FKBP52

From Wikipedia, the free encyclopedia

FK506 binding protein 4, 59kDa

PDB rendering based on 1n1a.

Available structures: 1n1a, 1p5q, 1q1c, 1qz2, 1rot, 1rou

Identifiers

Symbol(s)

FKBP4; PPIase; FKBP52; FKBP59; HBI; Hsp56; p52

External IDs

OMIM: 600611 MGI: 95543 HomoloGene: 36085

Gene ontology
Molecular Function:	• peptidyl-prolyl cis-trans isomerase activity • ATP binding • GTP binding • FK506 binding • isomerase activity • protein binding, bridging • heat shock protein binding • glucocorticoid receptor binding • phosphoprotein binding
Cellular Component:	• intracellular • nucleus • cytoplasm
Biological Process:	• protein folding • steroid hormone receptor complex assembly • embryo implantation • protein complex localization • male sex differentiation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002014 (mRNA)
NP_002005 (protein)

NM_010219 (mRNA)
NP_034349 (protein)

Location

Chr 12: 2.77 - 2.78 Mb

Chr 6: 128.4 - 128.4 Mb

Pubmed search

[1]

[2]

FK506 binding protein 4, 59kDa, also known as FKBP4, 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 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.^[1]

This protein has TPR domain and PPlase domain.

1 See also
2 References
3 Further reading
4 External links

[edit] See also

[edit] References

^ ^a ^b Entrez Gene: FKBP4 FK506 binding protein 4, 59kDa.

[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.
Peattie DA, Harding MW, Fleming MA, et al. (1992). "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.". Proc. Natl. Acad. Sci. U.S.A. 89 (22): 10974–8. PMID 1279700.
Yem AW, Tomasselli AG, Heinrikson RL, et al. (1992). "The Hsp56 component of steroid receptor complexes binds to immobilized FK506 and shows homology to FKBP-12 and FKBP-13.". J. Biol. Chem. 267 (5): 2868–71. PMID 1371107.
Tai PK, Albers MW, Chang H, et al. (1992). "Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex.". Science 256 (5061): 1315–8. PMID 1376003.
Wiederrecht G, Hung S, Chan HK, et al. (1992). "Characterization of high molecular weight FK-506 binding activities reveals a novel FK-506-binding protein as well as a protein complex.". J. Biol. Chem. 267 (30): 21753–60. PMID 1383226.
Sanchez ER, Faber LE, Henzel WJ, Pratt WB (1990). "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.". Biochemistry 29 (21): 5145–52. PMID 2378870.
Alnemri ES, Fernandes-Alnemri T, Nelki DS, et al. (1993). "Overexpression, characterization, and purification of a recombinant mouse immunophilin FKBP-52 and identification of an associated phosphoprotein.". Proc. Natl. Acad. Sci. U.S.A. 90 (14): 6839–43. PMID 8341706.
Chambraud B, Radanyi C, Camonis JH, et al. (1997). "FAP48, a new protein that forms specific complexes with both immunophilins FKBP59 and FKBP12. Prevention by the immunosuppressant drugs FK506 and rapamycin.". J. Biol. Chem. 271 (51): 32923–9. PMID 8955134.
Bruner KL, Derfoul A, Robertson NM, et al. (1998). "The unliganded mineralocorticoid receptor is associated with heat shock proteins 70 and 90 and the immunophilin FKBP-52.". Receptors & signal transduction 7 (2): 85–98. PMID 9392437.
Miyata Y, Chambraud B, Radanyi C, et al. (1998). "Phosphorylation of the immunosuppressant FK506-binding protein FKBP52 by casein kinase II: regulation of HSP90-binding activity of FKBP52.". Proc. Natl. Acad. Sci. U.S.A. 94 (26): 14500–5. PMID 9405642.
Bermingham NA, Rauf S, Katsanis N, et al. (1998). "The immunophilin FKBP4 (FKBP52/FKBP59) maps to the distal short arm of human chromosome 12.". Mamm. Genome 9 (3): 268. PMID 9501323.
Chambraud B, Radanyi C, Camonis JH, et al. (1999). "Immunophilins, Refsum disease, and lupus nephritis: the peroxisomal enzyme phytanoyl-COA alpha-hydroxylase is a new FKBP-associated protein.". Proc. Natl. Acad. Sci. U.S.A. 96 (5): 2104–9. PMID 10051602.
Mamane Y, Sharma S, Petropoulos L, et al. (2000). "Posttranslational regulation of IRF-4 activity by the immunophilin FKBP52.". Immunity 12 (2): 129–40. PMID 10714679.
Neye H (2001). "Mutation of FKBP associated protein 48 (FAP48) at proline 219 disrupts the interaction with FKBP12 and FKBP52.". Regul. Pept. 97 (2-3): 147–52. PMID 11164950.
Galigniana MD, Radanyi C, Renoir JM, et al. (2001). "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.". J. Biol. Chem. 276 (18): 14884–9. doi:10.1074/jbc.M010809200. PMID 11278753.
Qing K, Hansen J, Weigel-Kelley KA, et al. (2001). "Adeno-associated virus type 2-mediated gene transfer: role of cellular FKBP52 protein in transgene expression.". J. Virol. 75 (19): 8968–76. doi:10.1128/JVI.75.19.8968-8976.2001. PMID 11533160.
Guo Y, Guettouche T, Fenna M, et al. (2002). "Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex.". J. Biol. Chem. 276 (49): 45791–9. doi:10.1074/jbc.M105931200. PMID 11583998.
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.
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.