FKBP5

From Wikipedia, the free encyclopedia

FK506 binding protein 5

PDB rendering based on 1kt0.

Available structures: 1kt0, 1kt1

Identifiers

Symbol(s)

FKBP5; P54; PPIase; FKBP51; FKBP54; MGC111006; Ptg-10

External IDs

OMIM: 602623 MGI: 104670 HomoloGene: 3038

Gene ontology
Molecular Function:	• peptidyl-prolyl cis-trans isomerase activity • protein binding • FK506 binding • isomerase activity
Cellular Component:	• nucleus
Biological Process:	• protein folding

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004117 (mRNA)
NP_004108 (protein)

NM_010220 (mRNA)
NP_034350 (protein)

Location

Chr 6: 35.65 - 35.8 Mb

Chr 17: 28.13 - 28.21 Mb

Pubmed search

[1]

[2]

FK506 binding protein 5, also known as FKBP5, is a human gene.^[1]

The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds to the immunosuppressants FK506 and rapamycin. It is thought to mediate calcineurin inhibition. It also interacts functionally with mature hetero-oligomeric progesterone receptor complexes along with the 90 kDa heat shock protein and P23 protein. This gene has been found to have multiple polyadenylation sites.^[1]

[edit] References

^ ^a ^b Entrez Gene: FKBP5 FK506 binding protein 5.

[edit] Further reading

Schiene-Fischer C, Yu C (2001). "Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases.". FEBS Lett. 495 (1-2): 1–6. PMID 11322937.
Baughman G, Wiederrecht GJ, Campbell NF, et al. (1995). "FKBP51, a novel T-cell-specific immunophilin capable of calcineurin inhibition.". Mol. Cell. Biol. 15 (8): 4395–402. PMID 7542743.
Smith DF, Baggenstoss BA, Marion TN, Rimerman RA (1993). "Two FKBP-related proteins are associated with progesterone receptor complexes.". J. Biol. Chem. 268 (24): 18365–71. PMID 7688746.
Smith DF, Albers MW, Schreiber SL, et al. (1993). "FKBP54, a novel FK506-binding protein in avian progesterone receptor complexes and HeLa extracts.". J. Biol. Chem. 268 (32): 24270–3. PMID 7693698.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Johnson J, Corbisier R, Stensgard B, Toft D (1996). "The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes.". J. Steroid Biochem. Mol. Biol. 56 (1-6 Spec No): 31–7. PMID 8603045.
Nair SC, Rimerman RA, Toran EJ, et al. (1997). "Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor.". Mol. Cell. Biol. 17 (2): 594–603. PMID 9001212.
Baughman G, Wiederrecht GJ, Chang F, et al. (1997). "Tissue distribution and abundance of human FKBP51, and FK506-binding protein that can mediate calcineurin inhibition.". Biochem. Biophys. Res. Commun. 232 (2): 437–43. PMID 9125197.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Young JC, Obermann WM, Hartl FU (1998). "Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90.". J. Biol. Chem. 273 (29): 18007–10. PMID 9660753.
Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. PMID 11076863.
Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.". Genome Res. 11 (3): 422–35. doi:10.1101/gr.154701. PMID 11230166.
Pirkl F, Buchner J (2001). "Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40.". J. Mol. Biol. 308 (4): 795–806. doi:10.1006/jmbi.2001.4595. PMID 11350175.
Davies TH, Ning YM, Sánchez ER (2002). "A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins.". J. Biol. Chem. 277 (7): 4597–600. doi:10.1074/jbc.C100531200. PMID 11751894.
Giraudier S, Chagraoui H, Komura E, et al. (2002). "Overexpression of FKBP51 in idiopathic myelofibrosis regulates the growth factor independence of megakaryocyte progenitors.". Blood 100 (8): 2932–40. doi:10.1182/blood-2002-02-0485. PMID 12351405.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Sinars CR, Cheung-Flynn J, Rimerman RA, et al. (2003). "Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complexes.". Proc. Natl. Acad. Sci. U.S.A. 100 (3): 868–73. doi:10.1073/pnas.0231020100. PMID 12538866.
Hubler TR, Denny WB, Valentine DL, et al. (2003). "The FK506-binding immunophilin FKBP51 is transcriptionally regulated by progestin and attenuates progestin responsiveness.". Endocrinology 144 (6): 2380–7. PMID 12746298.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway.". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216.