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FKBP3 Protein, Antibody, ELISA Kit, cDNA Clone

FKBP3 Related Areas

FKBP3 Related Pathways

FKBP3 Related Product

    FKBP3 Summary & Protein Information

    FKBP3 Background

    Gene Summary: The protein encoded by this FKBP3 gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. FKBP3 is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin, as well as histone deacetylases, the transcription factor YY1, casein kinase II, and nucleolin. FKBP3 has a higher affinity for rapamycin than for FK506 and thus may be an important target molecule for immunosuppression by rapamycin. [provided by RefSeq, Sep 2008]
    General information above from NCBI
    Catalytic activity: Peptidylproline (omega=180) = peptidylproline (omega=0).
    Enzyme regulation: Inhibited preferentially by rapamycin over FK506.
    Subunit structure: Interacts with KCNMA1 tetramer. There are probably 4 molecules of KCMNB2 per KCNMA1 tetramer.
    Domain: The ball and chain domain mediates the inactivation of KCNMA1. It occludes the conduction pathway of KCNMA1 channels, and comprises the pore-blocking ball domain (residues 1-17) and the chain domain (residues 20-45) linking it to the transmembrane segment. The ball domain is made up of a flexible N-terminus anchored at a well ordered loop-helix motif. The chain domain consists of a 4-turn helix with an unfolded linker at its C- terminus.
    Subcellular location: Nucleus.
    Tissue specificity: Expressed in kidney, heart and brain. Highly expressed in ovary. Expressed at low level in other tissues.
    Post-translational: N-glycosylated.
    Sequence similarity: Belongs to the FKBP-type PPIase family.
    Contains 1 PPIase FKBP-type domain.
    General information above from UniProt

    FKBP3 Alternative Name

    FKBP25,PPIase,FKBP-25,FKBP3, [human]
    25kDa,FKBP25,FKBP-3,Fkbp3, [mouse]

    FKBP3 Related Studies

  • Wiederrecht G., et al., 1992, Biochem. Biophys. Res. Commun. 185: 298 - 303.
  • Dephoure N., et al.,2008, Proc. Natl. Acad. Sci. USA.105:10762-7.
  • Gauci S., et al., 2009, Anal. Chem. 81:4493-4501.
  • Choudhary C., et al., 2009, Science. 325:834-840.
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