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Protein

Protein Gawky

Gene

gw

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

Functioni

Required for gene silencing mediated by micro-RNAs (miRNAs). Silences both polyadenylated and deadenylated mRNAs. Required for miRNA-mediated translational repression and mRNA decay. Not required for miRNA target recognition. Necessary to initiate but not to maintain silencing. Promotes mRNA deadenylation through the recruitment of the CCR4-NOT and PAN complexes and promotes decapping by the DCP1-DCP2 complex. Dissociates from silenced mRNAs after deadenylation. Required for completion of nuclear divisions during early embryonic development.6 Publications

GO - Molecular functioni

GO - Biological processi

  • embryonic development via the syncytial blastoderm Source: FlyBase
  • gene silencing by miRNA Source: UniProtKB
  • locomotor rhythm Source: FlyBase
  • mRNA catabolic process Source: FlyBase
  • regulation of protein localization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

RNA-mediated gene silencing, Translation regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-DME-426496. Post-transcriptional silencing by small RNAs.
R-DME-5578749. Transcriptional regulation by small RNAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein GawkyImported
Gene namesi
Name:gw
Synonyms:GW1821 Publication
ORF Names:CG31992
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 4

Organism-specific databases

FlyBaseiFBgn0051992. gw.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic mRNA processing body Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13841384Protein GawkyPRO_0000415948Add
BLAST

Proteomic databases

PaxDbiQ8SY33.
PRIDEiQ8SY33.

Expressioni

Developmental stagei

Highest levels are found during early embryonic development until approximately 18 hours and during pupariation.1 Publication

Gene expression databases

BgeeiQ8SY33.
GenevisibleiQ8SY33. DM.

Interactioni

Subunit structurei

Interacts (via N-terminal region) with AGO1 (via Piwi domain); the interaction is essential for localization of AGO1 in P-bodies and for miRNA-mediated silencing. Interacts with pAbp/PABPC1; this interaction interferes with the binding of pAbp to eIF4G and is required for miRNA-mediated silencing. Interacts with CCR4-NOT complex members Not1, Rga/NOT2, twin/CCR4, Pop2 and NOT3/5 and with PAN complex members CG8232/PAN2 and CG11486/PAN3.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AGO1Q32KD43EBI-160693,EBI-105513
CG11486-RCD3DMN92EBI-160693,EBI-6512959
Not1A8DY812EBI-160693,EBI-3428401
pAbpP2118711EBI-160693,EBI-103658
PAN2A1Z7K92EBI-160693,EBI-193297

Protein-protein interaction databases

BioGridi68639. 12 interactions.
DIPiDIP-35525N.
IntActiQ8SY33. 12 interactions.
MINTiMINT-764572.
STRINGi7227.FBpp0088165.

Structurei

Secondary structure

1
1384
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1118 – 11225Combined sources
Helixi1131 – 114010Combined sources
Beta strandi1143 – 11497Combined sources
Turni1150 – 11534Combined sources
Beta strandi1154 – 11618Combined sources
Helixi1162 – 117211Combined sources
Beta strandi1175 – 11773Combined sources
Beta strandi1180 – 11856Combined sources
Helixi1189 – 11968Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WBRNMR-A1114-1198[»]
ProteinModelPortaliQ8SY33.
SMRiQ8SY33. Positions 1110-1198.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8SY33.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini547 – 58842UBAPROSITE-ProRule annotationAdd
BLAST
Domaini1117 – 118973RRMSequence analysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 605605Sufficient for miRNA-mediated silencing1 PublicationAdd
BLAST
Regioni1 – 205205Required for interaction with AGO11 PublicationAdd
BLAST
Regioni205 – 490286Minimal N-terminal region required for miRNA-mediated silencing1 PublicationAdd
BLAST
Regioni605 – 830226Sufficient for miRNA-mediated silencing1 PublicationAdd
BLAST
Regioni862 – 1115254Not required for interaction with AGO1 or miRNAs or for localization to P-bodies but necessary for miRNA-mediated silencing and for interaction with pAbp3 PublicationsAdd
BLAST
Regioni940 – 1215276Sufficient for miRNA-mediated silencing1 PublicationAdd
BLAST
Regioni1200 – 1384185Not required for interaction with AGO1 or miRNAs or for localization to P-bodies but necessary for miRNA-mediated silencing, dissociation from AGO1 and miRNAs and interaction with pAbp3 PublicationsAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi81 – 281201Gly-richSequence analysisAdd
BLAST
Compositional biasi527 – 5304Poly-GlnSequence analysis
Compositional biasi713 – 824112Gln-richSequence analysisAdd
BLAST
Compositional biasi1204 – 1366163Ser-richSequence analysisAdd
BLAST

Domaini

The UBA domain is not required for correct subcellular location, gene silencing or interaction with pAbp.1 Publication
The RRM domain lacks RNA-binding properties and does not bind RNA in vitro. It is not required for P-body localization or for interaction with AGO1 or miRNAs but is required for silencing. May play a role in protein-protein interactions.1 Publication1 Publication

Sequence similaritiesi

Belongs to the GW182 family.Sequence analysis
Contains 1 RRM (RNA recognition motif) domain.Sequence analysis
Contains 1 UBA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IFAU. Eukaryota.
ENOG41110AX. LUCA.
GeneTreeiENSGT00410000025966.
InParanoidiQ8SY33.
KOiK18412.
OMAiWSSSYTT.
OrthoDBiEOG7BP81M.
PhylomeDBiQ8SY33.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR019486. Argonaute_hook_dom.
IPR026805. GW182_M_dom.
IPR012677. Nucleotide-bd_a/b_plait.
IPR015940. UBA.
IPR009060. UBA-like.
[Graphical view]
PfamiPF10427. Ago_hook. 1 hit.
PF12938. M_domain. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS50030. UBA. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: Q8SY33-1) [UniParc]FASTAAdd to basket

Also known as: B, E, F

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
MREALFSQDG WGCQHVNQDT NWEVPSSPEP ANKDAPGPPM WKPSINNGTD
60 70 80 90 100
LWESNLRNGG QPAAQQVPKP SWGHTPSSNL GGTWGEDDDG ADSSSVWTGG
110 120 130 140 150
AVSNAGSGAA VGVNQAGVNV GPGGVVSSGG PQWGQGVVGV GLGSTGGNGS
160 170 180 190 200
SNITGSSGVA TGSSGNSSNA GNGWGDPREI RPLGVGGSMD IRNVEHRGGN
210 220 230 240 250
GSGATSSDPR DIRMIDPRDP IRGDPRGISG RLNGTSEMWG HHPQMSHNQL
260 270 280 290 300
QGINKMVGQS VATASTSVGT SGSGIGPGGP GPSTVSGNIP TQWGPAQPVS
310 320 330 340 350
VGVSGPKDMS KQISGWEEPS PPPQRRSIPN YDDGTSLWGQ QTRVPAASGH
360 370 380 390 400
WKDMTDSIGR SSHLMRGQSQ TGGIGIAGVG NSNVPVGANP SNPISSVVGP
410 420 430 440 450
QARIPSVGGV QHKPDGGAMW VHSGNVGGRN NVAAVTTWGD DTHSVNVGAP
460 470 480 490 500
SSGSVSSNNW VDDKSNSTLA QNSWSDPAPV GVSWGNKQSK PPSNSASSGW
510 520 530 540 550
STAAGVVDGV DLGSEWNTHG GIIGKSQQQQ KLAGLNVGMV NVINAEIIKQ
560 570 580 590 600
SKQYRILVEN GFKKEDVERA LVIANMNIEE AADMLRANSS LSMDGWRRHD
610 620 630 640 650
ESLGSYADHN SSTSSGGFAG RYPVNSGQPS MSFPHNNLMN NMGGTAVTGG
660 670 680 690 700
NNNTNMTALQ VQKYLNQGQH GVAVGPQAVG NSSAVSVGFG QNTSNAAVAG
710 720 730 740 750
AASVNIAANT NNQPSGQQIR MLGQQIQLAI HSGFISSQIL TQPLTQTTLN
760 770 780 790 800
LLNQLLSNIK HLQAAQQSLT RGGNVNPMAV NVAISKYKQQ IQNLQNQINA
810 820 830 840 850
QQAVYVKQQN MQPTSQQQQP QQQQLPSVHL SNSGNDYLRG HDAINNLQSN
860 870 880 890 900
FSELNINKPS GYQGASNQQS RLNQWKLPVL DKEINSDSTE FSRAPGATKQ
910 920 930 940 950
NLTANTSNIN SLGLQNDSTW STGRSIGDGW PDPSSDNENK DWSVAQPTSA
960 970 980 990 1000
ATAYTDLVQE FEPGKPWKGS QIKSIEDDPS ITPGSVARSP LSINSTPKDA
1010 1020 1030 1040 1050
DIFANTGKNS PTDLPPLSLS SSTWSFNPNQ NYPSHSWSDN SQQCTATSEL
1060 1070 1080 1090 1100
WTSPLNKSSS RGPPPGLTAN SNKSANSNAS TPTTITGGAN GWLQPRSGGV
1110 1120 1130 1140 1150
QTTNTNWTGG NTTWGSSWLL LKNLTAQIDG PTLRTLCMQH GPLVSFHPYL
1160 1170 1180 1190 1200
NQGIALCKYT TREEANKAQM ALNNCVLANT TIFAESPSEN EVQSIMQHLP
1210 1220 1230 1240 1250
QTPSSTSSSG TSGGNVGGVG TSANNANSGS AACLSGNNSG NGNGSASGAG
1260 1270 1280 1290 1300
SGNNGNSSCN NSAAGGGSSS NNTITTVANS NLVGSSGSVS NSSGVTANSS
1310 1320 1330 1340 1350
TVSVVSCTAS GNSINGAGTA NSSGSKSSAN NLASGQSSAS NLTNSTNSTW
1360 1370 1380
RQTSQNQALQ SQSRPSGREA DFDYISLVYS IVDD
Length:1,384
Mass (Da):142,973
Last modified:June 1, 2002 - v1
Checksum:i4E87DFE49050883E
GO
Isoform I (identifier: Q8SY33-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     969-971: Missing.

Note: No experimental confirmation available.
Show »
Length:1,381
Mass (Da):142,701
Checksum:i9823EFFFE67253C4
GO
Isoform J (identifier: Q8SY33-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1035-1036: Missing.

Note: No experimental confirmation available.
Show »
Length:1,382
Mass (Da):142,749
Checksum:iBCBC248F4836B070
GO

Sequence cautioni

The sequence AAM50720.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei969 – 9713Missing in isoform I. CuratedVSP_047895
Alternative sequencei1035 – 10362Missing in isoform J. CuratedVSP_047896

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014135 Genomic DNA. Translation: AAF59322.2.
AE014135 Genomic DNA. Translation: AAF59323.2.
AE014135 Genomic DNA. Translation: AAN06507.2.
AE014135 Genomic DNA. Translation: AAN06508.1.
AE014135 Genomic DNA. Translation: AAN06509.1.
AE014135 Genomic DNA. Translation: AAX52511.2.
AY075429 mRNA. Translation: AAL68245.1.
AY118860 mRNA. Translation: AAM50720.1. Different initiation.
RefSeqiNP_001014691.2. NM_001014691.2. [Q8SY33-3]
NP_726596.1. NM_166780.2. [Q8SY33-1]
NP_726597.1. NM_166781.2. [Q8SY33-1]
NP_726599.2. NM_166783.2. [Q8SY33-2]
NP_726600.1. NM_166784.2. [Q8SY33-1]
NP_726601.1. NM_166785.2. [Q8SY33-1]
UniGeneiDm.1403.

Genome annotation databases

EnsemblMetazoaiFBtr0089096; FBpp0088165; FBgn0051992. [Q8SY33-1]
FBtr0089097; FBpp0088166; FBgn0051992. [Q8SY33-1]
FBtr0089100; FBpp0088169; FBgn0051992. [Q8SY33-1]
FBtr0089101; FBpp0088170; FBgn0051992. [Q8SY33-1]
GeneIDi43808.
KEGGidme:Dmel_CG31992.
UCSCiCG31992-RA. d. melanogaster. [Q8SY33-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014135 Genomic DNA. Translation: AAF59322.2.
AE014135 Genomic DNA. Translation: AAF59323.2.
AE014135 Genomic DNA. Translation: AAN06507.2.
AE014135 Genomic DNA. Translation: AAN06508.1.
AE014135 Genomic DNA. Translation: AAN06509.1.
AE014135 Genomic DNA. Translation: AAX52511.2.
AY075429 mRNA. Translation: AAL68245.1.
AY118860 mRNA. Translation: AAM50720.1. Different initiation.
RefSeqiNP_001014691.2. NM_001014691.2. [Q8SY33-3]
NP_726596.1. NM_166780.2. [Q8SY33-1]
NP_726597.1. NM_166781.2. [Q8SY33-1]
NP_726599.2. NM_166783.2. [Q8SY33-2]
NP_726600.1. NM_166784.2. [Q8SY33-1]
NP_726601.1. NM_166785.2. [Q8SY33-1]
UniGeneiDm.1403.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WBRNMR-A1114-1198[»]
ProteinModelPortaliQ8SY33.
SMRiQ8SY33. Positions 1110-1198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68639. 12 interactions.
DIPiDIP-35525N.
IntActiQ8SY33. 12 interactions.
MINTiMINT-764572.
STRINGi7227.FBpp0088165.

Proteomic databases

PaxDbiQ8SY33.
PRIDEiQ8SY33.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089096; FBpp0088165; FBgn0051992. [Q8SY33-1]
FBtr0089097; FBpp0088166; FBgn0051992. [Q8SY33-1]
FBtr0089100; FBpp0088169; FBgn0051992. [Q8SY33-1]
FBtr0089101; FBpp0088170; FBgn0051992. [Q8SY33-1]
GeneIDi43808.
KEGGidme:Dmel_CG31992.
UCSCiCG31992-RA. d. melanogaster. [Q8SY33-1]

Organism-specific databases

CTDi43808.
FlyBaseiFBgn0051992. gw.

Phylogenomic databases

eggNOGiENOG410IFAU. Eukaryota.
ENOG41110AX. LUCA.
GeneTreeiENSGT00410000025966.
InParanoidiQ8SY33.
KOiK18412.
OMAiWSSSYTT.
OrthoDBiEOG7BP81M.
PhylomeDBiQ8SY33.

Enzyme and pathway databases

ReactomeiR-DME-426496. Post-transcriptional silencing by small RNAs.
R-DME-5578749. Transcriptional regulation by small RNAs.

Miscellaneous databases

ChiTaRSigw. fly.
EvolutionaryTraceiQ8SY33.
GenomeRNAii43808.
NextBioi835971.
PROiQ8SY33.

Gene expression databases

BgeeiQ8SY33.
GenevisibleiQ8SY33. DM.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR019486. Argonaute_hook_dom.
IPR026805. GW182_M_dom.
IPR012677. Nucleotide-bd_a/b_plait.
IPR015940. UBA.
IPR009060. UBA-like.
[Graphical view]
PfamiPF10427. Ago_hook. 1 hit.
PF12938. M_domain. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS50030. UBA. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: Berkeley.
  2. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley1 Publication.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: BerkeleyImported.
    Tissue: Embryo1 Publication and Ovary1 Publication.
  4. "A crucial role for GW182 and the DCP1:DCP2 decapping complex in miRNA-mediated gene silencing."
    Rehwinkel J., Behm-Ansmant I., Gatfield D., Izaurralde E.
    RNA 11:1640-1647(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "mRNA degradation by miRNAs and GW182 requires both CCR4:NOT deadenylase and DCP1:DCP2 decapping complexes."
    Behm-Ansmant I., Rehwinkel J., Doerks T., Stark A., Bork P., Izaurralde E.
    Genes Dev. 20:1885-1898(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AGO1, SUBCELLULAR LOCATION.
  6. "Gawky is a component of cytoplasmic mRNA processing bodies required for early Drosophila development."
    Schneider M.D., Najand N., Chaker S., Pare J.M., Haskins J., Hughes S.C., Hobman T.C., Locke J., Simmonds A.J.
    J. Cell Biol. 174:349-358(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  7. "GW182 interaction with Argonaute is essential for miRNA-mediated translational repression and mRNA decay."
    Eulalio A., Huntzinger E., Izaurralde E.
    Nat. Struct. Mol. Biol. 15:346-353(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AGO1.
  8. "The silencing domain of GW182 interacts with PABPC1 to promote translational repression and degradation of microRNA targets and is required for target release."
    Zekri L., Huntzinger E., Heimstadt S., Izaurralde E.
    Mol. Cell. Biol. 29:6220-6231(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PABP.
  9. "Multiple independent domains of dGW182 function in miRNA-mediated repression in Drosophila."
    Chekulaeva M., Filipowicz W., Parker R.
    RNA 15:794-803(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGIONS SUFFICIENT FOR MIRNA-MEDIATED SILENCING.
  10. "A C-terminal silencing domain in GW182 is essential for miRNA function."
    Eulalio A., Helms S., Fritzsch C., Fauser M., Izaurralde E.
    RNA 15:1067-1077(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGIONS REQUIRED FOR INTERACTION WITH AGO1 AND MIRNA-MEDIATED SILENCING, ROLE OF UBA DOMAIN.
  11. "The GW/WG repeats of Drosophila GW182 function as effector motifs for miRNA-mediated repression."
    Chekulaeva M., Parker R., Filipowicz W.
    Nucleic Acids Res. 38:6673-6683(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGIONS REQUIRED FOR INTERACTION WITH AGO1 AND MIRNA-MEDIATED SILENCING.
  12. "GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets."
    Braun J.E., Huntzinger E., Fauser M., Izaurralde E.
    Mol. Cell 44:120-133(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CCR4-NOT AND PAN COMPLEXES.
  13. "The RRM domain in GW182 proteins contributes to miRNA-mediated gene silencing."
    Eulalio A., Tritschler F., Buttner R., Weichenrieder O., Izaurralde E., Truffault V.
    Nucleic Acids Res. 37:2974-2983(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1114-1198, ROLE OF RRM DOMAIN.

Entry informationi

Entry nameiGAWKY_DROME
AccessioniPrimary (citable) accession number: Q8SY33
Secondary accession number(s): Q8MSF0, Q9V4F1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: June 1, 2002
Last modified: May 11, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.