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Gene Review

FKBP14  -  FK506 binding protein 14, 22 kDa

Homo sapiens

Synonyms: 22 kDa FK506-binding protein, 22 kDa FKBP, EDSKMH, FK506-binding protein 14, FKBP-14, ...
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Disease relevance of FKBP14


High impact information on FKBP14

  • We propose that the binding site of SIB1 FKBP22 to a protein substrate of PPIase is located at the N-terminal domain [2].
  • SIB1 FKBP22 is a homodimer, with each subunit consisting of the C-terminal catalytic domain and N-terminal dimerization domain [2].
  • These analyses suggest that the FKBP multigene family emerged early in the evolutionary history of eukaryotes, and during that time some members, including the FKBP65 gene, have experienced gene elongation by means of PPIase domain duplication [3].
  • Both families, although dissimilar in sequence, possess peptidyl-prolyl cis-trans isomerase activity in vitro and can play roles in protein folding and transport, RNA splicing and the regulation of multi-protein complexes in cells [4].
  • All but one of the PPIase inhibiting mAbs were able to significantly inhibit the early establishment and initiation of an intracellular infection of the bacteria in Acanthamoeba castellanii, the natural host, and in the human phagocytic cell line U937 [1].

Analytical, diagnostic and therapeutic context of FKBP14

  • Using surface plasmon resonance, we showed that SIB1 FKBP22 loses the binding ability to a folding intermediate of protein upon truncation of the N-terminal domain but does not lose it upon truncation of the C-terminal domain [2].


  1. The PPIase active site of Legionella pneumophila Mip protein is involved in the infection of eukaryotic host cells. Helbig, J.H., König, B., Knospe, H., Bubert, B., Yu, C., Lück, C.P., Riboldi-Tunnicliffe, A., Hilgenfeld, R., Jacobs, E., Hacker, J., Fischer, G. Biol. Chem. (2003) [Pubmed]
  2. Binding analysis of a psychrotrophic FKBP22 to a folding intermediate of protein using surface plasmon resonance. Suzuki, Y., Win, O.Y., Koga, Y., Takano, K., Kanaya, S. FEBS Lett. (2005) [Pubmed]
  3. Genomic organization of mouse and human 65 kDa FK506-binding protein genes and evolution of the FKBP multigene family. Patterson, C.E., Gao, J., Rooney, A.P., Davis, E.C. Genomics (2002) [Pubmed]
  4. Peptidyl-prolyl cis-trans isomerases (immunophilins) and their roles in parasite biochemistry, host-parasite interaction and antiparasitic drug action. Bell, A., Monaghan, P., Page, A.P. Int. J. Parasitol. (2006) [Pubmed]
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