 |
InterPro: IPR001876 Zinc finger, RanBP2-type
Protein matches
|
UniProtKB Matches: 1993 proteins |
|
Accession
|
IPR001876 Znf_RanBP2 |
Type
|
Domain |
Signatures
|
|
InterPro Relationships
|
|
Found in
|
IPR015458 MDM4/MDMX protein
IPR015459 Ubiquitin-protein ligase E3 MDM2
IPR016495 p53 negative regulator Mdm2/Mdm4
IPR017337 Uncharacterised conserved protein UCP037956, zinc finger Ran-binding
|
GO Term annotation
|
|
Function
|
GO:0008270 zinc ion binding
|
|
Component
|
GO:0005622 intracellular
|
|
InterPro annotation
|
|
Entry Details in BioMart
|
Abstract
|
Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [1, 2, 3, 4, 5]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few [6]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.
This entry represents the zinc finger domain found in RanBP2 proteins. 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 2 (RanBP2) is a 358kDa nucleoporin located on the cytoplasmic side of the nuclear pore complex which plays a role in nuclear protein import [7]. RanBP2 contains multiple zinc fingers which mediate binding to RanGDP [8].
More information about these proteins can be found at Protein of the Month: Zinc Fingers [9].
|
Structural links
|
|
Database links
|
|
Additional Reading
|
|
Wang B, Alam SL, Meyer HH, Payne M, Stemmler TL, Davis DR, Sundquist WI.
Structure and ubiquitin interactions of the conserved zinc finger domain of Npl4.
J. Biol. Chem. 278 2003 20225-34
[PubMed: 12644454]
http://dx.doi.org/10.1074/jbc.M300459200
|
|
Matunis MJ, 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 1996 1457-70
[PubMed: 8978815]
http://dx.doi.org/10.1083/jcb.135.6.1457
|
|
Higa MM, Alam SL, Sundquist WI, Ullman KS.
Molecular characterization of the Ran-binding zinc finger domain of Nup153.
J. Biol. Chem. 282 2007 17090-100
[PubMed: 17426026]
http://dx.doi.org/10.1074/jbc.M702715200
|
|
Yu GW, Allen MD, Andreeva A, Fersht AR, Bycroft M.
Solution structure of the C4 zinc finger domain of HDM2.
Protein Sci. 15 2006 384-9
[PubMed: 16385008]
http://dx.doi.org/10.1110/ps.051927306
|
|
Alam SL, Sun J, Payne M, Welch BD, Blake BK, Davis DR, Meyer HH, Emr SD, Sundquist WI.
Ubiquitin interactions of NZF zinc fingers.
EMBO J. 23 2004 1411-21
[PubMed: 15029239]
http://dx.doi.org/10.1038/sj.emboj.7600114
|
|
Gill DJ, Teo H, Sun J, Perisic O, Veprintsev DB, Emr SD, Williams RL.
Structural insight into the ESCRT-I/-II link and its role in MVB trafficking.
EMBO J. 26 2007 600-12
[PubMed: 17215868]
http://dx.doi.org/10.1038/sj.emboj.7601501
|
|
Melchior F, Gerace L.
Two-way trafficking with Ran.
Trends Cell Biol. 8 1998 175-9
[PubMed: 9695834]
http://dx.doi.org/10.1016/S0962-8924(98)01252-5
|
|
Mattaj IW, Englmeier L.
Nucleocytoplasmic transport: the soluble phase.
Annu. Rev. Biochem. 67 1998 265-306
[PubMed: 9759490]
http://dx.doi.org/10.1146/annurev.biochem.67.1.265
|
|
Singh BB, Patel HH, Roepman R, Schick D, Ferreira PA.
The zinc finger cluster domain of RanBP2 is a specific docking site for the nuclear export factor, exportin-1.
J. Biol. Chem. 274 1999 37370-8
[PubMed: 10601307]
http://dx.doi.org/10.1074/jbc.274.52.37370
|
|
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 1997 97-107
[PubMed: 9019411]
http://dx.doi.org/10.1016/S0092-8674(00)81862-0
|
|
|
InterPro 24.0
|