FKBP3

FK506 binding protein 3, 25kDa

PDB rendering based on 1pbk.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1PBK, 2KFV, 2MPH

Identifiers

Symbols

FKBP3 ; FKBP-25; FKBP-3; FKBP25; PPIase

External IDs

OMIM: 186947 MGI: 1353460 HomoloGene: 1525 ChEMBL: 4746 GeneCards: FKBP3 Gene

EC number

5.2.1.8

Gene ontology
Molecular function	• peptidyl-prolyl cis-trans isomerase activity • receptor activity • protein binding • FK506 binding • poly(A) RNA binding
Cellular component	• nucleus • cytoplasm • endoplasmic reticulum membrane
Biological process	• protein peptidyl-prolyl isomerization • chaperone-mediated protein folding
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
45.12 – 45.14 Mb

Chr 12:
65.06 – 65.07 Mb

PubMed search

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

Function

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.
1 2 "Entrez Gene: FKBP3 FK506 binding protein 3, 25kDa".
1 2 3 Yang WM, Yao YL, Seto E (Sep 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.
↑ Ochocka AM, Kampanis P, Nicol S, Allende-Vega N, Cox M, Marcar L, Milne D, Fuller-Pace F, Meek D (Feb 2009). "FKBP25, a novel regulator of the p53 pathway, induces the degradation of MDM2 and activation of p53". FEBS Lett. 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.
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, Suyama A, Sugano S (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.
Meng X, Chen J, Yang Q, Wang S, Chao Y, Ying K, Xie Y, Mao Y (2002). "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.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (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

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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FKBP3

Function

Interactions

References

Further reading