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O04379 (AGO1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein argonaute 1
Gene names
Name:AGO1
Ordered Locus Names:At1g48410
ORF Names:F11A17.3, T1N15.2
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1048 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.17 Ref.18 Ref.19

Cofactor

Magnesium or manganese By similarity.

Subunit structure

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. Ref.8 Ref.9 Ref.20 Ref.21

Subcellular location

Cytoplasm Potential.

Tissue specificity

Widely expressed at low levels.

Developmental stage

Expressed throughout all developmental stages.

Disruption phenotype

Narrow rosette leaves. Single shoot bearing a terminal inflorescence. Abnormal inflorescence with infertile flowers and filamentous organs. Ref.1 Ref.7

Sequence similarities

Belongs to the argonaute family. Ago subfamily.

Contains 1 PAZ domain.

Contains 1 Piwi domain.

Sequence caution

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

Ontologies

Keywords
   Biological processHost-virus interaction
Plant defense
RNA-mediated gene silencing
Transcription
Transcription regulation
Translation regulation
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandMagnesium
Manganese
Metal-binding
RNA-binding
   Molecular functionDevelopmental protein
Repressor
Ribonucleoprotein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA interference

Inferred from mutant phenotype PubMed 17558406. Source: TAIR

RNA phosphodiester bond hydrolysis, endonucleolytic

Inferred from direct assay Ref.7. Source: GOC

adaxial/abaxial pattern specification

Inferred from mutant phenotype PubMed 22623415. Source: TAIR

adventitious root development

Inferred from mutant phenotype PubMed 15829601. Source: TAIR

auxin metabolic process

Inferred from genetic interaction PubMed 15829601. Source: TAIR

defense response

Inferred from electronic annotation. Source: UniProtKB-KW

embryo development ending in seed dormancy

Inferred from genetic interaction PubMed 9876176. Source: TAIR

gene silencing by RNA

Inferred from electronic annotation. Source: UniProtKB-KW

gene silencing by miRNA

Inferred from mutant phenotype PubMed 15131082. Source: TAIR

innate immune response

Inferred from mutant phenotype PubMed 20164210. Source: TAIR

leaf morphogenesis

Inferred from mutant phenotype Ref.1. Source: TAIR

leaf proximal/distal pattern formation

Inferred from mutant phenotype PubMed 22623415. Source: TAIR

leaf vascular tissue pattern formation

Inferred from mutant phenotype PubMed 22623415. Source: TAIR

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

posttranscriptional gene silencing

Inferred from expression pattern PubMed 11910010. Source: TAIR

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

response to auxin

Inferred from genetic interaction PubMed 15829601. Source: TAIR

response to far red light

Inferred from genetic interaction PubMed 15829601. Source: TAIR

stem cell development

Inferred from genetic interaction PubMed 18653559. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

virus induced gene silencing

Inferred from direct assay Ref.8. Source: TAIR

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 17442570PubMed 22247253. Source: TAIR

cytosol

Inferred from direct assay Ref.12. Source: TAIR

extrinsic component of membrane

Inferred from direct assay PubMed 22247288. Source: TAIR

nucleus

Inferred from direct assay PubMed 17442570PubMed 22247253. Source: TAIR

ribonucleoprotein complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

endoribonuclease activity

Inferred from direct assay Ref.7. Source: TAIR

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

miRNA binding

Inferred from physical interaction Ref.7. Source: TAIR

protein binding

Inferred from physical interaction PubMed 17869109. Source: TAIR

siRNA binding

Inferred from physical interaction Ref.7. Source: TAIR

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AMP1Q9M1S82EBI-6912745,EBI-6912802

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O04379-1)

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.
Isoform 2 (identifier: O04379-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10481048Protein argonaute 1
PRO_0000194068

Regions

Domain391 – 501111PAZ
Domain676 – 997322Piwi
Region886 – 8872Interaction with guide RNA Potential
Region932 – 9409Interaction with guide RNA Potential
Region969 – 99123Interaction with guide RNA Potential
Compositional bias13 – 10492Gly-rich

Sites

Metal binding7601Divalent metal cation By similarity
Metal binding8461Divalent metal cation By similarity
Metal binding9861Divalent metal cation By similarity

Amino acid modifications

Modified residue10011Phosphoserine Ref.12

Natural variations

Alternative sequence3321R → RIR in isoform 2.
VSP_040612

Secondary structure

................... 1048
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 3E5146343A09C541

FASTA1,048116,191
        10         20         30         40         50         60 
MVRKRRTDAP SEGGEGSGSR EAGPVSGGGR GSQRGGFQQG GGQHQGGRGY TPQPQQGGRG 

        70         80         90        100        110        120 
GRGYGQPPQQ QQQYGGPQEY QGRGRGGPPH QGGRGGYGGG RGGGPSSGPP QRQSVPELHQ 

       130        140        150        160        170        180 
ATSPTYQAVS SQPTLSEVSP TQVPEPTVLA QQFEQLSVEQ GAPSQAIQPI PSSSKAFKFP 

       190        200        210        220        230        240 
MRPGKGQSGK RCIVKANHFF AELPDKDLHH YDVTITPEVT SRGVNRAVMK QLVDNYRDSH 

       250        260        270        280        290        300 
LGSRLPAYDG RKSLYTAGPL PFNSKEFRIN LLDEEVGAGG QRREREFKVV IKLVARADLH 

       310        320        330        340        350        360 
HLGMFLEGKQ SDAPQEALQV LDIVLRELPT SRYIPVGRSF YSPDIGKKQS LGDGLESWRG 

       370        380        390        400        410        420 
FYQSIRPTQM GLSLNIDMSS TAFIEANPVI QFVCDLLNRD ISSRPLSDAD RVKIKKALRG 

       430        440        450        460        470        480 
VKVEVTHRGN MRRKYRISGL TAVATRELTF PVDERNTQKS VVEYFHETYG FRIQHTQLPC 

       490        500        510        520        530        540 
LQVGNSNRPN YLPMEVCKIV EGQRYSKRLN ERQITALLKV TCQRPIDREK DILQTVQLND 

       550        560        570        580        590        600 
YAKDNYAQEF GIKISTSLAS VEARILPPPW LKYHESGREG TCLPQVGQWN MMNKKMINGG 

       610        620        630        640        650        660 
TVNNWICINF SRQVQDNLAR TFCQELAQMC YVSGMAFNPE PVLPPVSARP EQVEKVLKTR 

       670        680        690        700        710        720 
YHDATSKLSQ GKEIDLLIVI LPDNNGSLYG DLKRICETEL GIVSQCCLTK HVFKMSKQYM 

       730        740        750        760        770        780 
ANVALKINVK VGGRNTVLVD ALSRRIPLVS DRPTIIFGAD VTHPHPGEDS SPSIAAVVAS 

       790        800        810        820        830        840 
QDWPEITKYA GLVCAQAHRQ ELIQDLFKEW KDPQKGVVTG GMIKELLIAF RRSTGHKPLR 

       850        860        870        880        890        900 
IIFYRDGVSE GQFYQVLLYE LDAIRKACAS LEAGYQPPVT FVVVQKRHHT RLFAQNHNDR 

       910        920        930        940        950        960 
HSVDRSGNIL PGTVVDSKIC HPTEFDFYLC SHAGIQGTSR PAHYHVLWDE NNFTADGLQS 

       970        980        990       1000       1010       1020 
LTNNLCYTYA RCTRSVSIVP PAYYAHLAAF RARFYMEPET SDSGSMASGS MARGGGMAGR 

      1030       1040 
STRGPNVNAA VRPLPALKEN VKRVMFYC 

« Hide

Isoform 2 [UniParc].

Checksum: 233B89E5E4D9E1EC
Show »

FASTA1,050116,460

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis."
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.
J. Proteome Res. 7:2458-2470(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001185169.1. NM_001198240.1. [O04379-2]
NP_175274.1. NM_103737.3. [O04379-1]
NP_849784.1. NM_179453.2. [O04379-2]
UniGeneAt.21124.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalO04379.
SMRO04379. Positions 175-996.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid26487. 4 interactions.
IntActO04379. 1 interaction.

Proteomic databases

PaxDbO04379.
PRIDEO04379.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G48410.1; AT1G48410.1; AT1G48410. [O04379-1]
GeneID841262.
KEGGath:AT1G48410.

Organism-specific databases

TAIRAT1G48410.

Phylogenomic databases

eggNOGNOG279895.
HOGENOMHOG000116043.
InParanoidO04379.
KOK11593.
OMAGRSMPEP.
PhylomeDBO04379.

Gene expression databases

ArrayExpressO04379.
GenevestigatorO04379.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
InterProIPR024357. Argonaut_Gly-rich.
IPR014811. DUF1785.
IPR003100. PAZ_dom.
IPR003165. Piwi.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamPF08699. DUF1785. 1 hit.
PF12764. Gly-rich_Ago1. 1 hit.
PF02170. PAZ. 1 hit.
PF02171. Piwi. 1 hit.
[Graphical view]
SMARTSM00949. PAZ. 1 hit.
SM00950. Piwi. 1 hit.
[Graphical view]
SUPFAMSSF101690. SSF101690. 2 hits.
SSF53098. SSF53098. 1 hit.
PROSITEPS50821. PAZ. 1 hit.
PS50822. PIWI. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAGO1_ARATH
AccessionPrimary (citable) accession number: O04379
Secondary accession number(s): Q0WSQ4, Q3ECU7, Q9LP83
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 1, 1997
Last modified: June 11, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names