// Workers AI · dad joke modeWhat did FKBP3 say to its date? You bind me.
| FKBP3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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FK506-binding protein 3 also known as FKBP25 is a protein that in humans is encoded by the FKBP3 gene.[5][6][7]
Function
[edit]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.[8][7]
Interactions
[edit]FKBP3 has been shown to interact with YY1,[9] HDAC1,[9] Histone deacetylase 2,[9] DNA,[10] and Mdm2.[11] 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.[8][10]
References
[edit]- 1 2 3 GRCh38: Ensembl release 89: ENSG00000100442 – Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020949 – Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ Hung DT, Schreiber SL (June 1992). "cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein". Biochemical and Biophysical Research Communications. 184 (2): 733–738. Bibcode:1992BBRC..184..733H. 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 Journal. 6 (7): 2482–2486. doi:10.1096/fasebj.6.7.1532945. PMID 1532945. S2CID 29899093.
- 1 2 "Entrez Gene: FKBP3 FK506 binding protein 3, 25kDa".
- 1 2 Prakash A, Rajan S, Yoon HS (April 2016). "Crystal structure of the FK506 binding domain of human FKBP25 in complex with FK506". Protein Science. 25 (4): 905–910. doi:10.1002/pro.2875. PMC 4941220. PMID 26749369.
- 1 2 3 Yang WM, Yao YL, Seto E (September 2001). "The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1". The EMBO Journal. 20 (17): 4814–4825. doi:10.1093/emboj/20.17.4814. PMC 125595. PMID 11532945.
- 1 2 Prakash A, Shin J, Rajan S, Yoon HS (2016). "Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin". Nucleic Acids Research. 44 (6): 2909–2925. doi:10.1093/nar/gkw001. PMC 4824100. PMID 26762975.
- ↑ Ochocka AM, Kampanis P, Nicol S, Allende-Vega N, Cox M, Marcar L, et al. (February 2009). "FKBP25, a novel regulator of the p53 pathway, induces the degradation of MDM2 and activation of p53". FEBS Letters. 583 (4): 621–626. Bibcode:2009FEBSL.583..621O. doi:10.1016/j.febslet.2009.01.009. PMID 19166840. S2CID 6110.
Further reading
[edit]- Jin YJ, Burakoff SJ, Bierer BE (1992). "Molecular cloning of a 25-kDa high affinity rapamycin binding protein, FKBP25". The Journal of Biological Chemistry. 267 (16): 10942–10945. 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". Biochemical and Biophysical Research Communications. 185 (1): 298–303. Bibcode:1992BBRC..185..298W. 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". Proceedings of the National Academy of Sciences of the United States of America. 90 (16): 7769–7773. 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". Nature Genetics. 6 (3): 236–244. 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): 171–174. 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): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Meng X, Chen J, Yang Q, Wang S, Chao Y, Ying K, et al. (2002). "Cloning and identification of a novel cDNA which may be associated with FKBP25". Biochemical Genetics. 40 (9–10): 303–310. doi:10.1023/A:1020256718720. PMID 12392168. S2CID 24265377.
- Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–1178. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.