InterPro : IPR000156

Name  Ran binding domain Short Name  Ran_bind_dom
Type  Domain Description  Ran is an evolutionary conserved member of the Ras superfamily that regulates all receptor-mediated transport between the nucleus and the cytoplasm. Ran Binding Protein 1 (RanBP1) has guanine nucleotide dissociation inhibitory activity, specific for the GTP form of Ran and also functions to stimulate Ran GTPase activating protein(GAP)-mediated GTP hydrolysis by Ran. RanBP1 contributes to maintaining the gradient of RanGTP across the nuclear envelope high (GDI activity) or the cytoplasmic levels of RanGTP low (GAP cofactor) [].All RanBP1 proteins contain an approx 150 amino acid residue Ran binding domain. Ran BP1 binds directly to RanGTP with high affinity.There are four sites of contact between Ran and the Ran binding domain. One of these involves binding of the C-terminal segment of Ran to a groove on the Ran binding domain that is analogous to the surface utilised in the EVH1-peptide interaction []. Nup358 contains four Ran binding domains. The structure of the first of these is known [].
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

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0 Found In

1 Parent Features

Id Name Short Name Type
IPR011993 Pleckstrin homology-like domain PH_like_dom Domain

3 Publications

First Author Title Year Journal Volume Pages
Vetter IR Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport. 1999 Nature 398 39-46
Steggerda SM Regulation of nuclear import and export by the GTPase Ran. 2002 Int Rev Cytol 217 41-91
Fedorov AA Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function. 1999 Nat Struct Biol 6 661-5



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)