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RANBP3 Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF- beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export. Interacts with CHC1 in a Ran-stimulated manner. Interacts with XPO1. Interacts (via its C-terminal R domain) with SMAD2 (dephosphorylated form via its MH1 and MH2 domains); the interaction results in the nuclear export of SMAD2 and termination of the TGF-beta signaling. Interacts (via its C-terminal R domain) with SMAD3 (dephosphorylated form via its MH1 domain); the interaction results in the nuclear export of SMAD3 and termination of the TGF-beta signaling. Widely expressed with high levels in testis and heart. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Adaptor/scaffold
Chromosomal Location of Human Ortholog: 19p13.3
Cellular Component: centrosome; cytoplasm; nucleoplasm; nucleus
Molecular Function: GTPase activator activity; protein binding; Ran GTPase binding
Biological Process: G1/S transition of mitotic cell cycle; positive regulation of mitotic centrosome separation; protein import into nucleus; RNA export from nucleus; spindle organization and biogenesis; ubiquitin-dependent protein catabolic process
Reference #:  Q9H6Z4 (UniProtKB)
Alt. Names/Synonyms: DKFZp586I1520; RAN binding protein 3; Ran-binding protein 3; RAN-binding protein-3; RANB3; RANBP3
Gene Symbols: RANBP3
Molecular weight: 60,210 Da
Basal Isoelectric point: 4.7  Predict pI for various phosphorylation states
CST Pathways:  Growth And Differentiation Control by MAPKs
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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