Sep1, septin, iby, dSEPT1
Gene model reviewed during 5.53
Gene model reviewed during 5.48
Gene model reviewed during 5.55
There is only one protein coding transcript and one polypeptide associated with this gene
Ubiquitinated by park, leading to its degradation by the proteasome.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Septin1 using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\Septin1 in GBrowse 2
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.
Shows particularly robust cycling of transcription in adult heads, as assessed by expression analysis using high density oligonucleotide arrays with probe generated during three 12-point time course experiments over the course of 6 days.
A complex of septin polypeptides is isolated that bind and hydrolyse GTP and form filaments. Their high degree of conservation, ubiquitous expression and proven role in cytokinesis suggests septins are certain to be important players in regulating cell architecture and function. Septins alone can form regular filamentous polymers, since filament formation is likely to be central to their localisation and function.
Sep1 localises to the leading edge of the cleavage furrows in dividing cells and in cellularising embryos. Sep1 is also concentrated in other locations that suggest additional roles unrelated to cytokinesis. Immunolocalisation and biochemical data suggest that Sep1 and pnut probably function as parts of a complex.