1,217
    Mass (Da):137,216
    Checksum:i7C794ABF4D993EAF
    GO

    Sequence cautioni

    The sequence AAM11104.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti201 – 2011G → D in AAO39550. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti714 – 7141S → R in strain: 186. 1 Publication
    Natural varianti740 – 7401S → P in strain: 130. 1 Publication
    Natural varianti783 – 7831S → N in strain: 138, 140 and 196. 2 Publications
    Natural varianti835 – 8351T → A in strain: 128, 130, 138, 140, 141, 186, 187 and 196. 2 Publications
    Natural varianti854 – 8541S → T in strain: 128, 130, 138, 140, 141, 186, 187 and 196. 2 Publications
    Natural varianti866 – 8661D → E in strain: 128, 130, 141, 186 and 187. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 66MGKKDK → MHFPITTPE in isoform C. 1 PublicationVSP_050781

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014296 Genomic DNA. Translation: AAF49619.2.
    AE014296 Genomic DNA. Translation: AAF49620.2.
    BT003546 mRNA. Translation: AAO39550.1.
    BT099682 mRNA. Translation: ACV44468.1.
    DQ228766 Genomic DNA. Translation: ABB54719.1.
    DQ228767 Genomic DNA. Translation: ABB54720.1.
    DQ228768 Genomic DNA. Translation: ABB54721.1.
    DQ228769 Genomic DNA. Translation: ABB54722.1.
    DQ228770 Genomic DNA. Translation: ABB54723.1.
    DQ228771 Genomic DNA. Translation: ABB54724.1.
    DQ228772 Genomic DNA. Translation: ABB54725.1.
    DQ228773 Genomic DNA. Translation: ABB54726.1.
    AY094751 mRNA. Translation: AAM11104.1. Different initiation.
    RefSeqiNP_648775.1. NM_140518.3. [Q9VUQ5-1]
    NP_730054.1. NM_168626.3. [Q9VUQ5-2]
    UniGeneiDm.9677.

    Genome annotation databases

    EnsemblMetazoaiFBtr0075559; FBpp0075312; FBgn0087035. [Q9VUQ5-1]
    GeneIDi39683.
    KEGGidme:Dmel_CG7439.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014296 Genomic DNA. Translation: AAF49619.2 .
    AE014296 Genomic DNA. Translation: AAF49620.2 .
    BT003546 mRNA. Translation: AAO39550.1 .
    BT099682 mRNA. Translation: ACV44468.1 .
    DQ228766 Genomic DNA. Translation: ABB54719.1 .
    DQ228767 Genomic DNA. Translation: ABB54720.1 .
    DQ228768 Genomic DNA. Translation: ABB54721.1 .
    DQ228769 Genomic DNA. Translation: ABB54722.1 .
    DQ228770 Genomic DNA. Translation: ABB54723.1 .
    DQ228771 Genomic DNA. Translation: ABB54724.1 .
    DQ228772 Genomic DNA. Translation: ABB54725.1 .
    DQ228773 Genomic DNA. Translation: ABB54726.1 .
    AY094751 mRNA. Translation: AAM11104.1 . Different initiation.
    RefSeqi NP_648775.1. NM_140518.3. [Q9VUQ5-1 ]
    NP_730054.1. NM_168626.3. [Q9VUQ5-2 ]
    UniGenei Dm.9677.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1R6Z X-ray 2.80 A/P/Z 589-726 [» ]
    1T2R NMR - A 602-720 [» ]
    1T2S NMR - A 602-720 [» ]
    1VYN NMR - A 602-740 [» ]
    3MJ0 X-ray 2.31 A 601-723 [» ]
    ProteinModelPortali Q9VUQ5.
    SMRi Q9VUQ5. Positions 591-719.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 65002. 9 interactions.
    DIPi DIP-41570N.
    IntActi Q9VUQ5. 7 interactions.
    MINTi MINT-248245.

    Proteomic databases

    PaxDbi Q9VUQ5.
    PRIDEi Q9VUQ5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0075559 ; FBpp0075312 ; FBgn0087035 . [Q9VUQ5-1 ]
    GeneIDi 39683.
    KEGGi dme:Dmel_CG7439.

    Organism-specific databases

    CTDi 27161.
    FlyBasei FBgn0087035. AGO2.

    Phylogenomic databases

    eggNOGi NOG279895.
    GeneTreei ENSGT00640000091312.
    InParanoidi Q9VUQ5.
    KOi K11593.
    OMAi QGQEGGY.
    OrthoDBi EOG722J7S.
    PhylomeDBi Q9VUQ5.

    Miscellaneous databases

    EvolutionaryTracei Q9VUQ5.
    GenomeRNAii 39683.
    NextBioi 814859.

    Gene expression databases

    Bgeei Q9VUQ5.

    Family and domain databases

    Gene3Di 3.30.420.10. 1 hit.
    InterProi IPR014811. DUF1785.
    IPR003100. PAZ_dom.
    IPR003165. Piwi.
    IPR012337. RNaseH-like_dom.
    [Graphical view ]
    Pfami PF08699. DUF1785. 1 hit.
    PF02170. PAZ. 1 hit.
    PF02171. Piwi. 1 hit.
    [Graphical view ]
    SMARTi SM00950. Piwi. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101690. SSF101690. 1 hit.
    SSF53098. SSF53098. 1 hit.
    PROSITEi PS50821. PAZ. 1 hit.
    PS50822. PIWI. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley1 Publication.
    2. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C).
      Strain: BerkeleyImported.
      Tissue: Embryo.
    4. "Natural selection drives extremely rapid evolution in antiviral RNAi genes."
      Obbard D.J., Jiggins F.M., Halligan D.L., Little T.J.
      Curr. Biol. 16:580-585(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 376-1214, VARIANTS ARG-714; PRO-740; ASN-783; ALA-835; THR-854 AND GLU-866.
      Strain: 128, 130, 138, 140, 141, 186, 187 and 196.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 449-1214, VARIANTS ASN-783; ALA-835 AND THR-854.
      Strain: Berkeley1 Publication.
      Tissue: Ovary1 Publication.
    6. "Argonaute2, a link between genetic and biochemical analyses of RNAi."
      Hammond S.M., Boettcher S., Caudy A.A., Kobayashi R., Hannon G.J.
      Science 293:1146-1150(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 506-515; 525-531; 554-557; 617-627; 662-674; 809-815 AND 1181-1188 (ISOFORM B), FUNCTION, INTERACTION WITH DCR-1.
    7. "A Drosophila fragile X protein interacts with components of RNAi and ribosomal proteins."
      Ishizuka A., Siomi M.C., Siomi H.
      Genes Dev. 16:2497-2508(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FMR1.
    8. "Cricket paralysis virus antagonizes Argonaute 2 to modulate antiviral defense in Drosophila."
      Nayak A., Berry B., Tassetto M., Kunitomi M., Acevedo A., Deng C., Krutchinsky A., Gross J., Antoniewski C., Andino R.
      Nat. Struct. Mol. Biol. 17:547-554(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CRICKET PARALYSIS VIRUS PROTEIN 1A.
    9. "The crystal structure of the Argonaute2 PAZ domain reveals an RNA binding motif in RNAi effector complexes."
      Song J.J., Liu J., Tolia N.H., Schneiderman J., Smith S.K., Martienssen R.A., Hannon G.J., Joshua-Tor L.
      Nat. Struct. Biol. 10:1026-1032(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 591-726.
    10. "Structure and nucleic-acid binding of the Drosophila Argonaute 2 PAZ domain."
      Lingel A., Simon B., Izaurralde E., Sattler M.
      Nature 426:465-469(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 602-740.
    11. "Nucleic acid 3'-end recognition by the Argonaute2 PAZ domain."
      Lingel A., Simon B., Izaurralde E., Sattler M.
      Nat. Struct. Mol. Biol. 11:576-577(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 605-720.

    Entry informationi

    Entry nameiAGO2_DROME
    AccessioniPrimary (citable) accession number: Q9VUQ5
    Secondary accession number(s): C7LAD2
    , Q2Q3Y0, Q2Q3Y1, Q2Q3Y3, Q2Q3Y4, Q2Q3Y5, Q86P07, Q8T3N2, Q9VUQ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 107 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3