Structural highlights
Function
[RANB3_HUMAN] 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.[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Mueller L, Cordes VC, Bischoff FR, Ponstingl H. Human RanBP3, a group of nuclear RanGTP binding proteins. FEBS Lett. 1998 May 15;427(3):330-6. PMID:9637251
- ↑ Englmeier L, Fornerod M, Bischoff FR, Petosa C, Mattaj IW, Kutay U. RanBP3 influences interactions between CRM1 and its nuclear protein export substrates. EMBO Rep. 2001 Oct;2(10):926-32. Epub 2001 Sep 24. PMID:11571268 doi:http://dx.doi.org/10.1093/embo-reports/kve200
- ↑ Lindsay ME, Holaska JM, Welch K, Paschal BM, Macara IG. Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export. J Cell Biol. 2001 Jun 25;153(7):1391-402. PMID:11425870
- ↑ Nemergut ME, Lindsay ME, Brownawell AM, Macara IG. Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor. J Biol Chem. 2002 May 17;277(20):17385-8. Epub 2002 Apr 3. PMID:11932251 doi:http://dx.doi.org/10.1074/jbc.C100620200
- ↑ Dai F, Lin X, Chang C, Feng XH. Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-beta signaling. Dev Cell. 2009 Mar;16(3):345-57. doi: 10.1016/j.devcel.2009.01.022. PMID:19289081 doi:10.1016/j.devcel.2009.01.022
