FB2024_03 , released June 25, 2024
Gene: Dmel\osk
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General Information
Symbol
Dmel\osk
Species
D. melanogaster
Name
oskar
Annotation Symbol
CG10901
Feature Type
FlyBase ID
FBgn0003015
Gene Model Status
Stock Availability
Gene Summary
Organizes the germ plasm and directs localization of the posterior determinant nanos. Oskar protein is required to keep nanos (nos) RNA and staufen protein at the posterior pole. (UniProt, P25158)
Contribute a Gene Snapshot for this gene.
Key Links
Genomic Location
Cytogenetic map
Sequence location
Recombination map
3-48
RefSeq locus
NT_033777 REGION:8935126..8938395
Sequence
Genomic Maps
Other Genome Views
The following external sites may use different assemblies or annotations than FlyBase.
Function
Gene Ontology (GO) Annotations (26 terms)
Molecular Function (1 term)
Terms Based on Experimental Evidence (1 term)
CV Term
Evidence
References
enables mRNA binding
inferred from direct assay
Terms Based on Predictions or Assertions (0 terms)
Biological Process (19 terms)
Terms Based on Experimental Evidence (14 terms)
CV Term
Evidence
References
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
involved_in oogenesis
inferred from mutant phenotype
involved_in P granule assembly
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
involved_in visual behavior
inferred from mutant phenotype
involved_in visual learning
inferred from mutant phenotype
Terms Based on Predictions or Assertions (6 terms)
CV Term
Evidence
References
Cellular Component (6 terms)
Terms Based on Experimental Evidence (5 terms)
CV Term
Evidence
References
located_in cell cortex
inferred from direct assay
located_in cytoplasm
inferred from direct assay
inferred from direct assay
located_in P granule
inferred from direct assay
inferred from direct assay
Terms Based on Predictions or Assertions (1 term)
CV Term
Evidence
References
Gene Group (FlyBase)
Protein Family (UniProt)
-
Summaries
Protein Function (UniProtKB)
Organizes the germ plasm and directs localization of the posterior determinant nanos. Oskar protein is required to keep nanos (nos) RNA and staufen protein at the posterior pole.
(UniProt, P25158)
Phenotypic Description (Red Book; Lindsley and Zimm 1992)
osk: oskar
Homozygous females normally viable and fecund; homozygous males fertile. Embryos produced by homozygous females lack pole plasm and fail to produce pole cells; abdominal region remains unsegmented and eventually dies. Temperature-sensitive period for the germ-line effect is the last six hours of oogenesis and for abdominal development the last twelve to fourteen hours (osk8). Homozygous osk germ cells autonomous in pole cell transplants. Polar cytoplasm from unfertilized eggs or normal embryos capable of rescuing pole cell formation if injected at the posterior extremity of the early embryo and abdominal segmentation, to the extent of producing viable but sterile adults, if injected into the posterior half of preblastoderm embryos. Embryos produced by homozygous BicD; osk females are indistinguishable from those produced by osk alone suggesting that osk+ product is required for the formation of bicaudal embryos; also required for the early anterior-posterior gradient of hb expression (Tautz, 1988, Nature 332: 181-84).
Summary (Interactive Fly)

novel - assembles germ plasm - a anterior/posterior determinant regulating embryonic development - oskar RNA plays multiple noncoding roles to support oogenesis and maintain integrity of the germline/soma distinction.

Gene Model and Products
Number of Transcripts
2
Number of Unique Polypeptides
2

Please see the JBrowse view of Dmel\osk for information on other features

To submit a correction to a gene model please use the Contact FlyBase form

Protein Domains (via Pfam)
Isoform displayed:
Pfam protein domains
InterPro name
classification
start
end
Protein Domains (via SMART)
Isoform displayed:
SMART protein domains
InterPro name
classification
start
end
Structure
Protein 3D structure   (Predicted by AlphaFold)   (AlphaFold entry P25158)

If you don't see a structure in the viewer, refresh your browser.
Model Confidence:
  • Very high (pLDDT > 90)
  • Confident (90 > pLDDT > 70)
  • Low (70 > pLDDT > 50)
  • Very low (pLDDT < 50)

AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.

Experimentally Determined Structures
Crossreferences
PDB - An information portal to biological macromolecular structures
Comments on Gene Model

Gene model reviewed during 5.47

Gene model reviewed during 6.04

Overlaps non-coding gene lncRNA:osk .

Gene model reviewed during 6.27

Sequence Ontology: Class of Gene
Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Assoc. CDS (aa)
FBtr0081954
2869
606
FBtr0081956
2869
468
Additional Transcript Data and Comments
Reported size (kB)

2.9 (longest cDNA)

2.9 (northern blot)

Comments
External Data
Crossreferences
Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
UniProt
RefSeq ID
GenBank
FBpp0081435
69.3
606
9.60
FBpp0089372
53.7
468
8.81
Polypeptides with Identical Sequences

None of the polypeptides share 100% sequence identity.

Additional Polypeptide Data and Comments
Reported size (kDa)

606 (aa); 69 (kD predicted)

Comments
External Data
Subunit Structure (UniProtKB)

Interacts with smaug (smg).

(UniProt, P25158)
Crossreferences
InterPro - A database of protein families, domains and functional sites
PDB - An information portal to biological macromolecular structures
Linkouts
Sequences Consistent with the Gene Model
Mapped Features

Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\osk using the Feature Mapper tool.

External Data
Crossreferences
Eukaryotic Promoter Database - A collection of databases of experimentally validated promoters for selected model organisms.
Linkouts
Expression Data
Testis-specificity index

The testis specificity index was calculated from modENCODE tissue expression data by Vedelek et al., 2018 to indicate the degree of testis enrichment compared to other tissues. Scores range from -2.52 (underrepresented) to 5.2 (very high testis bias).

-0.29

Transcript Expression
No Assay Recorded
Stage
Tissue/Position (including subcellular localization)
Reference
in situ
Stage
Tissue/Position (including subcellular localization)
Reference
pole plasm

Comment: maternally deposited

organism

Comment: maternally deposited

microinjection
Stage
Tissue/Position (including subcellular localization)
Reference
oocyte | restricted

Comment: in vivo imaging, molecular beacons

northern blot
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data

Endogenous osk mRNA was visualized using molecular beacons. The in vivo dynamic behavior of osk was imaged over the entire oocyte in stage 7 to 10 oocytes, capturing the dynamics of osk from its nuclear export to localization at the posterior of the oocyte. osk mRNA is present in particles distince from stau protein for part of its transport and stable associates with stau protein near the posterior pole. osk mRNA oligomerizes as hundreds of copies forming large particles, which are necessary for long-range transport and localization.

osk expression at embryonic stages 1-4 is localized to the posterior pole of the embryo.

oskar mRNA is localized to the posterior pole of the oocyte.

osk mRNA is initially concentrated in the oocyte and becomes localized to the posterior pole. It persists at the posterior pole through oogenesis and through the cleavage stages of embryogenesis.

From the earliest stages in oogenesis, osk RNA is enriched in the cell that will become the oocyte but is also present in nurse cells. At the early stages, osk RNA is distributed throughout the oocyte. By stage S8, enrichment at the anterior and posterior poles of the oocyte are apparent. After stage S9, and throughout early embryogenesis, osk RNA is strictly localized to the posterior pole. By the cellular blastoderm stage, osk RNA is no longer detected by in situ hybridization.

osk transcripts are first detected in the most mature regions of the germarium where they are present in all of the dividing cells. In stages S1-S6, osk RNA is present throughout the nurse cell-oocyte complex but is concentrated in the cell that will be the oocyte. During stages S8 and S9, osk RNA becomes localized to a cap at the posterior pole of the oocyte. After the striking posterior localization has occurred, osk transcripts accumulate to high levels in the nurse cells. In embryos, osk transcripts are localized to the posterior pole. They begin to disappear from the posterior pole by nuclear division 6 or 7 and very little localized osk RNA remains after the 9th nuclear division.

osk mRNA accumulates at high levels in the oocyte starting in germarium region 2B and this accumulation is not affected in recessive BicD mutants. osk RNA does not localize to the oocyte in egl mutants.

Marker for
Subcellular Localization
CV Term
Polypeptide Expression
No Assay Recorded
Stage
Tissue/Position (including subcellular localization)
Reference
immunolocalization
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data

oskar protein is localized to the posterior pole of the oocyte. In 0-2 hour embryos, oskar protein is maintained in a tight crescent at the posterior pole.

In stage 10 oocytes, vas protein, osk protein, and stau protein colocalize at the posterior pole. In early embryos, vas protein and osk protein localize to the polar granules but stau protein does not colocalize with them. It is present in a thin crescent apposed closely to the posterior cortex and disappears before the pole cell stage. A GFP-Vas fusion protein was used to determine the vas protein distribution.

osk protein is first detected at the posterior pole of the oocyte during stage 9. It persists at the posterior pole into embryogenesis.

Marker for
Subcellular Localization
CV Term
Evidence
References
located_in cell cortex
inferred from direct assay
located_in cytoplasm
inferred from direct assay
inferred from direct assay
located_in P granule
inferred from direct assay
inferred from direct assay
Expression Deduced from Reporters
High-Throughput Expression Data
Associated Tools

JBrowse - Visual display of RNA-Seq signals

View Dmel\osk in JBrowse
RNA-Seq by Region - Search RNA-Seq expression levels by exon or genomic region
Reference
See Gelbart and Emmert, 2013 for analysis details and data files for all genes.
Developmental Proteome: Life Cycle
Developmental Proteome: Embryogenesis
External Data and Images
Linkouts
BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
DRscDB - A single-cell RNA-seq resource for data mining and data comparison across species
EMBL-EBI Single Cell Expression Atlas - Single cell expression across species
FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
FlyAtlas2 - A Drosophila melanogaster expression atlas with RNA-Seq, miRNA-Seq and sex-specific data
Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
Flygut - An atlas of the Drosophila adult midgut
Images
FlyExpress - Embryonic expression images (BDGP data)
  • Stages(s) 1-3
  • Stages(s) 4-6
  • Stages(s) 9-10
Alleles, Insertions, Transgenic Constructs, and Aberrations
Classical and Insertion Alleles ( 41 )
For All Classical and Insertion Alleles Show
 
Other relevant insertions
Transgenic Constructs ( 302 )
For All Alleles Carried on Transgenic Constructs Show
Transgenic constructs containing/affecting coding region of osk
Transgenic constructs containing regulatory region of osk
Aberrations (Deficiencies and Duplications) ( 8 )
Variants
Variant Molecular Consequences
Alleles Representing Disease-Implicated Variants
Phenotypes
For more details about a specific phenotype click on the relevant allele symbol.
Lethality
Allele
Sterility
Allele
Other Phenotypes
Allele
Phenotype manifest in
Allele
embryonic/first instar larval cuticle & embryonic head, with Scer\GAL4VP16.nanos.UTR
filamentous actin & oocyte, with Scer\GAL4VP16.mat.αTub67C
microtubule & oocyte | oogenesis stage S9, with Scer\GAL4VP16.mat.αTub67C
microtubule & oocyte | oogenesis stage S9 (with Df(3R)p-XT103)
Orthologs
Human Orthologs (via DIOPT v9.1)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
Homo sapiens (Human) (0)
Model Organism Orthologs (via DIOPT v9.1)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
Rattus norvegicus (Norway rat) (0)
Mus musculus (laboratory mouse) (0)
Xenopus tropicalis (Western clawed frog) (0)
Danio rerio (Zebrafish) (0)
Caenorhabditis elegans (Nematode, roundworm) (0)
Anopheles gambiae (African malaria mosquito) (1)
3 of 12
Yes
Yes
Arabidopsis thaliana (thale-cress) (0)
Saccharomyces cerevisiae (Brewer's yeast) (0)
Schizosaccharomyces pombe (Fission yeast) (0)
Escherichia coli (enterobacterium) (0)
Other Organism Orthologs (via OrthoDB)
Data provided directly from OrthoDB:osk. Refer to their site for version information.
Paralogs
Paralogs (via DIOPT v9.1)
Human Disease Associations
FlyBase Human Disease Model Reports
    Disease Ontology (DO) Annotations
    Models Based on Experimental Evidence ( 0 )
    Allele
    Disease
    Evidence
    References
    Potential Models Based on Orthology ( 0 )
    Human Ortholog
    Disease
    Evidence
    References
    Modifiers Based on Experimental Evidence ( 0 )
    Allele
    Disease
    Interaction
    References
    Disease Associations of Human Orthologs (via DIOPT v9.1 and OMIM)
    Note that ortholog calls supported by only 1 or 2 algorithms (DIOPT score < 3) are not shown.
    Homo sapiens (Human)
    Gene name
    Score
    OMIM
    OMIM Phenotype
    DO term
    Complementation?
    Transgene?
    Functional Complementation Data
    Functional complementation data is computed by FlyBase using a combination of the orthology data obtained from DIOPT and OrthoDB and the allele-level genetic interaction data curated from the literature.
    Interactions
    Summary of Physical Interactions
    esyN Network Diagram
    Show neighbor-neighbor interactions:
    Show/hide secondary interactors 
    (data from AllianceMine provided by esyN)
    Select Layout:
    Legend:
    Protein
    RNA
    Selected Interactor(s)
    Other Interaction Browsers

    Please see the Physical Interaction reports below for full details
    protein-protein
    Physical Interaction
    Assay
    References
    RNA-protein
    Physical Interaction
    Assay
    References
    Summary of Genetic Interactions
    esyN Network Diagram
    Show/hide secondary interactors 
    (data from AllianceMine provided by esyN)
    esyN Network Key:
    Suppression
    Enhancement
    Other Interaction Browsers

    Please look at the allele data for full details of the genetic interactions
    Starting gene(s)
    Interaction type
    Interacting gene(s)
    Reference
    Starting gene(s)
    Interaction type
    Interacting gene(s)
    Reference
    External Data
    Subunit Structure (UniProtKB)
    Interacts with smaug (smg).
    (UniProt, P25158 )
    Linkouts
    BioGRID - A database of protein and genetic interactions.
    DroID - A comprehensive database of gene and protein interactions.
    MIST (genetic) - An integrated Molecular Interaction Database
    MIST (protein-protein) - An integrated Molecular Interaction Database
    Pathways
    Signaling Pathways (FlyBase)
    Metabolic Pathways
    External Data
    Linkouts
    Genomic Location and Detailed Mapping Data
    Chromosome (arm)
    3R
    Recombination map
    3-48
    Cytogenetic map
    Sequence location
    FlyBase Computed Cytological Location
    Cytogenetic map
    Evidence for location
    85B7-85B7
    Limits computationally determined from genome sequence between P{lacW}l(3)L4740L4740 and P{EP}D1EP473
    Experimentally Determined Cytological Location
    Cytogenetic map
    Notes
    References
    85B-85B
    (determined by in situ hybridisation)
    Experimentally Determined Recombination Data
    Left of (cM)
    Right of (cM)
    Notes
    Stocks and Reagents
    Stocks (22)
    Genomic Clones (20)
    cDNA Clones (110)
     

    Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see JBrowse for alignment of the cDNAs and ESTs to the gene model.

    cDNA clones, fully sequenced
    BDGP DGC clones
    Other clones
      Drosophila Genomics Resource Center cDNA clones

      For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.

      cDNA Clones, End Sequenced (ESTs)
      RNAi and Array Information
      Linkouts
      DRSC - Results frm RNAi screens
      Antibody Information
      Laboratory Generated Antibodies
      Commercially Available Antibodies
       
      Cell Line Information
      Publicly Available Cell Lines
       
        Other Stable Cell Lines
         
          Other Comments

          osk RNA dimerization loop base-pairing promotes co-assembly of RNA molecules. The presence of a palindromic sequence in the dimerization loop is not essential for posterior localization of full-length spliced RNA molecules.

          osk RNA dimerizes through kissing-loop interactions.

          osk RNA is transported as particles from nurse cells to the oocyte by a Dhc64C/BicD dependent mechanism distinct from the general flow of cytoplasm from nurse cell to oocyte.

          osk has a role in early oogenesis, but this role is mediated by osk RNA, not osk protein.

          Splicing of the osk first intron is required for posterior localization of osk transcript in the oocyte.

          osk has a role in long-term memory.

          Identification: in a germline clone screen for mutants that are defective in localisation of an Avic\GFP-stau marker in living oocytes. 2 alleles of osk have been identified in the screen.

          orb is required for osk protein expression in oocytes.

          In ovaries mutant for hypomorphic alleles of Rbp9, osk mRNA localization is aberrant in the developing egg chamber.

          Translation of localised osk mRNA is activated specifically through a discrete element located at the 5' end of the osk transcript. This element is only active at the posterior pole of the embryo and is only required when the transcript is repressed through the Bruno-response element (BRE), suggesting that it functions as a derepressor.

          In a sample of 79 genes with multiple introns, 33 showed significant heterogeneity in G+C content among introns of the same gene and significant positive correspondence between the intron and the third codon position G+C content within genes. These results are consistent with selection adding against preferred codons at the start of genes.

          Studies of fluorescently labelled osk RNA injected into wild type or mutant embryos reveal that microtubule-dependent cytoplasmic flows could contribute to the long range transport of osk RNA, whereas microtubule independent processes could mediate short-range transport.

          Results propose than an osk-vas complex stimulates transcription of osk and speculate that phosphorylation of short osk acts in the spatial restriction of osk translation to the posterior pole.

          osk, stau, vas and tud are essential for pole plasm formation. osk RNA localises to the posterior pole of the oocyte.

          Transport and early localisation activities of fs(1)K10, bcd and osk mRNAs are remarkably similar to each other suggesting the mRNAs interact with a common set of microtubule based motor proteins and associated factors.

          Mutants in chic resemble those in capu in that they fail to localize stau protein and osk mRNA to the posterior pole of the developing oocyte.

          aub is required to enhance osk translation, acting through the osk 3'UTR and sequences upstream of the 3'UTR.

          Mutations in Tm1 virtually abolish osk RNA localisation to the posterior pole suggesting an involvement of the actin network in osk RNA localisation.

          Early ph-p gene expression is under the control of bcd and en as activators and of osk as an inhibitor.

          Nurse cell-specific genes are functional in the pseudonurse cells of otu mutants, but the transport of pum, otu, ovo and bcd RNAs to the cytoplasm is affected.

          One readily detectable protein with an apparent molecular weight of 80kD binds specifically to the nos mRNA 3' untranslated region (3'UTR), the protein is called aret. Binding assays demonstrate aret response elements (BRE) exist in the A, B and C region of osk 3' UTR. aret is required for preventing translation of osk mRNA prior to its localisation at the posterior pole of the oocyte.

          Contrary to a previous report (FBrf0072967), localization of mt:lrRNA depends on osk function even at the anterior pole.

          Targeting of osk to the posterior pole involves two steps of spatial restriction, cytoskeleton-dependent localisation of the mRNA and localisation-dependent translation. Two isoforms of osk protein are produced by alternative start codon usage, the short isoform has full osk activity. When osk RNA is localised accumulation of osk protein requires the functions of vas and tud, as well as osk itself, suggesting a positive feedback mechanism in the induction of pole plasm by osk.

          Microtubules are required for osk mRNA localisation in nurse cells and in the posterior oocyte.

          Gene functions that are not required for the localisation of osk RNA affect the stability or perhaps translational initiation of osk protein. The osk 3'UTR can confer translational repression on a heterologous coding sequence and results suggest that osk RNA localisation is regulated by osk translation and the mechanism responsible operates through the osk 3' UTR. Full length osk protein functions to maintain osk RNA localisation and therefore support a positive feedback model.

          The stau product associates specifically with both osk and bcd mRNAs to mediate their localizations, but at two distinct stages of development. stau protein is required to anchor bcd mRNA at the anterior of the egg, and is transported with osk mRNA during oogenesis.

          Mutations of Pka-C1 cause similar mislocalisations of bcd and osk RNAs to those observed from N mutations. Mutations also severely disrupt the organisation of microtubules at the posterior of the oocyte at the time of bcd and osk localisation.

          Comparisons of early development to that in other insects have revealed conservation of some aspects of development, as well as differences that may explain variations in early patterning events.

          A PCR based assay has been used to determine whether the encoded mRNAs exhibit changes in poly(A) status upon translational activation.

          Dvir\osk transgenes direct body patterning but not pole cell formation or maintenance of mRNA in D.melanogaster.

          Distribution of tud protein in mutant embryos has been studied.

          Different elements within the osk 3' untranslated region are necessary for distinct steps in the mRNA localization process: early movement into the oocyte, accumulation at the anterior margin of the oocyte, and localization to the posterior pole.

          The role of osk in the regulation of run mRNA expression in the early embryo has been investigated.

          The localization of the osk RNA and stau protein in oogenesis do not depend of the product of the psq locus.

          Oocyte-specific accumulation of osk, CycB and 65F mRNAs is blocked by microtubule assembly inhibitors.

          Mislocalisation of osk mRNA to the anterior of the oocyte is sufficient to direct formation of an abdomen and of functional germ cells at an ectopic site. Only vas and tud are essential for osk-induced pole cell and abdomen formation. The dosage of osk determines the final amount of components recruited and ultimately controls the number of pole cells formed.

          Overexpression of osk leads to higher levels of osk mRNA that is both correctly localised to the posterior pole and unlocalised. Consequently nos is activated ectopically causing extensive shifts in body patterning. Germ cell formation is also affected, this can be enhanced by genetically decreasing nos activity.

          osk is required for the correct positioning of nos product in the embryo.

          Cloning and molecular characterization of osk reveals that osk mRNA is concentrated in the oocyte throughout most of oogenesis and it is specifically localized to the posterior pole soon after the oocyte begins to visibly differentiate. Full length or nearly full length osk protein is required to maintain the posterior localization of osk mRNA.

          osk is required for the localization of the posterior signal.

          Mutations in maternal anterior class gene osk do not interact with RpII140wimp.

          osk expression patterns were investigated in egl embryos to determine the relationship between osk and egl.

          Mature follicles are immunologically stained for asymmetric distribution of ecdysteroid-related antigen. During late oogenesis localisation of the antigen changes dramatically suggesting the antigen plays a role in early embryogenesis and, perhaps, in pattern formation.

          In osk mutant females vas synthesis appears normal but the vas protein is not localized.

          osk plays a role in polar granule formation.

          An investigation of the role of gap genes in expression from Ubx and Antp promoters in the blastoderm embryo reveals that a unique combination of gap genes and pair rule genes is required for their initial activation.

          Homozygous females normally viable and fecund; homozygous males fertile. Embryos produced by homozygous females lack pole plasm and fail to produce pole cells; abdominal region remains unsegmented and eventually dies. Temperature-sensitive period for the germ-line effect is the last six hours of oogenesis and for abdominal development the last twelve to fourteen hours (osk8). Homozygous osk germ cells autonomous in pole cell transplants. Polar cytoplasm from unfertilized eggs or normal embryos capable of rescuing pole cell formation if injected at the posterior extremity of the early embryo and abdominal segmentation, to the extent of producing viable but sterile adults, if injected into the posterior half of preblastoderm embryos. Embryos produced by homozygous BicD; osk females are indistinguishable from those produced by osk alone suggesting that osk+ product is required for the formation of bicaudal embryos; also required for the early anterior-posterior gradient of hb expression (Tautz, 1988).

          Relationship to Other Genes
          Source for database merge of
          Additional comments
          Nomenclature History
          Source for database identify of
          Nomenclature comments
          Etymology
          Synonyms and Secondary IDs (9)
          Reported As
          Symbol Synonym
          osk
          (Baumgartner, 2024, Siddiqui et al., 2024, Weng et al., 2024, Beuchle et al., 2023.6.30, Curnutte et al., 2023, Eichler et al., 2023, Gáspár et al., 2023, Kara et al., 2023, Lu and Gelfand, 2023, Pang et al., 2023, Bose et al., 2022, Cassella and Ephrussi, 2022, Colonnetta et al., 2022, Eickelberg et al., 2022, Gupta et al., 2022, Valentino et al., 2022, Doherty et al., 2021, Ghotbi et al., 2021, Mukherjee and Mukherjee, 2021, Neiswender et al., 2021, Tanaka et al., 2021, Bono, 2020.3.10, Dold et al., 2020, Eichler et al., 2020, Hinnant et al., 2020, Lasko, 2020, Lee et al., 2020, Lu et al., 2020, McCambridge et al., 2020, Sankaranarayanan and Weil, 2020, Senthilkumar et al., 2020, Soluri et al., 2020, Stathopoulos and Newcomb, 2020, Barr et al., 2019, Barr et al., 2019, Goldman et al., 2019, Park et al., 2019, Trcek and Lehmann, 2019, Whittle and Extavour, 2019, Alhaj Abed et al., 2018, Flora et al., 2018, Gaspar et al., 2018, Kelleher et al., 2018, Lu et al., 2018, Niepielko et al., 2018, Wang et al., 2018, Dufourt et al., 2017, Gáspár et al., 2017, Goldman and Gonsalvez, 2017, Hamada-Kawaguchi and Yamamoto, 2017, Hu et al., 2017.6.13, Nieuwburg et al., 2017, Panchal et al., 2017, Vazquez-Pianzola et al., 2017, Voelzmann et al., 2017, Catrina et al., 2016, Clandinin and Owens, 2016-, Hurd et al., 2016, Lazzaretti et al., 2016, Lim et al., 2016, Macdonald et al., 2016, Na et al., 2016, Quinlan, 2016, Sanghavi et al., 2016, Sarov et al., 2016, Schwartz et al., 2016, Trovisco et al., 2016, Vourekas et al., 2016, Barckmann et al., 2015, Bor et al., 2015, Halstead et al., 2015, Jambor et al., 2015, Jones and Macdonald, 2015, Kanke and Macdonald, 2015, Kanke et al., 2015, Kim et al., 2015, Little et al., 2015, Liu et al., 2015, Rojas-Ríos et al., 2015, Ryu and Macdonald, 2015, Trcek et al., 2015, Wang et al., 2015, Gaspar et al., 2014, Ghosh et al., 2014, Guilgur et al., 2014, Hövelmann et al., 2014, Huylmans and Parsch, 2014, Jambor et al., 2014, Morais-de-Sá et al., 2014, Olesnicky et al., 2014, Sitaram et al., 2014, Tsai et al., 2014, Vazquez-Pianzola et al., 2014, Williams et al., 2014, Joly et al., 2013, Leibfried et al., 2013, McDermott and Davis, 2013, Morais-de-Sá et al., 2013, Saunders et al., 2013, Webber et al., 2013, Baffet et al., 2012, El-Sherif et al., 2012, Ghosh et al., 2012, Jansen and Niessing, 2012, Japanese National Institute of Genetics, 2012.5.21, McDermott et al., 2012, Sanghavi et al., 2012, Sano et al., 2012, Siddiqui et al., 2012, Vazquez-Pianzola and Suter, 2012, Xu and Gridley, 2012, Bader et al., 2011, Becalska et al., 2011, Chang et al., 2011, Dubin-Bar et al., 2011, Fan et al., 2011, Jambor et al., 2011, Jeske et al., 2011, Lerit and Gavis, 2011, Moua et al., 2011, Pruteanu-Malinici et al., 2011, Reveal et al., 2011, Shimada et al., 2011, Sinsimer et al., 2011, Smith et al., 2011, Sun et al., 2011, Tanaka and Nakamura, 2011, Tanaka et al., 2011, Vazquez-Pianzola et al., 2011, Wong et al., 2011, Yarunin et al., 2011, Anne, 2010, Anne, 2010, Anne, 2010, Becalska and Gavis, 2010, Cook et al., 2010.2.12, Doerflinger et al., 2010, Duchi et al., 2010, Fernández-Ayala et al., 2010, Kim et al., 2010, Patil and Kai, 2010, Reveal et al., 2010, Rouget et al., 2010, Casper and Van Doren, 2009, Kalifa et al., 2009, Lyon et al., 2009, McNeil et al., 2009, Mhlanga et al., 2009, Moore et al., 2009, Navarro et al., 2009, Rangan et al., 2009, Reich et al., 2009, Snee and Macdonald, 2009, Benoit et al., 2008, Christensen et al., 2008.4.15, Gervais et al., 2008, Haussmann et al., 2008, Hong et al., 2008, Jain and Gavis, 2008, Li et al., 2008, Meignin and Davis, 2008, Reveal and Macdonald, 2008, Snee et al., 2008, Tanaka and Nakamura, 2008, Technau and Roth, 2008, Tian and Deng, 2008, Voog et al., 2008, Xi et al., 2008, Zimyanin et al., 2008, Anne et al., 2007, Arama et al., 2007, Chicoine et al., 2007, Clark et al., 2007, Coutelis and Ephrussi, 2007, Dahlgaard et al., 2007, Geng and MacDonald, 2007, Jones and Macdonald, 2007, Kadyrova et al., 2007, Kitadate et al., 2007, Klattenhoff et al., 2007, Lecuyer et al., 2007, Lim and Kai, 2007, Meignin et al., 2007, Mukai et al., 2007, Peretz et al., 2007, Polesello and Tapon, 2007, Serbus and Sullivan, 2007, Stevens et al., 2007, Wang and Lin, 2007, Weiler, 2007, Zimyanin et al., 2007, Zimyanin et al., 2007, Beckett and Baylies, 2006, Chekulaeva et al., 2006, Doerflinger et al., 2006, Geng and Macdonald, 2006, Gilboa and Lehmann, 2006, Januschke et al., 2006, Jenny et al., 2006, Kalifa et al., 2006, Le Bras and Van Doren, 2006, Lin et al., 2006, Megosh et al., 2006, Munro et al., 2006, Vogt et al., 2006, Zaessinger et al., 2006, Hayashi et al., 2005, Norvell et al., 2005, Van De Bor et al., 2005, Motola and Neuman-Silberberg, 2004, Snee and Macdonald, 2004, Fouix et al., 2003, Lee et al., 2001, Leemans et al., 2001, Smibert et al., 1999, Wang et al., 1994)
          Name Synonyms
          oskar
          (Milas et al., 2023, St Johnston, 2023, Verma et al., 2023, Wippich et al., 2023, Colonnetta et al., 2022, Doerflinger et al., 2022, Kemph and Lynch, 2022, Kimble and Nüsslein-Volhard, 2022, Milas and Telley, 2022, Senthil Kumar et al., 2022, Blondel et al., 2021, Merkle et al., 2020, Hampoelz et al., 2019, Obrdlik et al., 2019, Schüpbach, 2019, Gaspar et al., 2018, Bilinski et al., 2017, Broyer et al., 2017, Goldman and Gonsalvez, 2017, Lakhotia, 2017, Nieuwburg et al., 2017, Aram et al., 2016, Barr et al., 2016, Ma et al., 2016, Nashchekin et al., 2016, Wen et al., 2016, Davis, 2015, Jones and Macdonald, 2015, Kanke and Macdonald, 2015, Cantera et al., 2014, Hövelmann et al., 2014, Cui et al., 2013, Hövelmann et al., 2013, Laver et al., 2013, McDermott and Davis, 2013, Seervai and Wessel, 2013, Bozzetti et al., 2012, Catrina et al., 2012, Ganguly et al., 2012, Ghosh et al., 2012, Gonsalvez and Long, 2012, Jansen and Niessing, 2012, McCue and Slotkin, 2012, Vazquez-Pianzola and Suter, 2012, Xu and Gridley, 2012, Chang et al., 2011, Findeiß et al., 2011, Jaglarz et al., 2011, Jambor et al., 2011, Jeske et al., 2011, Sinsimer et al., 2011, Sun et al., 2011, Vazquez-Pianzola et al., 2011, Wong et al., 2011, Yarunin et al., 2011, Bader et al., 2010, Becalska and Gavis, 2010, Duchi et al., 2010, Gonsalvez et al., 2010, Herpers et al., 2010, Kim et al., 2010, Lan et al., 2010, Loiseau et al., 2010, Patil and Kai, 2010, Quinones et al., 2010, Reveal et al., 2010, Rouget et al., 2010, Besse et al., 2009, Casper and Van Doren, 2009, Fang et al., 2009, Kalifa et al., 2009, Krauss et al., 2009, Lyon et al., 2009, McNeil et al., 2009, Mhlanga et al., 2009, Rangan et al., 2009, Snee and Macdonald, 2009, Suyama et al., 2009, Tian and Deng, 2009, Berger et al., 2008, Besse et al., 2008, Bushati et al., 2008, Gervais et al., 2008, Ghosh et al., 2008, Hong et al., 2008, Hong et al., 2008, Li et al., 2008, Lin et al., 2008, Lin et al., 2008, Meignin and Davis, 2008, Reich et al., 2008, Snee et al., 2008, Sung et al., 2008, Technau and Roth, 2008, Tian and Deng, 2008, Voog et al., 2008, Zimyanin et al., 2008, Arama et al., 2007, Dahlgaard et al., 2007, Goldman et al., 2007, Ho and Gavis, 2007, Jambor et al., 2007, Kugler and Lasko, 2007, Meignin et al., 2007, Polesello and Tapon, 2007, Snee et al., 2007, Stevens et al., 2007, Tadros et al., 2007, Vanzo et al., 2007, Wang and Lin, 2007, Bergmann, 2006, Denman, 2006, Geng and Macdonald, 2006, Gilboa and Lehmann, 2006, Irion et al., 2006, Januschke et al., 2006, Kerkhoff, 2006, Kiebler and Bassell, 2006, Kozak, 2006, Le Bras and Van Doren, 2006, Lin et al., 2006, Munro et al., 2006, Perkins et al., 2006, Shapiro and Anderson, 2006, Verdier et al., 2006, Benoit et al., 2005, Shav-Tal and Singer, 2005, Wilhelm et al., 2005, Motola and Neuman-Silberberg, 2004, Lee et al., 2001, Leemans et al., 2001, Shimell et al., 2000, Smibert et al., 1999, Miedema et al., 1995)
          Secondary FlyBase IDs
            Datasets (0)
            Study focus (0)
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            Project
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            Result
            Result Type
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            External Crossreferences and Linkouts ( 54 )
            Sequence Crossreferences
            NCBI Gene - Gene integrates information from a wide range of species. A record may include nomenclature, Reference Sequences (RefSeqs), maps, pathways, variations, phenotypes, and links to genome-, phenotype-, and locus-specific resources worldwide.
            GenBank Nucleotide - A collection of sequences from several sources, including GenBank, RefSeq, TPA, and PDB.
            GenBank Protein - A collection of sequences from several sources, including translations from annotated coding regions in GenBank, RefSeq and TPA, as well as records from SwissProt, PIR, PRF, and PDB.
            RefSeq - A comprehensive, integrated, non-redundant, well-annotated set of reference sequences including genomic, transcript, and protein.
            UniProt/GCRP - The gene-centric reference proteome (GCRP) provides a 1:1 mapping between genes and UniProt accessions in which a single 'canonical' isoform represents the product(s) of each protein-coding gene.
            UniProt/Swiss-Prot - Manually annotated and reviewed records of protein sequence and functional information
            Other crossreferences
            AlphaFold DB - AlphaFold provides open access to protein structure predictions for the human proteome and other key proteins of interest, to accelerate scientific research.
            BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
            DRscDB - A single-cell RNA-seq resource for data mining and data comparison across species
            EMBL-EBI Single Cell Expression Atlas - Single cell expression across species
            FlyAtlas2 - A Drosophila melanogaster expression atlas with RNA-Seq, miRNA-Seq and sex-specific data
            FlyMine - An integrated database for Drosophila genomics
            InterPro - A database of protein families, domains and functional sites
            KEGG Genes - Molecular building blocks of life in the genomic space.
            MARRVEL_MODEL - MARRVEL (model organism gene)
            PDB - An information portal to biological macromolecular structures
            Linkouts
            BioGRID - A database of protein and genetic interactions.
            Drosophila Genomics Resource Center - Drosophila Genomics Resource Center (DGRC) cDNA clones
            DroID - A comprehensive database of gene and protein interactions.
            DRSC - Results frm RNAi screens
            Eukaryotic Promoter Database - A collection of databases of experimentally validated promoters for selected model organisms.
            FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
            FlyCyc Genes - Genes from a BioCyc PGDB for Dmel
            Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
            Flygut - An atlas of the Drosophila adult midgut
            Interactive Fly - A cyberspace guide to Drosophila development and metazoan evolution
            MIST (genetic) - An integrated Molecular Interaction Database
            MIST (protein-protein) - An integrated Molecular Interaction Database
            References (989)