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InterPro: IPR001876 Zinc finger, RanBP2-type

Protein matchesHelp
UniProtKB
Matches:
1993 proteins
AccessionHelp IPR001876 Znf_RanBP2
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
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 annotationHelp
Function GO:0008270 zinc ion binding
Component GO:0005622 intracellular
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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 linksHelp
SCOP: g.41.11.1
CATH: 4.10.1060.10
Database linksHelp
PDBe-motif: PS01358
PROSITE doc: PDOC50199
PANDIT: PF00641
Blocks: IPB001876

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001876 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O15151 Protein Mdm4

P27398 Calpain-D

P60670 Nuclear protein localization protein 4 homolog

Q06696 Vacuolar protein-sorting-associated protein 36

Q84RQ8 Probable E3 ubiquitin-protein ligase ARI15

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR016495 p53 negative regulator Mdm2/Mdm4
IPR003121 SWIB/MDM2 domain
IPR016563 Polyubiquitin-tagged protein recognition complex, Npl4 component
IPR007717 NPL4
IPR001300 Peptidase C2, calpain
IPR007716 NPL4, zinc-binding putative
IPR007286 EAP30
IPR000169 Peptidase, cysteine peptidase active site
IPR015458 MDM4/MDMX protein
IPR001876 Zinc finger, RanBP2-type
IPR002867 Zinc finger, C6HC-type
IPR001841 Zinc finger, RING-type
PDB Chain
ModBase
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Klug A.
Zinc finger peptides for the regulation of gene expression.
J. Mol. Biol. 293 215-8 1999 [PubMed: 10529348]
http://dx.doi.org/10.1006/jmbi.1999.3007
2. Hall TM.
Multiple modes of RNA recognition by zinc finger proteins.
Curr. Opin. Struct. Biol. 15 367-73 2005 [PubMed: 15963892]
http://dx.doi.org/10.1016/j.sbi.2005.04.004
3. Brown RS.
Zinc finger proteins: getting a grip on RNA.
Curr. Opin. Struct. Biol. 15 94-8 2005 [PubMed: 15718139]
http://dx.doi.org/10.1016/j.sbi.2005.01.006
4. Gamsjaeger R, Liew CK, Loughlin FE, Crossley M, Mackay JP.
Sticky fingers: zinc-fingers as protein-recognition motifs.
Trends Biochem. Sci. 32 63-70 2007 [PubMed: 17210253]
http://dx.doi.org/10.1016/j.tibs.2006.12.007
5. Matthews JM, Sunde M.
Zinc fingers--folds for many occasions.
IUBMB Life 54 351-5 2002 [PubMed: 12665246]
http://dx.doi.org/10.1080/15216540216035
6. Laity JH, Lee BM, Wright PE.
Zinc finger proteins: new insights into structural and functional diversity.
Curr. Opin. Struct. Biol. 11 39-46 2001 [PubMed: 11179890]
http://dx.doi.org/10.1016/S0959-440X(00)00167-6
7. Steggerda SM, Paschal BM.
Regulation of nuclear import and export by the GTPase Ran.
Int. Rev. Cytol. 217 41-91 2002 [PubMed: 12019565]
http://dx.doi.org/10.1016/S0074-7696(02)17012-4
8. Yaseen NR, Blobel G.
Two distinct classes of Ran-binding sites on the nucleoporin Nup-358.
Proc. Natl. Acad. Sci. U.S.A. 96 5516-21 1999 [PubMed: 10318915]
http://dx.doi.org/10.1073/pnas.96.10.5516
9. McDowall J.
Protein of the Month: Zinc Fingers.
2007

Additional ReadingHelp
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
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InterPro 24.0