National and Kapodistrian University of Athens
Department of Biology
Biophysics & Bioinformatics Laboratory
Protein Information |
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| Protein Name | Nucleoprotein TPR |
| Accession Code | A1Z8P9 |
| Gene | Mtor |
| Organism | Drosophila melanogaster (Taxonomy: 7227) |
| Part of Reference Proteome? | Yes |
| Sequence (Length: 2346) |
Description |
Position in the Nuclear Envelope |
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| Location | Location ID | Description |
| Nuclear Envelope | SL-0178 | The nuclear envelope is a membrane system which surrounds the nucleoplasm of eukaryotic cells. It is composed of the nuclear lamina, nuclear pore complexes and two nuclear membranes. The space between the two membranes is called the nuclear intermembrane space. |
| Nuclear Lamina | SL-0180 | The nuclear lamina is a meshwork of intermediate filament proteins called lamins and lamin-binding proteins that are embedded in the inner nuclear membrane. |
| Nuclear Membrane | SL-0182 | The membrane surrounding the nucleus. This term is used when it is not known if the protein is found in or associated with the inner or outer nuclear membrane. |
| Nuclear Pore Complex | SL-0185 | The nuclear pore complex (NPC) constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active bidirectional transport of macromolecules such as proteins, RNAs etc across the double-membrane nuclear envelope.The NPC is composed of at least 30 distinct subunits known as Nucleoporins (NUPs). | Membrane Topology |
| Topology | Source | Annotation Type |
| Peripheral | UniProt | Curator Inference {ECO:0000305} | Assigned Ontology terms |
Description |
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| Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope (PubMed:9152019). Functions as a scaffolding element in the nuclear phase of the NPC (PubMed:12027452, PubMed:15356261). Plays a role in chromosomal organization and gene expression regulation; stimulates transcription by promoting the formation of an open chromatin environment (PubMed:12027452, PubMed:20174442). Binds chromatin to nucleoporin-associated regions (NARs) that define transcriptionally active regions of the genome (PubMed:20174442). Associates with extended chromosomal regions that alternate between domains of high density binding with those of low occupancy (PubMed:20174442). Preferentially binds to NARs of the male X chromosome (PubMed:20174442). In males, together with Nup153, required for the localization of the male-specific lethal (MSL) histone acetyltransferase complex to the X chromosome and therefore for the transcription of dosage compensation genes (PubMed:16543150). In males, restrains dosage-compensated expression at the level of nascent transcription probably by interacting with the MSL complex and by modulating RNA Polymerase II phosphorylation status and activity (PubMed:34133927). During mitosis forms a gel-like spindle matrix complex together with Skeletor, Chro, east, and Asator embedding the microtubule spindle apparatus (PubMed:15356261, PubMed:15962301, PubMed:19273613, PubMed:22855526). During interphase localizes Mad1 to the nuclear pore complex and thereby might act as a scaffold to assemble the Mad1-C-Mad2 complex, an heterotetramer that catalyzes the structural conversion of open-Mad2 (O-Mad2) into closed-Mad2 (C-Mad2) which is essential for spindle-assembly checkpoint (SAC) (PubMed:31913420). During the metaphase-anaphase transition and before chromosome congression, is phosphorylated by Msp-1; this modification releases Mad1 from the nuclear pore complex and thereby promotes assembly of SAC ensuring a timely and effective recruitment of spindle checkpoint proteins like Mad1, Mad2 and Mps1 to unattached kinetochores (KT) (PubMed:22855526, PubMed:26714316, PubMed:31913420). In testes, has a role in stem cell asymmetric division and maintenance via regulation of mitotic spindle assembly checkpoint (SAC) complex (PubMed:26714316). {Experimental EvidencePubMed:12027452, Experimental EvidencePubMed:15356261, Experimental EvidencePubMed:15962301, Experimental EvidencePubMed:16543150, Experimental EvidencePubMed:19273613, Experimental EvidencePubMed:20174442, Experimental EvidencePubMed:22855526, Experimental EvidencePubMed:26714316, Experimental EvidencePubMed:31913420, Experimental EvidencePubMed:34133927, Experimental EvidencePubMed:9152019}. | Assigned Ontology terms |
Interactions with other proteins (17 interactors) |
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National and Kapodistrian University of Athens
Department of Biology
Biophysics & Bioinformatics Laboratory