FKBP1B

From Wikipedia, the free encyclopedia

FK506 binding protein 1B, 12.6 kDa

PDB rendering based on 1c9h.

Available structures: 1c9h

Identifiers

Symbol(s)

FKBP1B; FKBP12.6; FKBP1L; FKBP9; OTK4; PKBP1L; PPIase

External IDs

OMIM: 600620 MGI: 1336205 HomoloGene: 68380

Gene ontology
Molecular Function:	• peptidyl-prolyl cis-trans isomerase activity • isomerase activity
Cellular Component:	• cytoplasm
Biological Process:	• protein folding • muscle contraction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004116 (mRNA)
NP_004107 (protein)

NM_016863 (mRNA)
NP_058559 (protein)

Location

Chr 2: 24.13 - 24.14 Mb

Chr 12: 4.86 - 4.86 Mb

Pubmed search

[1]

[2]

FK506 binding protein 1B, 12.6 kDa, also known as FKBP1B, is a human gene.^[1]

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 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.^[1]

[edit] References

^ ^a ^b Entrez Gene: FKBP1B FK506 binding protein 1B, 12.6 kDa.

[edit] 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. PMID 11322937.
Arakawa H, Nagase H, Hayashi N, et al. (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. PMID 7513996.
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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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.