Browse our anti-RAN Binding Protein 2 (RANBP2) Antibodies

Human RAN Binding Protein 2 (RANBP2) interaction partners

1. We describe three in vitro reconstituted disassembly intermediates, which show binding of a Crm1 export complex via two FG-repeat patches, cargo-release by RanBP2's Ran-binding domains and retention of free Crm1 at RanBP2 after Ran-GTP hydrolysis.

2. RAN binding protein 2 increase the sumoylation of cyclin-dependent kinase inhibitor 1B in cholangiocarcinoma cell line QBC939.

3. Importin-beta and CRM1 control a RANBP2 spatiotemporal switch essential for mitotic kinetochore function.

4. Translocation of p53 is regulated by androgen-dependent sumoylation mediated by the G3BP2-interacting SUMO-E3 ligase, RanBP2. G3BP2 knockdown results in reduced tumor growth and increased nuclear p53 accumulation in mouse xenograft models of prostate cancer with or without long-term androgen deprivation.

5. These our results reveal spatio-temporal regulation in the recruitment of nucleoporins and translation factors to cytoplasmic viral factories , and particularly the importance of Nup358 in vaccinia virus infection.

6. NUSAP1 contributes to accurate chromosome segregation by acting as a co-factor for RanBP2-RanGAP1-UBC9 during cell division.

7. Nup358-AGO interaction is important for miRNA-mediated gene silencing and identifies SIM as a new interacting motif for the AGO family of proteins.

8. recurrent or familial ANE without the RANBP2 mutation has a more severe outcome and greater predilection for male sex than that with the RANBP2 mutation. This suggests that there are unknown gene mutations linked to ANE.

9. Based on the literature review of ANE1 with RANBP2 mutation, we propose a threshold for RANBP2 mutation tes

10. findings indicate that RanGDP and not RanGTP is the physiological target for the RanBP2 SUMO E3 ligase complex

11. Taken together, topographic and functional interactions between dynactin, importin-beta and RanBP2 are involved in nuclear translocation of IGF-1R.

12. analysis of the RANBP2-ALK gene fusion identified in ALK-positive diffuse large B-cell lymphoma with a unique nuclear membrane staining of ALK protein

13. Nup358, a nucleoporin that forms the cytoplasmic filaments of the nuclear pore complex, plays an important role in the nuclear import of hTERT.

14. Our data show that Nup358 supports nuclear transport functions important for cellular homeostasis and for HIV-1 nuclear import

15. Case Report/Review: RANBP2-ALK gene rearrangement in inflammatory myofibroblastic tumors.

16. RANBP2-ALK fusion combined with monosomy 7 may be related to a unique clonal hematologic disorder of childhood and adolescence, characterized by myelomonocytic leukemia and a poor prognosis [case report/ review]

17. Mitotic arrest and the following cell death were caused by depletion of RanBP2.

18. Isomerization by NUP358 may be preserved by HIV-1 to target the nuclear pore and synchronize nuclear entry with capsid uncoating.

19. The translation of a subset of mRNAs encoding secretory proteins is potentiated by RanBP2.

20. These findings reveal novel roles of Ranbp2 in the modulation of intrinsic and extrinsic cell death mechanisms and pathways

Cow (Bovine) RAN Binding Protein 2 (RANBP2) interaction partners

1. reports identification of the cyclophilin-related protein, RanBP2 (note at the time the protein was not designated RanBP2), and the cis-trans prolyl isomerase activity of its cyclophilin domain

2. reports interaction of the RBD4 and CY domains of RanBP2 with red/green opsin and the chaperone activity of these domains toward red/green opsin.

3. reports interaction of the RBD4 and CY domains of RanBP2 with red/green opsin and the chaperone activity of these domains toward red/green opsin.

4. reports identification of a binding domain in RanBP2, the cyclophilin-like domain, toward components of the 19S cap of the proteasome

5. reports identification of a binding domain in RanBP2, the zinc-finger rich domain, toward CRM1/exportin-1

6. reports identification of a novel domain in RanBP2 located between RBD2 and RBD3 with specific binding activity against the conventional heavy chain kinesins, KIF5B and KIF5C

7. reports the novel subcellular localizations of RanBP2 in retinal neurons of human and bovine

8. the cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and protein biogenesis