FKBP1B

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1C9H, 3J8E, 4C02, 4IQ2, 4IQC

Identifiers

Aliases

FKBP1B, FKBP12.6, FKBP1L, OTK4, PKBP1L, PPIase, FK506 binding protein 1B

External IDs

MGI: 1336205 HomoloGene: 68380 GeneCards: FKBP1B

Gene ontology
Molecular function	• ryanodine-sensitive calcium-release channel activity • calcium channel inhibitor activity • ion channel binding • FK506 binding • isomerase activity • peptidyl-prolyl cis-trans isomerase activity • protein binding • receptor binding • cyclic nucleotide binding
Cellular component	• cytoplasm • cytosol • calcium channel complex • intracellular membrane-bounded organelle • membrane • sarcoplasmic reticulum • Z disc • sarcoplasmic reticulum membrane
Biological process	• smooth muscle contraction • regulation of ryanodine-sensitive calcium-release channel activity • release of sequestered calcium ion into cytosol • regulation of cardiac conduction • release of sequestered calcium ion into cytosol by sarcoplasmic reticulum • regulation of cytosolic calcium ion concentration • regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion • positive regulation of cytosolic calcium ion concentration • cell communication by electrical coupling involved in cardiac conduction • negative regulation of insulin secretion involved in cellular response to glucose stimulus • insulin secretion • response to glucose • positive regulation of axon regeneration • protein maturation by protein folding • response to organic substance • negative regulation of heart rate • response to vitamin E • regulation of heart rate • negative regulation of ryanodine-sensitive calcium-release channel activity • response to redox state • T cell proliferation • ion transmembrane transport • positive regulation of sequestering of calcium ion • protein folding • neuronal action potential propagation • protein refolding • negative regulation of protein phosphatase type 2B activity • negative regulation of release of sequestered calcium ion into cytosol • regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum • 'de novo' protein folding • calcium-mediated signaling using intracellular calcium source • response to hydrogen peroxide • chaperone-mediated protein folding • protein peptidyl-prolyl isomerization
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_054033 NM_001322963 NM_001322964


NM_016863

RefSeq (protein)


NP_004107.1 NP_473374.1


NP_058559.3

Location (UCSC)

Chr 2: 24.05 – 24.06 Mb

Chr 12: 4.83 – 4.84 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Peptidyl-prolyl cis-trans isomerase FKBP1B is an enzyme that in humans is encoded by the FKBP1B gene.^[3]^[4]

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.^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
1 2 "Entrez Gene: FKBP1B FK506 binding protein 1B, 12.6 kDa".

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. 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}}.)

PDB gallery

1c9h: CRYSTAL STRUCTURE OF FKBP12.6 IN COMPLEX WITH RAPAMYCIN

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

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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FKBP1B

References

Further reading