FKBP52

FK506 binding protein 4, 59kDa, also known as FKBP4, is a human gene.cite web | title = Entrez Gene: FKBP4 FK506 binding protein 4, 59kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2288| accessdate = ]

PBB_Summary
section_title =
summary_text = 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 has high structural and functional similarity to FK506-binding protein 1A (FKBP1A), but unlike FKBP1A, this protein does not have immunosuppressant activity when complexed with FK506. It interacts with interferon regulatory factor-4 and plays an important role in immunoregulatory gene expression in B and T lymphocytes. This encoded protein is known to associate with phytanoyl-CoA alpha-hydroxylase. It can also associate with two heat shock proteins (hsp90 and hsp70) and thus may play a role in the intracellular trafficking of hetero-oligomeric forms of the steroid hormone receptors. This protein correlates strongly with adeno-associated virus type 2 vectors (AAV) resulting in a significant increase in AAV-mediated transgene expression in human cell lines. Thus this encoded protein is thought to have important implications for the optimal use of AAV vectors in human gene therapy. This gene has been found to have multiple polyadenylation sites.cite web | title = Entrez Gene: FKBP4 FK506 binding protein 4, 59kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2288| accessdate = ]

This protein has TPR domain and PPlase domain.

ee also

* Glucocorticoid receptor
* Immunophilins

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Schiene-Fischer C, Yu C |title=Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases. |journal=FEBS Lett. |volume=495 |issue= 1-2 |pages= 1–6 |year= 2001 |pmid= 11322937 |doi=
*cite journal | author=Peattie DA, Harding MW, Fleming MA, "et al." |title=Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 22 |pages= 10974–8 |year= 1992 |pmid= 1279700 |doi=
*cite journal | author=Yem AW, Tomasselli AG, Heinrikson RL, "et al." |title=The Hsp56 component of steroid receptor complexes binds to immobilized FK506 and shows homology to FKBP-12 and FKBP-13. |journal=J. Biol. Chem. |volume=267 |issue= 5 |pages= 2868–71 |year= 1992 |pmid= 1371107 |doi=
*cite journal | author=Tai PK, Albers MW, Chang H, "et al." |title=Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex. |journal=Science |volume=256 |issue= 5061 |pages= 1315–8 |year= 1992 |pmid= 1376003 |doi=
*cite journal | author=Wiederrecht G, Hung S, Chan HK, "et al." |title=Characterization of high molecular weight FK-506 binding activities reveals a novel FK-506-binding protein as well as a protein complex. |journal=J. Biol. Chem. |volume=267 |issue= 30 |pages= 21753–60 |year= 1992 |pmid= 1383226 |doi=
*cite journal | author=Sanchez ER, Faber LE, Henzel WJ, Pratt WB |title=The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins. |journal=Biochemistry |volume=29 |issue= 21 |pages= 5145–52 |year= 1990 |pmid= 2378870 |doi=
*cite journal | author=Alnemri ES, Fernandes-Alnemri T, Nelki DS, "et al." |title=Overexpression, characterization, and purification of a recombinant mouse immunophilin FKBP-52 and identification of an associated phosphoprotein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 14 |pages= 6839–43 |year= 1993 |pmid= 8341706 |doi=
*cite journal | author=Chambraud B, Radanyi C, Camonis JH, "et al." |title=FAP48, a new protein that forms specific complexes with both immunophilins FKBP59 and FKBP12. Prevention by the immunosuppressant drugs FK506 and rapamycin. |journal=J. Biol. Chem. |volume=271 |issue= 51 |pages= 32923–9 |year= 1997 |pmid= 8955134 |doi=
*cite journal | author=Bruner KL, Derfoul A, Robertson NM, "et al." |title=The unliganded mineralocorticoid receptor is associated with heat shock proteins 70 and 90 and the immunophilin FKBP-52. |journal=Receptors & signal transduction |volume=7 |issue= 2 |pages= 85–98 |year= 1998 |pmid= 9392437 |doi=
*cite journal | author=Miyata Y, Chambraud B, Radanyi C, "et al." |title=Phosphorylation of the immunosuppressant FK506-binding protein FKBP52 by casein kinase II: regulation of HSP90-binding activity of FKBP52. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 26 |pages= 14500–5 |year= 1998 |pmid= 9405642 |doi=
*cite journal | author=Bermingham NA, Rauf S, Katsanis N, "et al." |title=The immunophilin FKBP4 (FKBP52/FKBP59) maps to the distal short arm of human chromosome 12. |journal=Mamm. Genome |volume=9 |issue= 3 |pages= 268 |year= 1998 |pmid= 9501323 |doi=
*cite journal | author=Chambraud B, Radanyi C, Camonis JH, "et al." |title=Immunophilins, Refsum disease, and lupus nephritis: the peroxisomal enzyme phytanoyl-COA alpha-hydroxylase is a new FKBP-associated protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 5 |pages= 2104–9 |year= 1999 |pmid= 10051602 |doi=
*cite journal | author=Mamane Y, Sharma S, Petropoulos L, "et al." |title=Posttranslational regulation of IRF-4 activity by the immunophilin FKBP52. |journal=Immunity |volume=12 |issue= 2 |pages= 129–40 |year= 2000 |pmid= 10714679 |doi=
*cite journal | author=Neye H |title=Mutation of FKBP associated protein 48 (FAP48) at proline 219 disrupts the interaction with FKBP12 and FKBP52. |journal=Regul. Pept. |volume=97 |issue= 2-3 |pages= 147–52 |year= 2001 |pmid= 11164950 |doi=
*cite journal | author=Galigniana MD, Radanyi C, Renoir JM, "et al." |title=Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus. |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 14884–9 |year= 2001 |pmid= 11278753 |doi= 10.1074/jbc.M010809200
*cite journal | author=Qing K, Hansen J, Weigel-Kelley KA, "et al." |title=Adeno-associated virus type 2-mediated gene transfer: role of cellular FKBP52 protein in transgene expression. |journal=J. Virol. |volume=75 |issue= 19 |pages= 8968–76 |year= 2001 |pmid= 11533160 |doi= 10.1128/JVI.75.19.8968-8976.2001
*cite journal | author=Guo Y, Guettouche T, Fenna M, "et al." |title=Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex. |journal=J. Biol. Chem. |volume=276 |issue= 49 |pages= 45791–9 |year= 2002 |pmid= 11583998 |doi= 10.1074/jbc.M105931200
*cite journal | author=Davies TH, Ning YM, Sánchez ER |title=A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins. |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 4597–600 |year= 2002 |pmid= 11751894 |doi= 10.1074/jbc.C100531200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899

External links

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