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DROME:DDX6

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Species (Taxon ID) Drosophila melanogaster (Fruit fly). (7227)
Gene Name(s) me31B
Protein Name(s) Putative ATP-dependent RNA helicase me31b

Maternal expression at 31B

External Links
UniProt P23128
EMBL M59926
AE014134
AE014134
AY051663
PIR A39157
RefSeq NP_523533.2
NP_723539.1
UniGene Dm.2770
ProteinModelPortal P23128
SMR P23128
BioGrid 60455
IntAct P23128
MINT MINT-769276
STRING 7227.FBpp0079565
iPTMnet P23128
PaxDb P23128
PRIDE P23128
EnsemblMetazoa FBtr0079975
GeneID 34364
KEGG dme:Dmel_CG4916
CTD 34364
FlyBase FBgn0004419
eggNOG KOG0326
ENOG410XRAZ
GeneTree ENSGT00870000136507
InParanoid P23128
KO K12614
OMA IYQKVQV
OrthoDB EOG091G0623
PhylomeDB P23128
Reactome [www.reactome.org/content/detail/R-DME-430039 R-DME-430039]
ChiTaRS me31B
GenomeRNAi 34364
PRO PR:P23128
Proteomes UP000000803
Bgee FBgn0004419
Genevisible P23128
GO GO:0005737
GO:0010494
GO:0005875
GO:0043186
GO:0000932
GO:0005524
GO:0004004
GO:0003723
GO:0033962
GO:0035195
GO:0046959
GO:0007095
GO:0030707
GO:0007279
GO:0050688
GO:0010906
GO:0090328
GO:0010501
Gene3D 3.40.50.300
InterPro IPR011545
IPR014001
IPR001650
IPR027417
IPR000629
IPR014014
Pfam PF00270
PF00271
SMART SM00487
SM00490
SUPFAM SSF52540
PROSITE PS00039
PS51192
PS51194
PS51195

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0000166

nucleotide binding

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0547

F

Seeded From UniProt

GO:0000932

P-body

PMID:17403906[1]

IDA: Inferred from Direct Assay

-

C

Seeded From UniProt

GO:0000932

P-body

PMID:17595295[2]

IDA: Inferred from Direct Assay

-

C

Seeded From UniProt

GO:0000932

P-body

PMID:20452345[3]

IDA: Inferred from Direct Assay

-

C

Seeded From UniProt

GO:0000932

P-body

PMID:21655181[4]

IDA: Inferred from Direct Assay

-

C

Seeded From UniProt

GO:0003676

nucleic acid binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011545

F

Seeded From UniProt

GO:0003723

RNA binding

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0694

F

Seeded From UniProt

GO:0003723

RNA binding

PMID:16469699[5]

IDA: Inferred from Direct Assay

-

F

Seeded From UniProt

GO:0004004

ATP-dependent RNA helicase activity

GO_REF:0000033

IBA: Inferred from Biological aspect of Ancestor

PANTHER:PTN000618218

F

Seeded From UniProt

GO:0004004

ATP-dependent RNA helicase activity

PMID:10471706[6]

NAS: Non-traceable Author Statement

-

F

Seeded From UniProt

GO:0004386

helicase activity

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0347

F

Seeded From UniProt

GO:0005515

protein binding

PMID:14605208[7]

IPI: Inferred from Physical Interaction

UniProtKB:Q9VMA3

F

Seeded From UniProt

GO:0005515

protein binding

PMID:14723848[8]

IPI: Inferred from Physical Interaction

UniProtKB:Q9VMA3

F

Seeded From UniProt

GO:0005515

protein binding

PMID:17923697[9]

IPI: Inferred from Physical Interaction

UniProtKB:Q9VVI2

F

Seeded From UniProt

GO:0005515

protein binding

PMID:21447556[10]

IPI: Inferred from Physical Interaction

FB:FBgn0031401

F

Seeded From UniProt

GO:0005524

ATP binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011545

F

Seeded From UniProt

GO:0005524

ATP binding

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0067

F

Seeded From UniProt

GO:0005737

cytoplasm

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0963

C

Seeded From UniProt

GO:0005737

cytoplasm

GO_REF:0000039

IEA: Inferred from Electronic Annotation

UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

GO:0005737

cytoplasm

PMID:18708044[11]

IDA: Inferred from Direct Assay

-

C

Seeded From UniProt

GO:0005737

cytoplasm

PMID:25294944[12]

IDA: Inferred from Direct Assay

-

C

Seeded From UniProt

GO:0005875

microtubule associated complex

PMID:18433294[13]

IDA: Inferred from Direct Assay

-

C

Seeded From UniProt

GO:0007095

mitotic G2 DNA damage checkpoint

PMID:21205937[14]

IGI: Inferred from Genetic Interaction

FB:FBgn0261530

P

Seeded From UniProt

GO:0007279

pole cell formation

PMID:18590813[15]

IGI: Inferred from Genetic Interaction

FB:FBgn0003891

P

Seeded From UniProt

GO:0007279

pole cell formation

PMID:18590813[15]

IGI: Inferred from Genetic Interaction

FB:FBgn0283442

P

Seeded From UniProt

GO:0010494

cytoplasmic stress granule

GO_REF:0000033

IBA: Inferred from Biological aspect of Ancestor

PANTHER:PTN000619958

C

Seeded From UniProt

GO:0010501

RNA secondary structure unwinding

GO_REF:0000033

IBA: Inferred from Biological aspect of Ancestor

PANTHER:PTN000618218

P

Seeded From UniProt

GO:0010906

regulation of glucose metabolic process

PMID:25994086[16]

IMP: Inferred from Mutant Phenotype

-

P

Seeded From UniProt

GO:0016787

hydrolase activity

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0378

F

Seeded From UniProt

GO:0030707

ovarian follicle cell development

PMID:26205122[17]

IMP: Inferred from Mutant Phenotype

-

P

Seeded From UniProt

GO:0033962

cytoplasmic mRNA processing body assembly

PMID:17403906[1]

IMP: Inferred from Mutant Phenotype

-

P

Seeded From UniProt

GO:0035195

gene silencing by miRNA

PMID:19029310[18]

IGI: Inferred from Genetic Interaction

FB:FBgn0283682

P

Seeded From UniProt

GO:0043186

P granule

PMID:18590813[15]

IDA: Inferred from Direct Assay

-

C

Seeded From UniProt

GO:0043186

P granule

PMID:21447556[10]

IDA: Inferred from Direct Assay

-

C

Seeded From UniProt

GO:0046959

habituation

PMID:21795609[19]

IMP: Inferred from Mutant Phenotype

-

P

Seeded From UniProt

GO:0050688

regulation of defense response to virus

PMID:25126784[20]

IMP: Inferred from Mutant Phenotype

-

P

Seeded From UniProt

GO:0090328

regulation of olfactory learning

PMID:21795609[19]

IMP: Inferred from Mutant Phenotype

-

P

Seeded From UniProt

GO:0005783

endoplasmic reticulum

PMID:16256742[21]

IDA: Inferred from Direct Assay

C

Figure 6. E&G Me31B and Cup Colocalize with Both Tral and the ER in Egg Chambers. D–F) Tral and Me31B colocalize to the same particles in nurse cells. (E) Me31B. (G–I) Me31B particles localize to discrete sites on the ER (arrows). (G) Me31B. Drosophila.

complete
CACAO 12351

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Eulalio, A et al. (2007) P-body formation is a consequence, not the cause, of RNA-mediated gene silencing. Mol. Cell. Biol. 27 3970-81 PubMed GONUTS page
  2. Liu, JL & Gall, JG (2007) U bodies are cytoplasmic structures that contain uridine-rich small nuclear ribonucleoproteins and associate with P bodies. Proc. Natl. Acad. Sci. U.S.A. 104 11655-9 PubMed GONUTS page
  3. Cauchi, RJ et al. (2010) Drosophila SMN complex proteins Gemin2, Gemin3, and Gemin5 are components of U bodies. Exp. Cell Res. 316 2354-64 PubMed GONUTS page
  4. Fan, SJ et al. (2011) Drosophila Ge-1 promotes P body formation and oskar mRNA localization. PLoS ONE 6 e20612 PubMed GONUTS page
  5. Chekulaeva, M et al. (2006) Bruno acts as a dual repressor of oskar translation, promoting mRNA oligomerization and formation of silencing particles. Cell 124 521-33 PubMed GONUTS page
  6. Spradling, AC et al. (1999) The Berkeley Drosophila Genome Project gene disruption project: Single P-element insertions mutating 25% of vital Drosophila genes. Genetics 153 135-77 PubMed GONUTS page
  7. Giot, L et al. (2003) A protein interaction map of Drosophila melanogaster. Science 302 1727-36 PubMed GONUTS page
  8. Nakamura, A et al. (2004) Drosophila cup is an eIF4E binding protein that associates with Bruno and regulates oskar mRNA translation in oogenesis. Dev. Cell 6 69-78 PubMed GONUTS page
  9. Tritschler, F et al. (2007) A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting. Mol. Cell. Biol. 27 8600-11 PubMed GONUTS page
  10. 10.0 10.1 Liu, L et al. (2011) PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and TRAL in the nuage to silence transposition. Development 138 1863-73 PubMed GONUTS page
  11. Lin, MD et al. (2008) Drosophila processing bodies in oogenesis. Dev. Biol. 322 276-88 PubMed GONUTS page
  12. Lye, CM et al. (2014) Subcellular localisations of the CPTI collection of YFP-tagged proteins in Drosophila embryos. Development 141 4006-17 PubMed GONUTS page
  13. Hughes, JR et al. (2008) A microtubule interactome: complexes with roles in cell cycle and mitosis. PLoS Biol. 6 e98 PubMed GONUTS page
  14. Kondo, S & Perrimon, N (2011) A genome-wide RNAi screen identifies core components of the G₂-M DNA damage checkpoint. Sci Signal 4 rs1 PubMed GONUTS page
  15. 15.0 15.1 15.2 Thomson, T et al. () Isolation of new polar granule components in Drosophila reveals P body and ER associated proteins. Mech. Dev. 125 865-73 PubMed GONUTS page
  16. Ugrankar, R et al. (2015) Drosophila glucome screening identifies Ck1alpha as a regulator of mammalian glucose metabolism. Nat Commun 6 7102 PubMed GONUTS page
  17. Jia, D et al. (2015) A large-scale in vivo RNAi screen to identify genes involved in Notch-mediated follicle cell differentiation and cell cycle switches. Sci Rep 5 12328 PubMed GONUTS page
  18. Eulalio, A et al. (2009) Deadenylation is a widespread effect of miRNA regulation. RNA 15 21-32 PubMed GONUTS page
  19. 19.0 19.1 McCann, C et al. (2011) The Ataxin-2 protein is required for microRNA function and synapse-specific long-term olfactory habituation. Proc. Natl. Acad. Sci. U.S.A. 108 E655-62 PubMed GONUTS page
  20. Moy, RH et al. (2014) Stem-loop recognition by DDX17 facilitates miRNA processing and antiviral defense. Cell 158 764-77 PubMed GONUTS page
  21. Wilhelm, JE et al. (2005) Efficient protein trafficking requires trailer hitch, a component of a ribonucleoprotein complex localized to the ER in Drosophila. Dev. Cell 9 675-85 PubMed GONUTS page