FKBP3

FK506 binding protein 3, 25kDa

PDB rendering based on 1pbk.

Available structures
PDB	1PBK, 2KFV

Identifiers

Symbols

FKBP3; FKBP-25; PPIase

External IDs

OMIM: 186947 MGI: 1353460 HomoloGene: 1525 GeneCards: FKBP3 Gene

EC number

5.2.1.8

Gene Ontology
Molecular function	• peptidyl-prolyl cis-trans isomerase activity • receptor activity • FK506 binding • isomerase activity
Cellular component	• nucleus • membrane
Biological process	• protein peptidyl-prolyl isomerization • protein folding • peptidyl-proline modification
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
45.58 – 45.6 Mb

Chr 12:
66.16 – 66.17 Mb

PubMed search

[1]

[2]

FK506-binding protein 3 is a protein that in humans is encoded by the FKBP3 gene.^[1]^[2]^[3]

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 the immunosuppressants FK506 and rapamycin. It has a higher affinity for rapamycin than for FK506 and thus may be an important target molecule for immunosuppression by rapamycin.^[3]

Interactions

FKBP3 has been shown to interact with YY1,^[4] HDAC1,^[4] Histone deacetylase 2^[4] and Mdm2.^[5]

References

^ Hung DT, Schreiber SL (Jun 1992). "cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein". Biochem Biophys Res Commun 184 (2): 733–8. doi:10.1016/0006-291X(92)90651-Z. PMID 1374240.
^ Porat R, Poutsiaka DD, Miller LC, Granowitz EV, Dinarello CA (May 1992). "Interleukin-1 (IL-1) receptor blockade reduces endotoxin and Borrelia burgdorferi-stimulated IL-8 synthesis in human mononuclear cells". FASEB J 6 (7): 2482–6. PMID 1532945.
^ ^a ^b "Entrez Gene: FKBP3 FK506 binding protein 3, 25kDa". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2287.
^ ^a ^b ^c Yang, W M; Yao Y L, Seto E (Sep. 2001). "The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1". EMBO J. (England) 20 (17): 4814–25. doi:10.1093/emboj/20.17.4814. ISSN 0261-4189. PMC 125595. PMID 11532945. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125595.
^ Ochocka, Anna Maria; Kampanis Petros, Nicol Samantha, Allende-Vega Nerea, Cox Miranda, Marcar Lynnette, Milne Diane, Fuller-Pace Frances, Meek David (Feb. 2009). "FKBP25, a novel regulator of the p53 pathway, induces the degradation of MDM2 and activation of p53". FEBS Lett. (Netherlands) 583 (4): 621–6. doi:10.1016/j.febslet.2009.01.009. PMID 19166840.

Jin YJ, Burakoff SJ, Bierer BE (1992). "Molecular cloning of a 25-kDa high affinity rapamycin binding protein, FKBP25". J. Biol. Chem. 267 (16): 10942–5. PMID 1375932.
Wiederrecht G, Martin MM, Sigal NH, Siekierka JJ (1992). "Isolation of a human cDNA encoding a 25 kDa FK-506 and rapamycin binding protein". Biochem. Biophys. Res. Commun. 185 (1): 298–303. doi:10.1016/S0006-291X(05)80990-8. PMID 1376117.
Jin YJ, Burakoff SJ (1993). "The 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase II and nucleolin". Proc. Natl. Acad. Sci. U.S.A. 90 (16): 7769–73. doi:10.1073/pnas.90.16.7769. PMC 47224. PMID 7689229. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=47224.
Cross SH, Charlton JA, Nan X, Bird AP (1994). "Purification of CpG islands using a methylated DNA binding column". Nat. Genet. 6 (3): 236–44. doi:10.1038/ng0394-236. PMID 8012384.
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. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
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. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Yang WM, Yao YL, Seto E (2001). "The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1". EMBO J. 20 (17): 4814–25. doi:10.1093/emboj/20.17.4814. PMC 125595. PMID 11532945. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125595.
Meng X, Chen J, Yang Q, et al. (2003). "Cloning and identification of a novel cDNA which may be associated with FKBP25". Biochem. Genet. 40 (9–10): 303–10. doi:10.1023/A:1020256718720. PMID 12392168.
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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
Won J, Kim M, Yi YW, et al. (2005). "A magnetic nanoprobe technology for detecting molecular interactions in live cells". Science 309 (5731): 121–5. doi:10.1126/science.1112869. PMID 15994554.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.

PDB gallery

1pbk: HOMOLOGOUS DOMAIN OF HUMAN FKBP25

Isomerases: geometric (EC 5.2)

5.2.1	FKBP: FKBP1A · FKBP1B · FKBP2 · FKBP3 · FKBP5 · FKBP6 · FKBP8 · FKBP9 · FKBP10 · FKBP52 · FKBPL other: Cyclophilin · Parvulin · Prolyl isomerase

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

FKBP3

Interactions

References

Further reading