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O04379

- AGO1_ARATH

UniProt

O04379 - AGO1_ARATH

Protein

Protein argonaute 1

Gene

AGO1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Involved in RNA-mediated post-transcriptional gene silencing (PTGS). Main component of the RNA-induced silencing complex (RISC) that binds to a short guide RNA such as microRNA (miRNA) or small interfering RNA (siRNA). RISC uses the mature miRNA or siRNA as a guide for slicer-directed cleavage of homologous mRNAs to repress gene expression. Requires DRB1 for directional loading of the small RNA duplex (guide stand and passenger strand) onto RISC for passenger strand degradation. Unlike animal RISC that associates in high molecular weight complex, Arabidopsis RISC is probably composed only of the AGO1 protein and associated RNA without any other proteins. Associates mainly with miRNAs of 21 nucleotide in length and preferentially recruits small RNAs with a 5' terminal uridine. Associates with 22 nucleotide miRNAs to trigger RDR6-dependent secondary siRNAs biogenesis. This pathway amplifies silencing by using the target RNA as substrate to generate secondary siRNAs. Binds to miR168 which targets its own mRNA for repression, establishing a homeostatic regulatory loop. Involved in antiviral RNA silencing by contributing to viral RNA clearance. Is capable of targeting viral RNAs with more compact structures than AGO7 which favors less structured RNA targets. May not associate with 24 nucleotide siRNAs involved in chromatin silencing. Essential for multiple processes in development. Essential for proper development of leaves and floral organs, and formation of axillary meristems. Like AGO10, required for stem cell function and organ polarity.11 Publications

    Cofactori

    Magnesium or manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi760 – 7601Divalent metal cationBy similarity
    Metal bindingi846 – 8461Divalent metal cationBy similarity
    Metal bindingi986 – 9861Divalent metal cationBy similarity

    GO - Molecular functioni

    1. endoribonuclease activity Source: TAIR
    2. metal ion binding Source: UniProtKB-KW
    3. miRNA binding Source: TAIR
    4. protein binding Source: TAIR
    5. RNA binding Source: UniProtKB-KW
    6. siRNA binding Source: TAIR

    GO - Biological processi

    1. adaxial/abaxial pattern specification Source: TAIR
    2. adventitious root development Source: TAIR
    3. auxin metabolic process Source: TAIR
    4. defense response Source: UniProtKB-KW
    5. embryo development ending in seed dormancy Source: TAIR
    6. gene silencing by miRNA Source: TAIR
    7. gene silencing by RNA Source: UniProtKB-KW
    8. innate immune response Source: TAIR
    9. leaf morphogenesis Source: TAIR
    10. leaf proximal/distal pattern formation Source: TAIR
    11. leaf vascular tissue pattern formation Source: TAIR
    12. multicellular organismal development Source: UniProtKB-KW
    13. posttranscriptional gene silencing Source: TAIR
    14. regulation of transcription, DNA-templated Source: UniProtKB-KW
    15. regulation of translation Source: UniProtKB-KW
    16. response to auxin Source: TAIR
    17. response to far red light Source: TAIR
    18. RNA interference Source: TAIR
    19. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    20. stem cell development Source: UniProtKB
    21. transcription, DNA-templated Source: UniProtKB-KW
    22. viral process Source: UniProtKB-KW
    23. virus induced gene silencing Source: TAIR

    Keywords - Molecular functioni

    Developmental protein, Repressor, Ribonucleoprotein

    Keywords - Biological processi

    Host-virus interaction, Plant defense, RNA-mediated gene silencing, Transcription, Transcription regulation, Translation regulation

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_184981. Small interfering RNA (siRNA) biogenesis.
    REACT_190885. Post-transcriptional silencing by small RNAs.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein argonaute 1
    Gene namesi
    Name:AGO1
    Ordered Locus Names:At1g48410
    ORF Names:F11A17.3, T1N15.2
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G48410.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: TAIR
    2. cytosol Source: TAIR
    3. extrinsic component of membrane Source: TAIR
    4. nucleus Source: TAIR
    5. ribonucleoprotein complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Narrow rosette leaves. Single shoot bearing a terminal inflorescence. Abnormal inflorescence with infertile flowers and filamentous organs.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10481048Protein argonaute 1PRO_0000194068Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1001 – 10011Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO04379.
    PRIDEiO04379.

    Expressioni

    Tissue specificityi

    Widely expressed at low levels.

    Developmental stagei

    Expressed throughout all developmental stages.

    Gene expression databases

    ArrayExpressiO04379.
    GenevestigatoriO04379.

    Interactioni

    Subunit structurei

    Interacts with turnip yellows virus (TuYV) protein P0 (via F-box-like domain); this interaction targets AGO1 for degradation, and thereby suppresses its function in silencing. Interacts with turnip crinkle virus (TCV) capsid protein P38 (via GW motifs); these interactions inhibit RNA silencing ability of AGO1. Interacts (via PAZ domain) with cucumber mosaic virus (CMV) protein 2b; these interactions inhibit AGO1 function in RNA silencing. Interacts with SDE3.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AMP1Q9M1S82EBI-6912745,EBI-6912802

    Protein-protein interaction databases

    BioGridi26487. 4 interactions.
    IntActiO04379. 1 interaction.

    Structurei

    Secondary structure

    1
    1048
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi596 – 5983
    Beta strandi604 – 6096
    Helixi616 – 63217
    Helixi650 – 6523
    Helixi653 – 66614
    Beta strandi676 – 6816
    Helixi688 – 69811
    Beta strandi704 – 7085
    Helixi709 – 7146
    Helixi717 – 73014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3VNAX-ray2.00A592-739[»]
    3VNBX-ray1.50A592-739[»]
    4G0PX-ray1.80A593-738[»]
    4G0QX-ray1.80A593-738[»]
    4G0XX-ray1.35A593-738[»]
    4G0YX-ray1.65A593-738[»]
    4G0ZX-ray1.75A593-738[»]
    ProteinModelPortaliO04379.
    SMRiO04379. Positions 175-996.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini391 – 501111PAZPROSITE-ProRule annotationAdd
    BLAST
    Domaini676 – 997322PiwiPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni886 – 8872Interaction with guide RNASequence Analysis
    Regioni932 – 9409Interaction with guide RNASequence Analysis
    Regioni969 – 99123Interaction with guide RNASequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi13 – 10492Gly-richAdd
    BLAST

    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.
    HOGENOMiHOG000116043.
    InParanoidiO04379.
    KOiK11593.
    OMAiGRSMPEP.
    PhylomeDBiO04379.

    Family and domain databases

    Gene3Di3.30.420.10. 1 hit.
    InterProiIPR024357. Argonaut_Gly-rich.
    IPR014811. DUF1785.
    IPR003100. PAZ_dom.
    IPR003165. Piwi.
    IPR012337. RNaseH-like_dom.
    [Graphical view]
    PfamiPF08699. DUF1785. 1 hit.
    PF12764. Gly-rich_Ago1. 1 hit.
    PF02170. PAZ. 1 hit.
    PF02171. Piwi. 1 hit.
    [Graphical view]
    SMARTiSM00949. PAZ. 1 hit.
    SM00950. Piwi. 1 hit.
    [Graphical view]
    SUPFAMiSSF101690. SSF101690. 2 hits.
    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 1 (identifier: O04379-1) [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

    MVRKRRTDAP SEGGEGSGSR EAGPVSGGGR GSQRGGFQQG GGQHQGGRGY     50
    TPQPQQGGRG GRGYGQPPQQ QQQYGGPQEY QGRGRGGPPH QGGRGGYGGG 100
    RGGGPSSGPP QRQSVPELHQ ATSPTYQAVS SQPTLSEVSP TQVPEPTVLA 150
    QQFEQLSVEQ GAPSQAIQPI PSSSKAFKFP MRPGKGQSGK RCIVKANHFF 200
    AELPDKDLHH YDVTITPEVT SRGVNRAVMK QLVDNYRDSH LGSRLPAYDG 250
    RKSLYTAGPL PFNSKEFRIN LLDEEVGAGG QRREREFKVV IKLVARADLH 300
    HLGMFLEGKQ SDAPQEALQV LDIVLRELPT SRYIPVGRSF YSPDIGKKQS 350
    LGDGLESWRG FYQSIRPTQM GLSLNIDMSS TAFIEANPVI QFVCDLLNRD 400
    ISSRPLSDAD RVKIKKALRG VKVEVTHRGN MRRKYRISGL TAVATRELTF 450
    PVDERNTQKS VVEYFHETYG FRIQHTQLPC LQVGNSNRPN YLPMEVCKIV 500
    EGQRYSKRLN ERQITALLKV TCQRPIDREK DILQTVQLND YAKDNYAQEF 550
    GIKISTSLAS VEARILPPPW LKYHESGREG TCLPQVGQWN MMNKKMINGG 600
    TVNNWICINF SRQVQDNLAR TFCQELAQMC YVSGMAFNPE PVLPPVSARP 650
    EQVEKVLKTR YHDATSKLSQ GKEIDLLIVI LPDNNGSLYG DLKRICETEL 700
    GIVSQCCLTK HVFKMSKQYM ANVALKINVK VGGRNTVLVD ALSRRIPLVS 750
    DRPTIIFGAD VTHPHPGEDS SPSIAAVVAS QDWPEITKYA GLVCAQAHRQ 800
    ELIQDLFKEW KDPQKGVVTG GMIKELLIAF RRSTGHKPLR IIFYRDGVSE 850
    GQFYQVLLYE LDAIRKACAS LEAGYQPPVT FVVVQKRHHT RLFAQNHNDR 900
    HSVDRSGNIL PGTVVDSKIC HPTEFDFYLC SHAGIQGTSR PAHYHVLWDE 950
    NNFTADGLQS LTNNLCYTYA RCTRSVSIVP PAYYAHLAAF RARFYMEPET 1000
    SDSGSMASGS MARGGGMAGR STRGPNVNAA VRPLPALKEN VKRVMFYC 1048
    Length:1,048
    Mass (Da):116,191
    Last modified:July 1, 1997 - v1
    Checksum:i3E5146343A09C541
    GO
    Isoform 2 (identifier: O04379-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         332-332: R → RIR

    Note: May be due to a competing acceptor splice site. No experimental confirmation available.

    Show »
    Length:1,050
    Mass (Da):116,460
    Checksum:i233B89E5E4D9E1EC
    GO

    Sequence cautioni

    The sequence AAF79718.1 differs from that shown. Reason: Erroneous gene model prediction.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei332 – 3321R → RIR in isoform 2. 1 PublicationVSP_040612

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U91995 mRNA. Translation: AAC18440.1.
    AC007932 Genomic DNA. Translation: AAD49755.1.
    AC020889 Genomic DNA. Translation: AAF79718.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE32287.1.
    CP002684 Genomic DNA. Translation: AEE32288.1.
    CP002684 Genomic DNA. Translation: AEE32289.1.
    BT000941 mRNA. Translation: AAN41341.1.
    AK227868 mRNA. Translation: BAE99844.1.
    RefSeqiNP_001185169.1. NM_001198240.1. [O04379-2]
    NP_175274.1. NM_103737.3. [O04379-1]
    NP_849784.1. NM_179453.2. [O04379-2]
    UniGeneiAt.21124.

    Genome annotation databases

    EnsemblPlantsiAT1G48410.1; AT1G48410.1; AT1G48410. [O04379-1]
    GeneIDi841262.
    KEGGiath:AT1G48410.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U91995 mRNA. Translation: AAC18440.1 .
    AC007932 Genomic DNA. Translation: AAD49755.1 .
    AC020889 Genomic DNA. Translation: AAF79718.1 . Sequence problems.
    CP002684 Genomic DNA. Translation: AEE32287.1 .
    CP002684 Genomic DNA. Translation: AEE32288.1 .
    CP002684 Genomic DNA. Translation: AEE32289.1 .
    BT000941 mRNA. Translation: AAN41341.1 .
    AK227868 mRNA. Translation: BAE99844.1 .
    RefSeqi NP_001185169.1. NM_001198240.1. [O04379-2 ]
    NP_175274.1. NM_103737.3. [O04379-1 ]
    NP_849784.1. NM_179453.2. [O04379-2 ]
    UniGenei At.21124.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3VNA X-ray 2.00 A 592-739 [» ]
    3VNB X-ray 1.50 A 592-739 [» ]
    4G0P X-ray 1.80 A 593-738 [» ]
    4G0Q X-ray 1.80 A 593-738 [» ]
    4G0X X-ray 1.35 A 593-738 [» ]
    4G0Y X-ray 1.65 A 593-738 [» ]
    4G0Z X-ray 1.75 A 593-738 [» ]
    ProteinModelPortali O04379.
    SMRi O04379. Positions 175-996.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 26487. 4 interactions.
    IntActi O04379. 1 interaction.

    Proteomic databases

    PaxDbi O04379.
    PRIDEi O04379.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G48410.1 ; AT1G48410.1 ; AT1G48410 . [O04379-1 ]
    GeneIDi 841262.
    KEGGi ath:AT1G48410.

    Organism-specific databases

    TAIRi AT1G48410.

    Phylogenomic databases

    eggNOGi NOG279895.
    HOGENOMi HOG000116043.
    InParanoidi O04379.
    KOi K11593.
    OMAi GRSMPEP.
    PhylomeDBi O04379.

    Enzyme and pathway databases

    Reactomei REACT_184981. Small interfering RNA (siRNA) biogenesis.
    REACT_190885. Post-transcriptional silencing by small RNAs.

    Gene expression databases

    ArrayExpressi O04379.
    Genevestigatori O04379.

    Family and domain databases

    Gene3Di 3.30.420.10. 1 hit.
    InterProi IPR024357. Argonaut_Gly-rich.
    IPR014811. DUF1785.
    IPR003100. PAZ_dom.
    IPR003165. Piwi.
    IPR012337. RNaseH-like_dom.
    [Graphical view ]
    Pfami PF08699. DUF1785. 1 hit.
    PF12764. Gly-rich_Ago1. 1 hit.
    PF02170. PAZ. 1 hit.
    PF02171. Piwi. 1 hit.
    [Graphical view ]
    SMARTi SM00949. PAZ. 1 hit.
    SM00950. Piwi. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101690. SSF101690. 2 hits.
    SSF53098. SSF53098. 1 hit.
    PROSITEi PS50821. PAZ. 1 hit.
    PS50822. PIWI. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "AGO1 defines a novel locus of Arabidopsis controlling leaf development."
      Bohmert K., Camus I., Bellini C., Bouchez D., Caboche M., Benning C.
      EMBO J. 17:170-180(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE.
      Strain: cv. Columbia.
      Tissue: Leaf.
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: cv. Columbia.
    5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-346 (ISOFORM 2).
      Strain: cv. Columbia.
    6. "The role of ARGONAUTE1 (AGO1) in meristem formation and identity."
      Kidner C.A., Martienssen R.A.
      Dev. Biol. 280:504-517(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Arabidopsis ARGONAUTE1 is an RNA Slicer that selectively recruits microRNAs and short interfering RNAs."
      Baumberger N., Baulcombe D.C.
      Proc. Natl. Acad. Sci. U.S.A. 102:11928-11933(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    8. "Cucumber mosaic virus-encoded 2b suppressor inhibits Arabidopsis Argonaute1 cleavage activity to counter plant defense."
      Zhang X., Yuan Y.R., Pei Y., Lin S.S., Tuschl T., Patel D.J., Chua N.H.
      Genes Dev. 20:3255-3268(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CUCUMBER MOSAIC VIRUS PROTEIN 2B.
    9. "The Polerovirus silencing suppressor P0 targets ARGONAUTE proteins for degradation."
      Baumberger N., Tsai C.-H., Lie M., Havecker E., Baulcombe D.C.
      Curr. Biol. 17:1609-1614(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TURNIP YELLOWS VIRUS PROTEIN P0.
    10. "Sorting of small RNAs into Arabidopsis argonaute complexes is directed by the 5' terminal nucleotide."
      Mi S., Cai T., Hu Y., Chen Y., Hodges E., Ni F., Wu L., Li S., Zhou H., Long C., Chen S., Hannon G.J., Qi Y.
      Cell 133:116-127(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Specificity of ARGONAUTE7-miR390 interaction and dual functionality in TAS3 trans-acting siRNA formation."
      Montgomery T.A., Howell M.D., Cuperus J.T., Li D., Hansen J.E., Alexander A.L., Chapman E.J., Fahlgren N., Allen E., Carrington J.C.
      Cell 133:128-141(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1001, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Root.
    13. "The mechanism selecting the guide strand from small RNA duplexes is different among argonaute proteins."
      Takeda A., Iwasaki S., Watanabe T., Utsumi M., Watanabe Y.
      Plant Cell Physiol. 49:493-500(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Arabidopsis DRB4, AGO1, AGO7, and RDR6 participate in a DCL4-initiated antiviral RNA silencing pathway negatively regulated by DCL1."
      Qu F., Ye X., Morris T.J.
      Proc. Natl. Acad. Sci. U.S.A. 105:14732-14737(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
      Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
      J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: cv. Columbia.
    16. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
      Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
      Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Unique functionality of 22-nt miRNAs in triggering RDR6-dependent siRNA biogenesis from target transcripts in Arabidopsis."
      Cuperus J.T., Carbonell A., Fahlgren N., Garcia-Ruiz H., Burke R.T., Takeda A., Sullivan C.M., Gilbert S.D., Montgomery T.A., Carrington J.C.
      Nat. Struct. Mol. Biol. 17:997-1003(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Redundant and specific roles of the ARGONAUTE proteins AGO1 and ZLL in development and small RNA-directed gene silencing."
      Mallory A.C., Hinze A., Tucker M.R., Bouche N., Gasciolli V., Elmayan T., Lauressergues D., Jauvion V., Vaucheret H., Laux T.
      PLoS Genet. 5:E1000646-E1000646(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "The Arabidopsis thaliana double-stranded RNA binding protein DRB1 directs guide strand selection from microRNA duplexes."
      Eamens A.L., Smith N.A., Curtin S.J., Wang M.B., Waterhouse P.M.
      RNA 15:2219-2235(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "Argonaute quenching and global changes in Dicer homeostasis caused by a pathogen-encoded GW repeat protein."
      Azevedo J., Garcia D., Pontier D., Ohnesorge S., Yu A., Garcia S., Braun L., Bergdoll M., Hakimi M.A., Lagrange T., Voinnet O.
      Genes Dev. 24:904-915(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TURNIP CRINKLE VIRUS CAPSID PROTEIN P38.
    21. "Ago hook and RNA helicase motifs underpin dual roles for SDE3 in antiviral defense and silencing of nonconserved intergenic regions."
      Garcia D., Garcia S., Pontier D., Marchais A., Renou J.P., Lagrange T., Voinnet O.
      Mol. Cell 48:109-120(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SDE3.
    22. "Arabidopsis Argonaute MID domains use their nucleotide specificity loop to sort small RNAs."
      Frank F., Hauver J., Sonenberg N., Nagar B.
      EMBO J. 31:3588-3595(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 593-738 IN COMPLEX WITH AMP; CMP; GMP AND UMP.
    23. "Structural insights into small RNA sorting and mRNA target binding by Arabidopsis Argonaute Mid domains."
      Zha X., Xia Q., Yuan Y.A.
      FEBS Lett. 586:3200-3207(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 592-739, RNA-BINDING.

    Entry informationi

    Entry nameiAGO1_ARATH
    AccessioniPrimary (citable) accession number: O04379
    Secondary accession number(s): Q0WSQ4, Q3ECU7, Q9LP83
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    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