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Q9VUQ5

- AGO2_DROME

UniProt

Q9VUQ5 - AGO2_DROME

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Protein

Protein argonaute-2

Gene

AGO2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

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

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Biological processi

Host-virus interaction, RNA-mediated gene silencing

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, RNA-binding

Names & Taxonomyi

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

Organism-specific databases

FlyBaseiFBgn0087035. AGO2.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

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

Proteomic databases

PaxDbiQ9VUQ5.
PRIDEiQ9VUQ5.

Expressioni

Gene expression databases

BgeeiQ9VUQ5.
ExpressionAtlasiQ9VUQ5. differential.

Interactioni

Subunit structurei

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

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9VUQ5.

Family & Domainsi

Domains and Repeats

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

Region

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

Compositional bias

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

Domaini

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG279895.
GeneTreeiENSGT00760000119148.
InParanoidiQ9VUQ5.
KOiK11593.
OMAiQGQEGGY.
OrthoDBiEOG722J7S.
PhylomeDBiQ9VUQ5.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform B (identifier: Q9VUQ5-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGKKDKNKKG GQDSAAAPQP QQQQKQQQQR QQQPQQLQQP QQLQQPQQLQ
60 70 80 90 100
QPQQQQQQQP HQQQQQSSRQ QPSTSSGGSR ASGFQQGGQQ QKSQDAEGWT
110 120 130 140 150
AQKKQGKQQV QGWTKQGQQG GHQQGRQGQD GGYQQRPPGQ QQGGHQQGRQ
160 170 180 190 200
GQEGGYQQRP PGQQQGGHQQ GRQGQEGGYQ QRPSGQQQGG HQQGRQGQEG
210 220 230 240 250
GYQQRPPGQQ QGGHQQGRQG QEGGYQQRPS GQQQGGHQQG RQGQEGGYQQ
260 270 280 290 300
RPPGQQQGGH QQGRQGQEGG YQQRPPGQQQ GGHEQGRQGQ EGGYQQRPSG
310 320 330 340 350
QQQGGHQQGR QGQEGGYQQR PSGQQQGGHQ QGRQGQEGGY QQRPSGQQQG
360 370 380 390 400
GHQQGRQGQE GGYQQRPPGQ QPNQTQSQGQ YQSRGPPQQQ QAAPLPLPPQ
410 420 430 440 450
PAGSIKRGTI GKPGQVGINY LDLDLSKMPS VAYHYDVKIM PERPKKFYRQ
460 470 480 490 500
AFEQFRVDQL GGAVLAYDGK ASCYSVDKLP LNSQNPEVTV TDRNGRTLRY
510 520 530 540 550
TIEIKETGDS TIDLKSLTTY MNDRIFDKPM RAMQCVEVVL ASPCHNKAIR
560 570 580 590 600
VGRSFFKMSD PNNRHELDDG YEALVGLYQA FMLGDRPFLN VDISHKSFPI
610 620 630 640 650
SMPMIEYLER FSLKAKINNT TNLDYSRRFL EPFLRGINVV YTPPQSFQSA
660 670 680 690 700
PRVYRVNGLS RAPASSETFE HDGKKVTIAS YFHSRNYPLK FPQLHCLNVG
710 720 730 740 750
SSIKSILLPI ELCSIEEGQA LNRKDGATQV ANMIKYAATS TNVRKRKIMN
760 770 780 790 800
LLQYFQHNLD PTISRFGIRI ANDFIVVSTR VLSPPQVEYH SKRFTMVKNG
810 820 830 840 850
SWRMDGMKFL EPKPKAHKCA VLYCDPRSGR KMNYTQLNDF GNLIISQGKA
860 870 880 890 900
VNISLDSDVT YRPFTDDERS LDTIFADLKR SQHDLAIVII PQFRISYDTI
910 920 930 940 950
KQKAELQHGI LTQCIKQFTV ERKCNNQTIG NILLKINSKL NGINHKIKDD
960 970 980 990 1000
PRLPMMKNTM YIGADVTHPS PDQREIPSVV GVAASHDPYG ASYNMQYRLQ
1010 1020 1030 1040 1050
RGALEEIEDM FSITLEHLRV YKEYRNAYPD HIIYYRDGVS DGQFPKIKNE
1060 1070 1080 1090 1100
ELRCIKQACD KVGCKPKICC VIVVKRHHTR FFPSGDVTTS NKFNNVDPGT
1110 1120 1130 1140 1150
VVDRTIVHPN EMQFFMVSHQ AIQGTAKPTR YNVIENTGNL DIDLLQQLTY
1160 1170 1180 1190 1200
NLCHMFPRCN RSVSYPAPAY LAHLVAARGR VYLTGTNRFL DLKKEYAKRT
1210
IVPEFMKKNP MYFV
Length:1,214
Mass (Da):136,850
Last modified:August 16, 2004 - v3
Checksum:i0DC73AF09CC33F73
GO
Isoform C (identifier: Q9VUQ5-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

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

Sequence cautioni

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

Experimental Info

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

Natural variant

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

Alternative sequence

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

Sequence databases

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

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

Proteomic databases

PaxDbi Q9VUQ5.
PRIDEi Q9VUQ5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

CTDi 27161.
FlyBasei FBgn0087035. AGO2.

Phylogenomic databases

eggNOGi NOG279895.
GeneTreei ENSGT00760000119148.
InParanoidi Q9VUQ5.
KOi K11593.
OMAi QGQEGGY.
OrthoDBi EOG722J7S.
PhylomeDBi Q9VUQ5.

Miscellaneous databases

EvolutionaryTracei Q9VUQ5.
GenomeRNAii 39683.
NextBioi 814859.

Gene expression databases

Bgeei Q9VUQ5.
ExpressionAtlasi Q9VUQ5. differential.

Family and domain databases

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

Publicationsi

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

Entry informationi

Entry nameiAGO2_DROME
AccessioniPrimary (citable) accession number: Q9VUQ5
Secondary accession number(s): C7LAD2
, Q2Q3Y0, Q2Q3Y1, Q2Q3Y3, Q2Q3Y4, Q2Q3Y5, Q86P07, Q8T3N2, Q9VUQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: November 26, 2014
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3