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Protein

Protein aubergine

Gene

aub

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

Functioni

Acts via the piwi-interacting RNA (piRNA) metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. In ovary, associates predominantly with antisense piRNAs that contain uridine at their 5' end. In testis, associates with Su(Ste) antisense piRNAs (most abundant class of piRNAs found in complex with aub in testes) and negatively regulates Ste expression, most likely by cleaving its transcripts. Also in testis, may repress translation of vas when associated with a piRNA derived from chromosome X, termed AT-chX-1, whose sequence shows strong complementarity to vas mRNA. Aub-piRNA complexes from ovary and testis possess RNA cleavage activity. Involved in telomere regulation by repressing specialized telomeric retroelements HeT-A and TART; Drosophila telomeres being maintained by transposition of specialized telomeric retroelements. Also involved in telomeric trans-silencing, a repression mechanism by which a transposon or a transgene inserted in subtelomeric heterochromatin has the capacity to repress in trans, in the female germline, a homologous transposon, or transgene located in euchromatin. Involved in the suppression of meiotic drive of sex chromosomes and autosomes. Involved in transposon silencing in the adult brain. Required for dorsal-ventral as well as anterior-posterior patterning of the egg. Required during oogenesis for primordial germ cell formation and activation of RNA interference. During early oogenesis, required for osk mRNA silencing and polarization of the microtubule cytoskeleton. During mid-oogenesis, required for osk mRNA localization to the posterior pole and efficient translation of osk and grk. During embryogenesis, required for posterior localization of nos mRNA, independently of osk, and pole cell formation. Essential for the formation and/or structural integrity of perinuclear nuage particles. Required for the localization of Mael to the meiotic nuage. Forms a complex with smg, twin, AGO3 and specific piRNAs that targets nos mRNA (and probably other maternal mRNAS) for deadenylation promoting its decay during early embryogenesis.21 Publications

GO - Molecular functioni

  • piRNA binding Source: FlyBase
  • RNA binding Source: FlyBase

GO - Biological processi

  • chromatin silencing Source: FlyBase
  • defense response to Gram-negative bacterium Source: FlyBase
  • dorsal appendage formation Source: FlyBase
  • karyosome formation Source: FlyBase
  • maintenance of pole plasm mRNA location Source: FlyBase
  • mitotic chromosome condensation Source: FlyBase
  • mRNA splicing, via spliceosome Source: FlyBase
  • negative regulation of transposition Source: FlyBase
  • oocyte maturation Source: FlyBase
  • oogenesis Source: FlyBase
  • pole cell formation Source: FlyBase
  • pole plasm protein localization Source: FlyBase
  • positive regulation of innate immune response Source: FlyBase
  • positive regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: FlyBase
  • positive regulation of oskar mRNA translation Source: FlyBase
  • regulation of oskar mRNA translation Source: FlyBase
  • regulation of pole plasm oskar mRNA localization Source: FlyBase
  • regulation of translational initiation Source: FlyBase
  • RNA interference Source: FlyBase
  • segmentation Source: FlyBase
  • targeting of mRNA for destruction involved in RNA interference Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Oogenesis, RNA-mediated gene silencing, Translation regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein aubergineImported
Alternative name(s):
Protein stingImported
Gene namesi
Name:aub
ORF Names:CG6137
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0000146. aub.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: FlyBase
  • cytoplasm Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • P granule Source: FlyBase
  • precatalytic spliceosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Female sterility, consequence of a maternal lethal effect. Approximately 2% of the embryos from aub mutant females are fertilized and secrete a recognizable cuticle, while all of them lack abdominal segments. Male sterility accompanied by production of Ste protein crystals in primary spermatocytes and by meiotic non-disjunction and drive of sex chromosomes and autosomes.4 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 177RGRGRGR → KGKGKGK: Abolishes methylation and interaction with tud. Does not affect piRNA binding. 2 Publications
Mutagenesisi721 – 7211E → A: Putative catalytic mutant. Enhances meiotic drive. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 866866Protein auberginePRO_0000422915Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei11 – 111Symmetric dimethylarginine2 Publications
Modified residuei13 – 131Symmetric dimethylarginine2 Publications
Modified residuei15 – 151Symmetric dimethylarginine2 Publications

Post-translational modificationi

Symmetrical dimethylation on Arg-11, Arg-13 and/or Arg-15, most likely by csul, is required for binding to tud, localization to the pole plasm and association with the correct piRNAs.1 Publication4 Publications

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

PaxDbiO76922.
PRIDEiO76922.

Expressioni

Tissue specificityi

Expressed in ovary. In the germarium, found in germline stem and cyst cells. In egg chambers from stage 6, expressed both in nurse cells and oocytes. In embryos, accumulates in the pole cells, although low expression is detected throughout the entire embryo. In testis, expressed in germline stem cells, gonialblast and spermatogonia cells (at protein level). In the adult brain, expressed in the ellipsoid body, the mushroom body subdivision in the peduncle and the cell body layer. Expressed specifically in alpha'/beta' and gamma neurons.10 Publications

Developmental stagei

Expressed maternally in oocytes and 0-6 hours old embryos (at protein level).3 Publications

Gene expression databases

ExpressionAtlasiO76922. differential.
GenevisibleiO76922. DM.

Interactioni

Subunit structurei

Interacts with vas and AGO3. Interacts (when methylated on arginine residues) with tud. Forms a complex with smg, twin, AGO3, nos mRNA and piRNAs that targets the nos 3'-untranslated region, in early embryos. Interacts with nos mRNA and rump (in an RNA-dependent manner). Interacts with papi and vret.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
tudP258237EBI-98862,EBI-498741

Protein-protein interaction databases

BioGridi60589. 5 interactions.
IntActiO76922. 4 interactions.
MINTiMINT-1628903.
STRINGi7227.FBpp0079754.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NTHX-ray2.80C10-15[»]
3NTIX-ray2.80C6-18[»]
ProteinModelPortaliO76922.
SMRiO76922. Positions 296-392, 492-843.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO76922.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini274 – 383110PAZPROSITE-ProRule annotationAdd
BLAST
Domaini555 – 852298PiwiPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1042. Eukaryota.
ENOG410XNRH. LUCA.
GeneTreeiENSGT00760000119148.
InParanoidiO76922.
KOiK02156.
OMAiYSQAIDN.
OrthoDBiEOG712TVQ.
PhylomeDBiO76922.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR003100. PAZ_dom.
IPR003165. Piwi.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF02170. PAZ. 1 hit.
PF02171. Piwi. 1 hit.
[Graphical view]
SMARTiSM00949. PAZ. 1 hit.
SM00950. 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. AlignAdd to basket

Isoform A7 Publications (identifier: O76922-1) [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
MNLPPNPVIA RGRGRGRKPN NVEANRGFAP SLGQKSDPSH SEGNQASGGN
60 70 80 90 100
GGGGDAQVGP SIEKSSLSAV QMHKSEGDPR GSVRGRRLIT DLVYSRPPGM
110 120 130 140 150
TSKKGVVGTH ITVQANYFKV LKRPNWTIYQ YRVDFTPDVE ATRLRRSFLY
160 170 180 190 200
EHKGILGGYI FDGTNMFCIN QFKAVQDSPY VLELVTKSRA GENIEIKIKA
210 220 230 240 250
VGSVQSTDAE QFQVLNLILR RAMEGLDLKL VSRYYYDPQA KINLENFRMQ
260 270 280 290 300
LWPGYQTSIR QHENDILLCS EICHKVMRTE TLYNILSDAI RDSDDYQSTF
310 320 330 340 350
KRAVMGMVIL TDYNNKTYRI DDVDFQSTPL CKFKTNDGEI SYVDYYKKRY
360 370 380 390 400
NIIIRDLKQP LVMSRPTDKN IRGGNDQAIM IIPELARATG MTDAMRADFR
410 420 430 440 450
TLRAMSEHTR LNPDRRIERL RMFNKRLKSC KQSVETLKSW NIELDSALVE
460 470 480 490 500
IPARVLPPEK ILFGNQKIFV CDARADWTNE FRTCSMFKNV HINRWYVITP
510 520 530 540 550
SRNLRETQEF VQMCIRTASS MKMNICNPIY EEIPDDRNGT YSQAIDNAAA
560 570 580 590 600
NDPQIVMVVM RSPNEEKYSC IKKRTCVDRP VPSQVVTLKV IAPRQQKPTG
610 620 630 640 650
LMSIATKVVI QMNAKLMGAP WQVVIPLHGL MTVGFDVCHS PKNKNKSYGA
660 670 680 690 700
FVATMDQKES FRYFSTVNEH IKGQELSEQM SVNMACALRS YQEQHRSLPE
710 720 730 740 750
RILFFRDGVG DGQLYQVVNS EVNTLKDRLD EIYKSAGKQE GCRMTFIIVS
760 770 780 790 800
KRINSRYFTG HRNPVPGTVV DDVITLPERY DFFLVSQAVR IGTVSPTSYN
810 820 830 840 850
VISDNMGLNA DKLQMLSYKM THMYYNYSGT IRVPAVCHYA HKLAFLVAES
860
INRAPSAGLQ NQLYFL
Length:866
Mass (Da):98,559
Last modified:November 1, 1998 - v1
Checksum:i8F84CF1B0B89103B
GO
Isoform C3 Publications (identifier: O76922-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-71: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:795
Mass (Da):91,455
Checksum:i4D16FF13551CC5EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81V → G in AGA18939 (PubMed:22997235).Curated
Sequence conflicti8 – 81V → G in AGA18942 (PubMed:22997235).Curated
Sequence conflicti118 – 1181F → S in AFX62835 (Ref. 7) Curated
Sequence conflicti193 – 1931N → T in AGA18939 (PubMed:22997235).Curated
Sequence conflicti193 – 1931N → T in AGA18941 (PubMed:22997235).Curated
Sequence conflicti193 – 1931N → T in AGA18942 (PubMed:22997235).Curated
Sequence conflicti193 – 1931N → T in AFX62834 (Ref. 7) Curated
Sequence conflicti295 – 2951D → G in AFX62833 (Ref. 7) Curated
Sequence conflicti551 – 5511N → K in AFX62833 (Ref. 7) Curated
Sequence conflicti551 – 5511N → K in AFX62834 (Ref. 7) Curated
Sequence conflicti578 – 5781D → G in AFX62834 (Ref. 7) Curated
Sequence conflicti615 – 6151K → R in AFX62834 (Ref. 7) Curated
Sequence conflicti685 – 6851A → S in AGA18946 (PubMed:22997235).Curated
Sequence conflicti747 – 7471I → T in AFX62834 (Ref. 7) Curated
Sequence conflicti755 – 7551S → T in AGA18940 (PubMed:22997235).Curated
Sequence conflicti755 – 7551S → T in AGA18942 (PubMed:22997235).Curated
Sequence conflicti755 – 7551S → T in AGA18946 (PubMed:22997235).Curated
Sequence conflicti755 – 7551S → T in AFX62833 (Ref. 7) Curated
Sequence conflicti755 – 7551S → T in AFX62834 (Ref. 7) Curated
Sequence conflicti823 – 8231M → T in AFX62833 (Ref. 7) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7171Missing in isoform C. 1 PublicationVSP_047356Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94613 Genomic DNA. Translation: CAA64320.1.
KC116210 Genomic DNA. Translation: AGA18939.1.
KC116211 Genomic DNA. Translation: AGA18940.1.
KC116212 Genomic DNA. Translation: AGA18941.1.
KC116213 Genomic DNA. Translation: AGA18942.1.
KC116214 Genomic DNA. Translation: AGA18943.1.
KC116215 Genomic DNA. Translation: AGA18944.1.
KC116216 Genomic DNA. Translation: AGA18945.1.
KC116217 Genomic DNA. Translation: AGA18946.1.
AE014134 Genomic DNA. Translation: AAF53046.1.
AE014134 Genomic DNA. Translation: ABV53667.1.
AF145680 mRNA. Translation: AAD38655.1.
JX656893 mRNA. Translation: AFX62833.1.
JX656894 mRNA. Translation: AFX62834.1.
JX656895 mRNA. Translation: AFX62835.1.
RefSeqiNP_001097144.1. NM_001103674.3. [O76922-2]
NP_476734.1. NM_057386.5. [O76922-1]
UniGeneiDm.3112.

Genome annotation databases

EnsemblMetazoaiFBtr0080165; FBpp0079754; FBgn0000146. [O76922-1]
GeneIDi34524.
KEGGidme:Dmel_CG6137.
UCSCiCG6137-RA. d. melanogaster. [O76922-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94613 Genomic DNA. Translation: CAA64320.1.
KC116210 Genomic DNA. Translation: AGA18939.1.
KC116211 Genomic DNA. Translation: AGA18940.1.
KC116212 Genomic DNA. Translation: AGA18941.1.
KC116213 Genomic DNA. Translation: AGA18942.1.
KC116214 Genomic DNA. Translation: AGA18943.1.
KC116215 Genomic DNA. Translation: AGA18944.1.
KC116216 Genomic DNA. Translation: AGA18945.1.
KC116217 Genomic DNA. Translation: AGA18946.1.
AE014134 Genomic DNA. Translation: AAF53046.1.
AE014134 Genomic DNA. Translation: ABV53667.1.
AF145680 mRNA. Translation: AAD38655.1.
JX656893 mRNA. Translation: AFX62833.1.
JX656894 mRNA. Translation: AFX62834.1.
JX656895 mRNA. Translation: AFX62835.1.
RefSeqiNP_001097144.1. NM_001103674.3. [O76922-2]
NP_476734.1. NM_057386.5. [O76922-1]
UniGeneiDm.3112.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NTHX-ray2.80C10-15[»]
3NTIX-ray2.80C6-18[»]
ProteinModelPortaliO76922.
SMRiO76922. Positions 296-392, 492-843.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60589. 5 interactions.
IntActiO76922. 4 interactions.
MINTiMINT-1628903.
STRINGi7227.FBpp0079754.

Proteomic databases

PaxDbiO76922.
PRIDEiO76922.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0080165; FBpp0079754; FBgn0000146. [O76922-1]
GeneIDi34524.
KEGGidme:Dmel_CG6137.
UCSCiCG6137-RA. d. melanogaster. [O76922-1]

Organism-specific databases

CTDi34524.
FlyBaseiFBgn0000146. aub.

Phylogenomic databases

eggNOGiKOG1042. Eukaryota.
ENOG410XNRH. LUCA.
GeneTreeiENSGT00760000119148.
InParanoidiO76922.
KOiK02156.
OMAiYSQAIDN.
OrthoDBiEOG712TVQ.
PhylomeDBiO76922.

Miscellaneous databases

EvolutionaryTraceiO76922.
GenomeRNAii34524.
PROiO76922.

Gene expression databases

ExpressionAtlasiO76922. differential.
GenevisibleiO76922. DM.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR003100. PAZ_dom.
IPR003165. Piwi.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF02170. PAZ. 1 hit.
PF02171. Piwi. 1 hit.
[Graphical view]
SMARTiSM00949. PAZ. 1 hit.
SM00950. Piwi. 1 hit.
[Graphical view]
SUPFAMiSSF101690. SSF101690. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEiPS50821. PAZ. 1 hit.
PS50822. PIWI. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A newly identified Minute locus, M(2)32D, encodes the ribosomal protein L9 in Drosophila melanogaster."
    Schmidt A., Hollmann M., Schaefer U.
    Mol. Gen. Genet. 251:381-387(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Canton-SImported.
    Tissue: EmbryoImported.
  2. "Genetic and molecular characterization of sting, a gene involved in crystal formation and meiotic drive in the male germ line of Drosophila melanogaster."
    Schmidt A., Palumbo G., Bozzetti M.P., Tritto P., Pimpinelli S., Schafer U.
    Genetics 151:749-760(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    Strain: Canton-SImported.
    Tissue: EmbryoImported.
  3. "Long-term and short-term evolutionary impacts of transposable elements on Drosophila."
    Lee Y.C., Langley C.H.
    Genetics 192:1411-1432(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 3846Imported, 3852Imported, 3853Imported, 3854Imported, 3892Imported, 3893Imported and 3895Imported.
  4. "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.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  7. "Variability in the piRNA pathway induces a variable load of transposable elements in wild type strains of Drosophila simulans."
    Fablet M., Akkouche A., Braman V., Vieira C.
    Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-847.
  8. "Female sterile mutations on the second chromosome of Drosophila melanogaster. II. Mutations blocking oogenesis or altering egg morphology."
    Schupbach T., Wieschaus E.
    Genetics 129:1119-1136(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  9. "aubergine enhances oskar translation in the Drosophila ovary."
    Wilson J.E., Connell J.E., Macdonald P.M.
    Development 122:1631-1639(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. "Aubergine encodes a Drosophila polar granule component required for pole cell formation and related to eIF2C."
    Harris A.N., Macdonald P.M.
    Development 128:2823-2832(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "RNAi is activated during Drosophila oocyte maturation in a manner dependent on aubergine and spindle-E."
    Kennerdell J.R., Yamaguchi S., Carthew R.W.
    Genes Dev. 16:1884-1889(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Maelstrom, a Drosophila spindle-class gene, encodes a protein that colocalizes with Vasa and RDE1/AGO1 homolog, Aubergine, in nuage."
    Findley S.D., Tamanaha M., Clegg N.J., Ruohola-Baker H.
    Development 130:859-871(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "The Drosophila SDE3 homolog armitage is required for oskar mRNA silencing and embryonic axis specification."
    Cook H.A., Koppetsch B.S., Wu J., Theurkauf W.E.
    Cell 116:817-829(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Live imaging of nuage and polar granules: evidence against a precursor-product relationship and a novel role for Oskar in stabilization of polar granule components."
    Snee M.J., Macdonald P.M.
    J. Cell Sci. 117:2109-2120(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. "aubergine mutations in Drosophila melanogaster impair P cytotype determination by telomeric P elements inserted in heterochromatin."
    Reiss D., Josse T., Anxolabehere D., Ronsseray S.
    Mol. Genet. Genomics 272:336-343(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Heterochromatic silencing and HP1 localization in Drosophila are dependent on the RNAi machinery."
    Pal-Bhadra M., Leibovitch B.A., Gandhi S.G., Rao M., Bhadra U., Birchler J.A., Elgin S.C.R.
    Science 303:669-672(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Telomere elongation is under the control of the RNAi-based mechanism in the Drosophila germline."
    Savitsky M., Kwon D., Georgiev P., Kalmykova A., Gvozdev V.
    Genes Dev. 20:345-354(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Discrete small RNA-generating loci as master regulators of transposon activity in Drosophila."
    Brennecke J., Aravin A.A., Stark A., Dus M., Kellis M., Sachidanandam R., Hannon G.J.
    Cell 128:1089-1103(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  19. "Gene silencing mechanisms mediated by Aubergine piRNA complexes in Drosophila male gonad."
    Nishida K.M., Saito K., Mori T., Kawamura Y., Nagami-Okada T., Inagaki S., Siomi H., Siomi M.C.
    RNA 13:1911-1922(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  20. "A slicer-mediated mechanism for repeat-associated siRNA 5' end formation in Drosophila."
    Gunawardane L.S., Saito K., Nishida K.M., Miyoshi K., Kawamura Y., Nagami T., Siomi H., Siomi M.C.
    Science 315:1587-1590(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING.
  21. "Isolation of new polar granule components in Drosophila reveals P body and ER associated proteins."
    Thomson T., Liu N., Arkov A., Lehmann R., Lasko P.
    Mech. Dev. 125:865-873(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VAS AND TUD, SUBCELLULAR LOCATION.
  22. Cited for: SUBCELLULAR LOCATION.
  23. "Functional involvement of Tudor and dPRMT5 in the piRNA processing pathway in Drosophila germlines."
    Nishida K.M., Okada T.N., Kawamura T., Mituyama T., Kawamura Y., Inagaki S., Huang H., Chen D., Kodama T., Siomi H., Siomi M.C.
    EMBO J. 28:3820-3831(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, RNA-BINDING, INTERACTION WITH TUD AND AGO3, ACETYLATION AT MET-1, METHYLATION AT ARG-11; ARG-13 AND ARG-15.
  24. "Arginine methylation of Piwi proteins catalysed by dPRMT5 is required for Ago3 and Aub stability."
    Kirino Y., Kim N., de Planell-Saguer M., Khandros E., Chiorean S., Klein P.S., Rigoutsos I., Jongens T.A., Mourelatos Z.
    Nat. Cell Biol. 11:652-658(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, METHYLATION, MUTAGENESIS OF 11-ARG--ARG-17.
  25. "Maternal mRNA deadenylation and decay by the piRNA pathway in the early Drosophila embryo."
    Rouget C., Papin C., Boureux A., Meunier A.C., Franco B., Robine N., Lai E.C., Pelisson A., Simonelig M.
    Nature 467:1128-1132(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, INTERACTION WITH SMG; TWIN AND AGO3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  26. "Arginine methylation of Aubergine mediates Tudor binding and germ plasm localization."
    Kirino Y., Vourekas A., Sayed N., de Lima Alves F., Thomson T., Lasko P., Rappsilber J., Jongens T.A., Mourelatos Z.
    RNA 16:70-78(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TUD, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, METHYLATION, MUTAGENESIS OF 11-ARG--ARG-17.
  27. "Biogenesis pathways of piRNAs loaded onto AGO3 in the Drosophila testis."
    Nagao A., Mituyama T., Huang H., Chen D., Siomi M.C., Siomi H.
    RNA 16:2503-2515(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  28. "PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and TRAL in the nuage to silence transposition."
    Liu L., Qi H., Wang J., Lin H.
    Development 138:1863-1873(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAPI, SUBCELLULAR LOCATION.
  29. "Vreteno, a gonad-specific protein, is essential for germline development and primary piRNA biogenesis in Drosophila."
    Zamparini A.L., Davis M.Y., Malone C.D., Vieira E., Zavadil J., Sachidanandam R., Hannon G.J., Lehmann R.
    Development 138:4039-4050(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VRET.
  30. "Aubergine is a component of a nanos mRNA localization complex."
    Becalska A.N., Kim Y.R., Belletier N.G., Lerit D.A., Sinsimer K.S., Gavis E.R.
    Dev. Biol. 349:46-52(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, INTERACTION WITH RUMP.
  31. "Mutations to the piRNA pathway component Aubergine enhance meiotic drive of segregation distorter in Drosophila melanogaster."
    Gell S.L., Reenan R.A.
    Genetics 193:771-784(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-721.
  32. "Transposition-driven genomic heterogeneity in the Drosophila brain."
    Perrat P.N., DasGupta S., Wang J., Theurkauf W., Weng Z., Rosbash M., Waddell S.
    Science 340:91-95(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  33. "Structural basis for methylarginine-dependent recognition of Aubergine by Tudor."
    Liu H., Wang J.Y., Huang Y., Li Z., Gong W., Lehmann R., Xu R.M.
    Genes Dev. 24:1876-1881(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 6-18 IN COMPLEX WITH TUD, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, METHYLATION AT ARG-11; ARG-13 AND ARG-15.

Entry informationi

Entry nameiAUB_DROME
AccessioniPrimary (citable) accession number: O76922
Secondary accession number(s): A8DYZ0
, K7WQ34, K7X543, K7XHY9, L0CPY1, L0CQ70, L0CRA0, L0CRA6, L0CRP1, L0CRZ4, L0CS00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2013
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 123 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.