FKBP3

FK506-binding protein 3 also known as FKBP25 is a protein that in humans is encoded by the FKBP3 gene.

FKBP3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1PBK, 2KFV, 2MPH, 5D75
Identifiers
Aliases	FKBP3, FKBP-25, FKBP-3, FKBP25, PPIase, FK506 binding protein 3, FKBP prolyl isomerase 3
External IDs	OMIM: 186947; MGI: 1353460; HomoloGene: 1525; GeneCards: FKBP3; OMA:FKBP3 - orthologs
Gene location (Human) Chr. Chromosome 14 (human) Band 14q21.2 Start 45,115,599 bp End 45,135,319 bp
Gene location (Mouse) Chr. Chromosome 12 (mouse) Band 12|12 C1 Start 65,109,198 bp End 65,120,781 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Skeletal muscle tissue of biceps brachii vastus lateralis muscle Skeletal muscle tissue of rectus abdominis Brodmann area 23 body of tongue muscle of thigh gastrocnemius muscle sperm thoracic diaphragm right ventricle Top expressed in medial vestibular nucleus mammillary body lateral hypothalamus intercostal muscle ventromedial nucleus tail of embryo deep cerebellar nuclei lateral septal nucleus dorsomedial hypothalamic nucleus paraventricular nucleus of hypothalamus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function isomerase activity FK506 binding peptidyl-prolyl cis-trans isomerase activity protein binding RNA binding signaling receptor activity Cellular component nucleus cytoplasm Biological process chaperone-mediated protein folding protein peptidyl-prolyl isomerization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2287 30795 Ensembl ENSG00000100442 ENSMUSG00000020949 UniProt Q00688 Q62446 RefSeq (mRNA) NM_002013 NM_013902 RefSeq (protein) NP_002004 NP_038930 Location (UCSC) Chr 14: 45.12 – 45.14 Mb Chr 12: 65.11 – 65.12 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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.

Interactions

FKBP3 has been shown to interact with YY1, HDAC1, Histone deacetylase 2, DNA, and Mdm2. Both crystal structure of FKBP25 with FK506 and the NMR structure of full length FKBP25 has been published with PDB ID 5D75 and 2MPH respectively.

Further reading

• 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. doi:10.1016/S0021-9258(19)49856-6. 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. Bibcode:1993PNAS...90.7769J. 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. S2CID 12847618.
• 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.
• 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. S2CID 24265377.
• 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

External links

• PDBe-KB provides an overview of all the structure information available in the PDB for Human Peptidyl-prolyl cis-trans isomerase FKBP3
• PDBe-KB provides an overview of all the structure information available in the PDB for Mouse Peptidyl-prolyl cis-trans isomerase FKBP3