{PDOC50199}
{PS01358; ZF_RANBP2_1}
{PS50199; ZF_RANBP2_2}
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* Zinc finger RanBP2-type signature and profile *
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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.

-Consensus pattern: W-x-C-x(2,4)-C-x(3)-N-x(6)-C-x(2)-C
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: May 2002 / Text revised.

[ 1] Mattaj I.W., Englmeier L.
     "Nucleocytoplasmic transport: the soluble phase."
     Annu. Rev. Biochem. 67:265-306(1998).
     PubMed=9759490; DOI=10.1146/annurev.biochem.67.1.265
[ 2] Melchior F., Gerace L.
     "Two-way trafficking with Ran."
     Trends Cell Biol. 8:175-179(1998).
     PubMed=9695834
[ 3] Matunis M.J., Coutavas E., Blobel G.
     "A novel ubiquitin-like modification modulates the partitioning of the
     Ran-GTPase-activating protein RanGAP1 between the cytosol and the
     nuclear pore complex."
     J. Cell Biol. 135:1457-1470(1996).
     PubMed=8978815
[ 4] Mahajan R., Delphin C., Guan T., Gerace L., Melchior F.
     "A small ubiquitin-related polypeptide involved in targeting RanGAP1
     to nuclear pore complex protein RanBP2."
     Cell 88:97-107(1997).
     PubMed=9019411
[ 5] Yaseen N.R., Blobel G.
     "Two distinct classes of Ran-binding sites on the nucleoporin
     Nup-358."
     Proc. Natl. Acad. Sci. U.S.A. 96:5516-5521(1999).
     PubMed=10318915
[ 6] Singh B.B., Patel H.H., Roepman R., Schick D., Ferreira P.A.
     "The zinc finger cluster domain of RanBP2 is a specific docking site
     for the nuclear export factor, exportin-1."
     J. Biol. Chem. 274:37370-37378(1999).
     PubMed=10601307

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