FKBP1B

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FK506 binding protein 1B, 12.6 kDa
PDB rendering based on 1c9h.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols FKBP1B ; FKBP12.6; FKBP1L; FKBP9; OTK4; PKBP1L; PPIase
External IDs Template:OMIM5 Template:MGI HomoloGene68380
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

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]

References

  1. 1.0 1.1 "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. 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.

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