gene_with_dicistronic_mRNA ; SO:0000722
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.46
Gene model reviewed during 5.56
Multiphase exon postulated: this gene shares a region of coding sequence with an overlapping gene, but different reading frames are utilized in the overlapping coding region.
1312 (aa); 180, 150, 110, 45 (kD observed); 130 (kD predicted)
Component of the osk RNP complex, which is composed of at least exu, yps, aret/bruno, cup, and the mRNA of osk (PubMed:10662770). Interacts with the decapping activators me31B and tral (PubMed:21937713). Component of the nos RNP complex, which is composed of at least smg, cup, tral, me31B, the CCR4-NOT complex members Rga/NOT2 and Caf1, and the mRNA of nos (PubMed:21081899). Interacts with btz (PubMed:14691132, PubMed:14723848). Recruited to the 3'-UTR of nos and osk mRNAs by smg and btz, respectively (PubMed:14685270, PubMed:14691132). Forms a ribonucleoprotein complex (RNP) containing at least me31B, eIF4E1, cup, tral and pAbp; this interaction is required for the translational silencing of maternal mRNAs during the maternal-to-zygotic transition (PubMed:28875934). No interaction was detected with pAbp in 1-5 hour embryos (PubMed:28875934). Interacts with osk and vas (PubMed:22454519). Interacts with Pop2, twin/CCR4, Rga, Not3 and Not1 which are all core components of the CCR4-NOT deadenylase complex; interaction with the complex is required for cup deadenylation activity (PubMed:21937713). Interacts with nos (PubMed:11060247). Interacts with smg (PubMed:14685270). Interacts with eIF4E1; the interaction promotes retention of cup in the cytoplasm (PubMed:14723848, PubMed:14685270, PubMed:15465908, PubMed:21937713). Interacts with orb; the interaction represses the orb positive autoregulatory loop (PubMed:22164257). Interacts with Nup154 (PubMed:17277377).
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\cup using the Feature Mapper tool.
cup protein colocalizes with Hsp83 protein in the cytoplasm of germline stem cells in region 1, is nearly absent in the anterior of region 2 (cystoblast cleavage stage), but rises to high levels in the posterior part of region 2, and in the maturing germline cysts of region 3. cup protein is accumulates at the posterior cytoplasm of oocytes up to oogenesis stage 8; around nurse cell nuclei in early egg chambers, and in nurse cell cytoplasm.
cup protein is uniform and abundant in the cytoplasm of all cleavage stage embryos up through stage 9. In the ovary, cup protein is found in the cytoplasm of all germ-line cells. It accumulates preferentially in the future oocyte as early as germarium stage 2a. It continues to be selectively enriched in the oocyte until stage S8. During stage S9, the nurse cells and oocyte contain similar amounts of cup protein and by stage S10, it is localized preferentially in the nurse cells. Within the nurse cells, cup protein accumulates in large aggregates whose location varies as egg chambers develop.
GBrowse - Visual display of RNA-Seq signalsView Dmel\cup 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: cup CG11181
Cell-free assays indicate that the cup protein represses osk translation by binding to the eIF-4E cap-binding protein and recruiting the aret protein, thus preventing recruitment of the small ribosomal subunit.
cup is continuously required for maintenance of nurse cell chromosome structure.
Mutaions at the cup locus cause defects in midoogenesis.