SRp55, RRM8, SR55, E(Dfd), l(3)s2249
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.
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.47
1.6 (northern blot)
Extensively phosphorylated on serine residues in the RS domain.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\B52 using the Feature Mapper tool.
Isoform-specific expression patterns are observed. Sex-specific expression of alternative transcripts observed.
Antibodies against B52 protein show that it is associated with regions of transcriptionally active chromatin in unstressed and heat shocked animals. It colocalizes with RNA polymerase II but its region of staining brackets the RNA polymerase II signal symmetrically. UV crosslinking studies show that B52 protein is also associated with boundaries of transcriptionally active chromatin on nonpolytene chromosomes.
GBrowse - Visual display of RNA-Seq signalsView Dmel\B52 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.
Expression is enriched in embryonic gonads.
B52 is referred to as E(Dfd) in FBrf0068180, the motivation behind E(Dfd) was that it was a bit more interesting than B52 and made reference to a phenotype. In subsequent publications B52 is used in favor of consistent nomenclature.
Both RNA recognition motifs of B52 are required for RNA binding, while the arginine-serine rich domain is not involved in this interaction.
The distribution of B52 protein at heat-shock loci depends on transcription levels.
In many cell types increasing the concentration of B52 adversely affects the development of the organism.
B52 is widely expressed throughout development. B52 accumulates in ovaries where it is packaged into the developing egg and is localised to nuclei by the late blastoderm stage of embryonic development.
A sequence comparison and numerical analysis of the RRM-containing (RNA recognition motif) proteins suggests that functionally related RRM-containing proteins have significant sequence similarities in their RRMs.
Identified in an in vitro system as a splicing factor present at low levels in the dsx female-specific splicing complex.
Encodes a nuclear phosphoprotein, the protein contains an RS domain common to several proteins known to be involved in RNA splicing.
Involved in pre-mRNA splicing.
Immunofluorescence of polytene chromosomes reveals the chromatin distribution of the B52 product.