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O04379

- AGO1_ARATH

UniProt

O04379 - AGO1_ARATH

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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

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

Mg2+By similarity, Mn2+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. RNA binding Source: UniProtKB-KW
  5. 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
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.
REACT_255398. MicroRNA (miRNA) biogenesis.
REACT_269630. Transcriptional regulation 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
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 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

ExpressionAtlasiO04379. baseline and differential.
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 – 5983Combined sources
Beta strandi604 – 6096Combined sources
Helixi616 – 63217Combined sources
Helixi650 – 6523Combined sources
Helixi653 – 66614Combined sources
Beta strandi676 – 6816Combined sources
Helixi688 – 69811Combined sources
Beta strandi704 – 7085Combined sources
Helixi709 – 7146Combined sources
Helixi717 – 73014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MVRKRRTDAP SEGGEGSGSR EAGPVSGGGR GSQRGGFQQG GGQHQGGRGY
60 70 80 90 100
TPQPQQGGRG GRGYGQPPQQ QQQYGGPQEY QGRGRGGPPH QGGRGGYGGG
110 120 130 140 150
RGGGPSSGPP QRQSVPELHQ ATSPTYQAVS SQPTLSEVSP TQVPEPTVLA
160 170 180 190 200
QQFEQLSVEQ GAPSQAIQPI PSSSKAFKFP MRPGKGQSGK RCIVKANHFF
210 220 230 240 250
AELPDKDLHH YDVTITPEVT SRGVNRAVMK QLVDNYRDSH LGSRLPAYDG
260 270 280 290 300
RKSLYTAGPL PFNSKEFRIN LLDEEVGAGG QRREREFKVV IKLVARADLH
310 320 330 340 350
HLGMFLEGKQ SDAPQEALQV LDIVLRELPT SRYIPVGRSF YSPDIGKKQS
360 370 380 390 400
LGDGLESWRG FYQSIRPTQM GLSLNIDMSS TAFIEANPVI QFVCDLLNRD
410 420 430 440 450
ISSRPLSDAD RVKIKKALRG VKVEVTHRGN MRRKYRISGL TAVATRELTF
460 470 480 490 500
PVDERNTQKS VVEYFHETYG FRIQHTQLPC LQVGNSNRPN YLPMEVCKIV
510 520 530 540 550
EGQRYSKRLN ERQITALLKV TCQRPIDREK DILQTVQLND YAKDNYAQEF
560 570 580 590 600
GIKISTSLAS VEARILPPPW LKYHESGREG TCLPQVGQWN MMNKKMINGG
610 620 630 640 650
TVNNWICINF SRQVQDNLAR TFCQELAQMC YVSGMAFNPE PVLPPVSARP
660 670 680 690 700
EQVEKVLKTR YHDATSKLSQ GKEIDLLIVI LPDNNGSLYG DLKRICETEL
710 720 730 740 750
GIVSQCCLTK HVFKMSKQYM ANVALKINVK VGGRNTVLVD ALSRRIPLVS
760 770 780 790 800
DRPTIIFGAD VTHPHPGEDS SPSIAAVVAS QDWPEITKYA GLVCAQAHRQ
810 820 830 840 850
ELIQDLFKEW KDPQKGVVTG GMIKELLIAF RRSTGHKPLR IIFYRDGVSE
860 870 880 890 900
GQFYQVLLYE LDAIRKACAS LEAGYQPPVT FVVVQKRHHT RLFAQNHNDR
910 920 930 940 950
HSVDRSGNIL PGTVVDSKIC HPTEFDFYLC SHAGIQGTSR PAHYHVLWDE
960 970 980 990 1000
NNFTADGLQS LTNNLCYTYA RCTRSVSIVP PAYYAHLAAF RARFYMEPET
1010 1020 1030 1040
SDSGSMASGS MARGGGMAGR STRGPNVNAA VRPLPALKEN VKRVMFYC
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. Curated

Alternative sequence

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
REACT_255398. MicroRNA (miRNA) biogenesis.
REACT_269630. Transcriptional regulation by small RNAs.

Gene expression databases

ExpressionAtlasi O04379. baseline and differential.
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: November 26, 2014
This is version 116 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