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O04379

- AGO1_ARATH

UniProt

O04379 - AGO1_ARATH

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Protein
Protein argonaute 1
Gene
AGO1, At1g48410, F11A17.3, T1N15.2
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 cation By similarity
Metal bindingi846 – 8461Divalent metal cation By similarity
Metal bindingi986 – 9861Divalent metal cation By similarity

GO - Molecular functioni

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

GO - Biological processi

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

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 Reviewed prediction

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
Complete GO annotation...

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 1
PRO_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 SDE3.4 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi26487. 4 interactions.
IntActiO04379. 1 interaction.

Structurei

Secondary structure

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini391 – 501111PAZ
Add
BLAST
Domaini676 – 997322Piwi
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni886 – 8872Interaction with guide RNA Reviewed prediction
Regioni932 – 9409Interaction with guide RNA Reviewed prediction
Regioni969 – 99123Interaction with guide RNA Reviewed prediction
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 PAZ domain.
Contains 1 Piwi domain.

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.
VSP_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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 113 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

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