RANBP9
Domain
The SPRY domain mediates the interaction with MET, AR, and CDC2L1.
Function
May act as scaffolding protein, and as adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Acts as a mediator of cell spreading and actin cytoskeleton rearrangement (PubMed:18710924). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). May be involved in signaling of ITGB2/LFA-1 and other integrins (PubMed:14722085). Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway (PubMed:12147692). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation (PubMed:12361945, PubMed:18222118). Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity (PubMed:15558019). Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA.
Post-translational modifications
Phosphorylated in response to stress. Can be phosphorylated by the cleaved p110 form of CDC2L1 (p110C).
Ubiquitinated. Polyubiquitination targets the protein for rapid degradation via the ubiquitin system. Can be deubiquitinated by USP11.
Sequence Similarities
Belongs to the RANBP9/10 family.
Tissue Specificity
Ubiquitously expressed, with highest levels in testes, placenta, heart, and muscle, and lowest levels in lung. Within the brain, expressed predominantly by neurons in the gray matter of cortex, the granular layer of cerebellum and the Purkinje cells.
Cellular localization
- Cytoplasm
- Nucleus
- Cell membrane
- Peripheral membrane protein
- The unphosphorylated form is predominantly cytoplasmic. A phosphorylated form is associated with the plasma membrane.
Alternative names
RANBPM, RANBP9, Ran-binding protein 9, RanBP9, BPM-L, BPM90, Ran-binding protein M, RanBP7, RanBPM