Home  |  Contact
PROSITE documentation PDOC50199 [for PROSITE entry PS01358]

Zinc finger RanBP2-type signature and profile





Description

Nucleocytoplasmic transport is mediated by large supramolecular structures that span the nuclear envelope called nuclear pore complexes (NPC). The export as well as the import pathway require three major component, the substrate, an adaptor complex and a receptor. The adaptor complex and the receptor pass through the NPC with the substrate. The nuclear transport is also dependent on the GTPase cycle of the small GTPase protein Ran and a number of Ran-binding proteins (RanBP) [1,2].

RanBP2 is one of these proteins located in the NPC on the cytoplasmic side of the ring. The function of RanBP2 is not yet well understood. It could function in coupling RanGTP hydrolysis to NPC translocation through its Ran binding domain (RanBD1) (see <PDOC50196>) [3,4]. RanBP2 contains also a cluster of zinc fingers, the RanBP2 zinc fingers. It has been shown that these zinc fingers bind RanGDP (but not RanGTP) [5] and the exportin-1 protein (a receptor of the export pathway) [6].

The RanBP2 zinc finger is also found in different proteins that are mainly involved in nuclear transport or localized to the nuclear envelope. Some of the proteins containing such a domain are listed below.

  • Mammalian RanBP2/Nup358 protein. Implicated in nuclear import and export processes (8 copies).
  • Human MDM2, play a central role in P53 regulation. MDM2 binds to P53 in the nucleus and the complexe is transported to the cytoplasm via a signal in MDM2 (1 copy).
  • Human EWS protein. May play a role in the tumorigenic process. It may disturb gene expression by mimicking, or interfering with the normal function of CTD-polII within the transcription initiation complex (1 copy).
  • FUS, probable RNA-binding protein. Exhibits diffuse staining throughout the nucleus (excluding nucleoli), together with a small number of intensely stained focal points, or granules, and punctate staining along the nuclear envelope (1 copy).
  • Human nuclear pore complex protein Nup153. Possible DNA-binding subunit of the nuclear pore complex (NPC). Located to the terminal ring structure of nucleoplasmic cage (4 copies).
  • Yeast asparagine-rich protein 1 (ARP1). Protein of unknown function (2 copies).

The RanBP2 zinc finger contains 4 cysteines and a conserved tryptophan upstream of the zinc finger. Our pattern starts with this tryptophan and includes the 4 cysteines. We have also developed a profile that covers a region slightly bigger than the zinc finger.

Last update:

May 2002 / Text revised.

-------------------------------------------------------------------------------

Technical section

PROSITE methods (with tools and information) covered by this documentation:

ZF_RANBP2_1, PS01358; Zinc finger RanBP2-type signature  (PATTERN)

ZF_RANBP2_2, PS50199; Zinc finger RanBP2 type profile  (MATRIX)


References

1AuthorsMattaj I.W. Englmeier L.
TitleNucleocytoplasmic transport: the soluble phase.
SourceAnnu. Rev. Biochem. 67:265-306(1998).
PubMed ID9759490
DOI10.1146/annurev.biochem.67.1.265

2AuthorsMelchior F. Gerace L.
TitleTwo-way trafficking with Ran.
SourceTrends Cell Biol. 8:175-179(1998).
PubMed ID9695834

3AuthorsMatunis M.J. Coutavas E. Blobel G.
TitleA novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex.
SourceJ. Cell Biol. 135:1457-1470(1996).
PubMed ID8978815

4AuthorsMahajan R. Delphin C. Guan T. Gerace L. Melchior F.
TitleA small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2.
SourceCell 88:97-107(1997).
PubMed ID9019411

5AuthorsYaseen N.R. Blobel G.
TitleTwo distinct classes of Ran-binding sites on the nucleoporin Nup-358.
SourceProc. Natl. Acad. Sci. U.S.A. 96:5516-5521(1999).
PubMed ID10318915

6AuthorsSingh B.B. Patel H.H. Roepman R. Schick D. Ferreira P.A.
TitleThe zinc finger cluster domain of RanBP2 is a specific docking site for the nuclear export factor, exportin-1.
SourceJ. Biol. Chem. 274:37370-37378(1999).
PubMed ID10601307



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)