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Gene Review

FPR3  -  peptidylprolyl isomerase FPR3

Saccharomyces cerevisiae S288c

Synonyms: FK506-binding nuclear protein, FKBP-70, NPI46, Nucleolar proline isomerase, PPIase, ...
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Disease relevance of FPR3


High impact information on FPR3

  • Impaired checkpoint function is observed both in cells lacking FPR3 and in cells treated with rapamycin, a small molecule inhibitor that binds to the proline isomerase (PPIase) domain of Fpr3 [2].
  • Here, we show that the FK506 binding protein Fpr3 prevents premature adaptation to damage and thus serves to maintain recombination checkpoint activity [2].
  • The FK506 binding protein Fpr3 counteracts protein phosphatase 1 to maintain meiotic recombination checkpoint activity [2].
  • Visualization of the complex by electron microscopy and immunogold labeling revealed a characteristic cluster-forming network of nonuniform size containing nucleolar proteins like Nop1p and Fpr3p and attached pol I [3].
  • Even fpr1 fpr2 fpr3 triple mutants are viable [1].

Biological context of FPR3


Anatomical context of FPR3


Associations of FPR3 with chemical compounds


Regulatory relationships of FPR3


Other interactions of FPR3

  • The yeast immunophilin Fpr3 is a physiological substrate of the tyrosine-specific phosphoprotein phosphatase Ptp1 [4].
  • Overexpression of ZDS1,2 suppressed the temperature sensitivity, geldanamycin (GA) sensitivity, slow growth, and flocculation of multiple cka2 alleles and enhanced CK2 activity in vivo toward a known physiological substrate, Fpr3 [11].
  • Here we show the phosphatase activity of Ltp1 on Fpr3 and we demonstrated that Tyr 184 is the residue phosphorylated on in vivo Fpr3 [7].


  1. A novel FK506- and rapamycin-binding protein (FPR3 gene product) in the yeast Saccharomyces cerevisiae is a proline rotamase localized to the nucleolus. Benton, B.M., Zang, J.H., Thorner, J. J. Cell Biol. (1994) [Pubmed]
  2. The FK506 binding protein Fpr3 counteracts protein phosphatase 1 to maintain meiotic recombination checkpoint activity. Hochwagen, A., Tham, W.H., Brar, G.A., Amon, A. Cell (2005) [Pubmed]
  3. Association of yeast RNA polymerase I with a nucleolar substructure active in rRNA synthesis and processing. Fath, S., Milkereit, P., Podtelejnikov, A.V., Bischler, N., Schultz, P., Bier, M., Mann, M., Tschochner, H. J. Cell Biol. (2000) [Pubmed]
  4. The yeast immunophilin Fpr3 is a physiological substrate of the tyrosine-specific phosphoprotein phosphatase Ptp1. Wilson, L.K., Benton, B.M., Zhou, S., Thorner, J., Martin, G.S. J. Biol. Chem. (1995) [Pubmed]
  5. Yeast NPI46 encodes a novel prolyl cis-trans isomerase that is located in the nucleolus. Shan, X., Xue, Z., Mélèse, T. J. Cell Biol. (1994) [Pubmed]
  6. FAP1, a homologue of human transcription factor NF-X1, competes with rapamycin for binding to FKBP12 in yeast. Kunz, J., Loeschmann, A., Deuter-Reinhard, M., Hall, M.N. Mol. Microbiol. (2000) [Pubmed]
  7. The in vivo tyrosine phosphorylation level of yeast immunophilin Fpr3 is influenced by the LMW-PTP Ltp1. Magherini, F., Gamberi, T., Paoli, P., Marchetta, M., Biagini, M., Raugei, G., Camici, G., Ramponi, G., Modesti, A. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  8. The yeast peptidyl proline isomerases FPR3 and FPR4, in high copy numbers, suppress defects resulting from the absence of the E3 ubiquitin ligase TOM1. Davey, M., Hannam, C., Wong, C., Brandl, C.J. Mol. Gen. Genet. (2000) [Pubmed]
  9. FK 506-binding protein proline rotamase is a target for the immunosuppressive agent FK 506 in Saccharomyces cerevisiae. Heitman, J., Movva, N.R., Hiestand, P.C., Hall, M.N. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  10. Casein kinase II catalyzes tyrosine phosphorylation of the yeast nucleolar immunophilin Fpr3. Wilson, L.K., Dhillon, N., Thorner, J., Martin, G.S. J. Biol. Chem. (1997) [Pubmed]
  11. Genetic interactions among ZDS1,2, CDC37, and protein kinase CK2 in Saccharomyces cerevisiae. Bandhakavi, S., McCann, R.O., Hanna, D.E., Glover, C.V. FEBS Lett. (2003) [Pubmed]
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