FKBP1B

FK506 binding protein 1B, 12.6 kDa
PDB rendering based on 1c9h.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1C9H​, 3J8E​, 4C02​, 4IQ2​, 4IQC​
Identifiers
Symbols	FKBP1B ; FKBP12.6; FKBP1L; OTK4; PKBP1L; PPIase
External IDs	OMIM: 600620 MGI: 1336205 HomoloGene: 68380 ChEMBL: 2430 GeneCards: FKBP1B Gene
EC number	5.2.1.8
Gene ontology Molecular function • peptidyl-prolyl cis-trans isomerase activity • receptor binding • ryanodine-sensitive calcium-release channel activity • protein binding • FK506 binding • calcium channel inhibitor activity • cyclic nucleotide binding • ion channel binding Cellular component • cytoplasm • cytosol • membrane • Z disc • sarcoplasmic reticulum membrane • calcium channel complex Biological process • protein peptidyl-prolyl isomerization • 'de novo' protein folding • smooth muscle contraction • response to glucose • negative regulation of heart rate • regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum • regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion • release of sequestered calcium ion into cytosol by sarcoplasmic reticulum • neuronal action potential propagation • protein maturation by protein folding • insulin secretion • negative regulation of protein phosphatase type 2B activity • response to vitamin E • ion transmembrane transport • calcium-mediated signaling using intracellular calcium source • protein refolding • T cell proliferation • response to hydrogen peroxide • positive regulation of axon regeneration • negative regulation of release of sequestered calcium ion into cytosol • positive regulation of sequestering of calcium ion • cytosolic calcium ion homeostasis • response to redox state • transmembrane transport • regulation of ryanodine-sensitive calcium-release channel activity • negative regulation of ryanodine-sensitive calcium-release channel activity • chaperone-mediated protein folding • negative regulation of insulin secretion involved in cellular response to glucose stimulus • calcium ion transmembrane transport • cell communication by electrical coupling involved in cardiac conduction Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2281	14226
Ensembl	ENSG00000119782	ENSMUSG00000020635
UniProt	P68106	Q9Z2I2
RefSeq (mRNA)	NM_004116	NM_016863
RefSeq (protein)	NP_004107	NP_058559
Location (UCSC)	Chr 2: 24.05 – 24.06 Mb	Chr 12: 4.83 – 4.84 Mb
PubMed search

Peptidyl-prolyl cis-trans isomerase FKBP1B is an enzyme that in humans is encoded by the FKBP1B gene.^[1][2]

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 (tacrolimus) and rapamycin (sirolimus). It is highly similar to the FK506-binding protein 1A. Its physiological role is thought to be in excitation-contraction coupling in cardiac muscle. There are two alternatively spliced transcript variants of this gene encoding different isoforms.^[2]

References

1. Arakawa H, Nagase H, Hayashi N, Fujiwara T, Ogawa M, Shin S, Nakamura Y (Jun 1994). "Molecular cloning and expression of a novel human gene that is highly homologous to human FK506-binding protein 12kDa (hFKBP-12) and characterization of two alternatively spliced transcripts". Biochem Biophys Res Commun 200 (2): 836–43. doi:10.1006/bbrc.1994.1527. PMID 7513996.
2. "Entrez Gene: FKBP1B FK506 binding protein 1B, 12.6 kDa".

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. doi:10.1016/S0014-5793(01)02326-2. PMID 11322937.
• Lam E, Martin MM, Timerman AP; et al. (1995). "A novel FK506 binding protein can mediate the immunosuppressive effects of FK506 and is associated with the cardiac ryanodine receptor.". J. Biol. Chem. 270 (44): 26511–22. doi:10.1074/jbc.270.44.26511. PMID 7592869.
• Noguchi N, Takasawa S, Nata K; et al. (1997). "Cyclic ADP-ribose binds to FK506-binding protein 12.6 to release Ca2+ from islet microsomes.". J. Biol. Chem. 272 (6): 3133–6. doi:10.1074/jbc.272.6.3133. PMID 9013543.
• Deivanayagam CC, Carson M, Thotakura A; et al. (2000). "Structure of FKBP12.6 in complex with rapamycin.". Acta Crystallogr. D Biol. Crystallogr. 56 (Pt 3): 266–71. doi:10.1107/S0907444999016571. PMID 10713512.
• Marx SO, Reiken S, Hisamatsu Y; et al. (2000). "PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts.". Cell 101 (4): 365–76. doi:10.1016/S0092-8674(00)80847-8. PMID 10830164.
• Jeyakumar LH, Ballester L, Cheng DS; et al. (2001). "FKBP binding characteristics of cardiac microsomes from diverse vertebrates.". Biochem. Biophys. Res. Commun. 281 (4): 979–86. doi:10.1006/bbrc.2001.4444. PMID 11237759.
• George CH, Sorathia R, Bertrand BM, Lai FA (2003). "In situ modulation of the human cardiac ryanodine receptor (hRyR2) by FKBP12.6.". Biochem. J. 370 (Pt 2): 579–89. doi:10.1042/BJ20021433. PMC 1223191. PMID 12443530.
• Masumiya H, Wang R, Zhang J; et al. (2003). "Localization of the 12.6-kDa FK506-binding protein (FKBP12.6) binding site to the NH2-terminal domain of the cardiac Ca2+ release channel (ryanodine receptor).". J. Biol. Chem. 278 (6): 3786–92. doi:10.1074/jbc.M210962200. PMID 12446682.
• Tiso N, Salamon M, Bagattin A; et al. (2003). "The binding of the RyR2 calcium channel to its gating protein FKBP12.6 is oppositely affected by ARVD2 and VTSIP mutations.". Biochem. Biophys. Res. Commun. 299 (4): 594–8. doi:10.1016/S0006-291X(02)02689-X. PMID 12459180.
• 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.
• George CH, Higgs GV, Mackrill JJ, Lai FA (2003). "Dysregulated ryanodine receptors mediate cellular toxicity: restoration of normal phenotype by FKBP12.6.". J. Biol. Chem. 278 (31): 28856–64. doi:10.1074/jbc.M212440200. PMID 12754204.
• Nishanian TG, Waldman T (2004). "Interaction of the BMPR-IA tumor suppressor with a developmentally relevant splicing factor.". Biochem. Biophys. Res. Commun. 323 (1): 91–7. doi:10.1016/j.bbrc.2004.08.060. PMID 15351706.
• 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.
• Maalej A, Mbarki F, Rebai A; et al. (2005). "Evidence of association between FKBP1B and thyroid autoimmune disorders in a large Tunisian family.". Autoimmunity 37 (3): 237–9. doi:10.1080/08916930410001702478. PMID 15497458.
• Zissimopoulos S, Lai FA (2005). "Interaction of FKBP12.6 with the cardiac ryanodine receptor C-terminal domain.". J. Biol. Chem. 280 (7): 5475–85. doi:10.1074/jbc.M412954200. PMID 15591045.
• Aizawa Y, Ueda K, Komura S; et al. (2005). "A novel mutation in FKBP12.6 binding region of the human cardiac ryanodine receptor gene (R2401H) in a Japanese patient with catecholaminergic polymorphic ventricular tachycardia.". Int. J. Cardiol. 99 (2): 343–5. doi:10.1016/j.ijcard.2003.11.050. PMID 15749201.
• Wehrens XH, Lehnart SE, Reiken S; et al. (2005). "Enhancing calstabin binding to ryanodine receptors improves cardiac and skeletal muscle function in heart failure.". Proc. Natl. Acad. Sci. U.S.A. 102 (27): 9607–12. doi:10.1073/pnas.0500353102. PMC 1172237. PMID 15972811.
• 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. (Retracted. If this is intentional, please replace {{Retracted}} with {{Retracted|intentional=yes}}.)