PTB, polypyrimidine tract-binding protein, l(3)03429, ema, dmPTB
polypyrimidine tract binding protein - controls alternative splicing - required to attenuate Notch activity after ligand-dependent activation during wing development - functions in male germline
Gene model reviewed during 5.53
Low-frequency RNA-Seq exon junction(s) not annotated.
Annotated transcripts do not represent all possible combinations of alternative exons and/or alternative promoters.
Annotated transcripts do not represent all supported alternative splices within 5' UTR.
Stage-specific extension of 3' UTRs observed during embryogenesis (FBrf0215804); all variants may not be annotated.
Gene model reviewed during 5.46
Gene model reviewed during 5.56
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\heph using the Feature Mapper tool.
heph is predominantly expressed in the nuclei of primary spermatocytes in males
heph accumulates in the cytoplasm in the germrium. It accumulates transiently in the center of the oocytes in stages S7,8 and is localized to the posterior pole of the oocyted from stage S9 onward suggesting that it is transported with Oskar mRNA to the pole. heph is expressed both in the germline and in the somatic epithelium.
GBrowse - Visual display of RNA-Seq signalsView Dmel\heph in GBrowse 2
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
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 GBrowse for alignment of the cDNAs and ESTs to the gene model.
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.
Source for identity of: ema l(3)03429
heph function is essential for spermatogenesis during spermatid differentiation.
Postmeiotic differentiation defect.