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FKBP3  -  FK506 binding protein 3, 25kDa

Homo sapiens

Synonyms: 25 kDa FK506-binding protein, 25 kDa FKBP, FK506-binding protein 3, FKBP-25, FKBP-3, ...
 
 
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Disease relevance of FKBP3

  • The putative peptidylprolyl cis-trans isomerase (PPIase) encoded by XC2699 of the plant bacterial pathogen Xanthomonas campestris pv. campestris 8004 exhibits a 49% similarity at the amino-acid level to the Mip protein of Legionella pneumophila [1].
  • This mip-like gene, XC2699, was overexpressed in Escherichia coli and the purified (His)6-tagged Mip-like protein encoded by XC2699 exhibited a PPIase activity specifically inhibited by FK-506 [1].
 

High impact information on FKBP3

 

Biological context of FKBP3

 

Anatomical context of FKBP3

  • On the localization of FKBP25 in T-lymphocytes [6].
  • Reverse transcription-polymerase chain reaction (RT-PCR) amplification of rabbit FKBP25 and FKBP12 in selected rabbit organs, including total cornea, showed higher expressions in cornea, retina, cerebrum and cerebellum than other compared tissues [11].
 

Associations of FKBP3 with chemical compounds

 

Other interactions of FKBP3

 

Analytical, diagnostic and therapeutic context of FKBP3

  • These data demonstrate that FKBP25 has a higher affinity for rapamycin than for FK506 and suggest that this cellular receptor may be an important target molecule for immunosuppression by rapamycin [5].
  • Using polyclonal rabbit antibodies against bovine FKBP25, NEPHGE/SDS-PAGE and Western blotting we demonstrate that the rapamycin-specific immunophilin FKBP25 is present in T-lymphoma Jurkat cells [6].

References

  1. Requirement of a mip-like gene for virulence in the phytopathogenic bacterium Xanthomonas campestris pv. campestris. Zang, N., Tang, D.J., Wei, M.L., He, Y.Q., Chen, B., Feng, J.X., Xu, J., Gan, Y.Q., Jiang, B.L., Tang, J.L. Mol. Plant Microbe Interact. (2007) [Pubmed]
  2. The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1. Yang, W.M., Yao, Y.L., Seto, E. EMBO J. (2001) [Pubmed]
  3. The 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase II and nucleolin. Jin, Y.J., Burakoff, S.J. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  4. Identification of the immunophilins capable of mediating inhibition of signal transduction by cyclosporin A and FK506: roles of calcineurin binding and cellular location. Bram, R.J., Hung, D.T., Martin, P.K., Schreiber, S.L., Crabtree, G.R. Mol. Cell. Biol. (1993) [Pubmed]
  5. Molecular cloning of a 25-kDa high affinity rapamycin binding protein, FKBP25. Jin, Y.J., Burakoff, S.J., Bierer, B.E. J. Biol. Chem. (1992) [Pubmed]
  6. On the localization of FKBP25 in T-lymphocytes. Rivière, S., Ménez, A., Galat, A. FEBS Lett. (1993) [Pubmed]
  7. cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein. Hung, D.T., Schreiber, S.L. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
  8. Isolation of a human cDNA encoding a 25 kDa FK-506 and rapamycin binding protein. Wiederrecht, G., Martin, M.M., Sigal, N.H., Siekierka, J.J. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
  9. Cloning and identification of a novel cDNA which may be associated with FKBP25. Meng, X., Chen, J., Yang, Q., Wang, S., Chao, Y., Ying, K., Xie, Y., Mao, Y. Biochem. Genet. (2002) [Pubmed]
  10. Rapamycin inhibits didemnin B-induced apoptosis in human HL-60 cells: evidence for the possible involvement of FK506-binding protein 25. Johnson, K.L., Lawen, A. Immunol. Cell Biol. (1999) [Pubmed]
  11. Cloning and high expression of rabbit FKBP25 in cornea. Kitagawa, H., Hotta, Y., Fujiki, K., Kanai, A. Jpn. J. Ophthalmol. (1996) [Pubmed]
  12. Molecular mechanisms of immunosuppression by cyclosporins. Zenke, G., Baumann, G., Wenger, R., Hiestand, P., Quesniaux, V., Andersen, E., Schreier, M.H. Ann. N. Y. Acad. Sci. (1993) [Pubmed]
  13. The serpins alpha-1-antitrypsin and alpha-1-antichymotrypsin specifically interact with immunophilins. Feldkämper, I., Verspohl, E.J., Neye, H. Die Pharmazie. (2003) [Pubmed]
  14. Nuclear proteins: promising targets for cancer drugs. Yao, Y.L., Yang, W.M. Current cancer drug targets. (2005) [Pubmed]
 
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