FKBP1A

FK506 binding protein 1A, 12kDa, also known as FKBP1A, is a human gene.

PBB_Summary
section_title =
summary_text = 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 interacts with several intracellular signal transduction proteins including type I TGF-beta receptor. It also interacts with multiple intracellular calcium release channels including the tetrameric skeletal muscle ryanodine receptor. In mouse, deletion of this homologous gene causes congenital heart disorder known as noncompaction of left ventricular myocardium. There is evidence of multiple alternatively spliced transcript variants for this gene, but the full length nature of some variants has not been determined. [cite web | title = Entrez Gene: FKBP1A FK506 binding protein 1A, 12kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2280| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Schiene-Fischer C, Yu C |title=Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases. |journal=FEBS Lett. |volume=495 |issue= 1-2 |pages= 1–6 |year= 2001 |pmid= 11322937 |doi=
*cite journal | author=DiLella AG, Hawkins A, Craig RJ, "et al." |title=Chromosomal band assignments of the genes encoding human FKBP12 and FKBP13. |journal=Biochem. Biophys. Res. Commun. |volume=189 |issue= 2 |pages= 819–23 |year= 1993 |pmid= 1281998 |doi=
*cite journal | author=Jayaraman T, Brillantes AM, Timerman AP, "et al." |title=FK506 binding protein associated with the calcium release channel (ryanodine receptor). |journal=J. Biol. Chem. |volume=267 |issue= 14 |pages= 9474–7 |year= 1992 |pmid= 1374404 |doi=
*cite journal | author=Lepre CA, Thomson JA, Moore JM |title=Solution structure of FK506 bound to FKBP-12. |journal=FEBS Lett. |volume=302 |issue= 1 |pages= 89–96 |year= 1992 |pmid= 1375171 |doi=
*cite journal | author=Maki N, Sekiguchi F, Nishimaki J, "et al." |title=Complementary DNA encoding the human T-cell FK506-binding protein, a peptidylprolyl cis-trans isomerase distinct from cyclophilin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 14 |pages= 5440–3 |year= 1990 |pmid= 1695378 |doi=
*cite journal | author=Standaert RF, Galat A, Verdine GL, Schreiber SL |title=Molecular cloning and overexpression of the human FK506-binding protein FKBP. |journal=Nature |volume=346 |issue= 6285 |pages= 671–4 |year= 1990 |pmid= 1696686 |doi= 10.1038/346671a0
*cite journal | author=Siekierka JJ, Wiederrecht G, Greulich H, "et al." |title=The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase. |journal=J. Biol. Chem. |volume=265 |issue= 34 |pages= 21011–5 |year= 1991 |pmid= 1701173 |doi=
*cite journal | author=Michnick SW, Rosen MK, Wandless TJ, "et al." |title=Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin. |journal=Science |volume=252 |issue= 5007 |pages= 836–9 |year= 1991 |pmid= 1709301 |doi=
*cite journal | author=Van Duyne GD, Standaert RF, Karplus PA, "et al." |title=Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex. |journal=Science |volume=252 |issue= 5007 |pages= 839–42 |year= 1991 |pmid= 1709302 |doi=
*cite journal | author=Rosen MK, Michnick SW, Karplus M, Schreiber SL |title=Proton and nitrogen sequential assignments and secondary structure determination of the human FK506 and rapamycin binding protein. |journal=Biochemistry |volume=30 |issue= 19 |pages= 4774–89 |year= 1991 |pmid= 1709363 |doi=
*cite journal | author=Jin YJ, Albers MW, Lane WS, "et al." |title=Molecular cloning of a membrane-associated human FK506- and rapamycin-binding protein, FKBP-13. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 15 |pages= 6677–81 |year= 1991 |pmid= 1713687 |doi=
*cite journal | author=DiLella AG, Craig RJ |title=Exon organization of the human FKBP-12 gene: correlation with structural and functional protein domains. |journal=Biochemistry |volume=30 |issue= 35 |pages= 8512–7 |year= 1991 |pmid= 1716149 |doi=
*cite journal | author=DiLella AG |title=Chromosomal assignment of the human immunophilin FKBP-12 gene. |journal=Biochem. Biophys. Res. Commun. |volume=179 |issue= 3 |pages= 1427–33 |year= 1991 |pmid= 1930186 |doi=
*cite journal | author=Harding MW, Galat A, Uehling DE, Schreiber SL |title=A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase. |journal=Nature |volume=341 |issue= 6244 |pages= 758–60 |year= 1989 |pmid= 2477715 |doi= 10.1038/341758a0
*cite journal | author=Wang T, Donahoe PK, Zervos AS |title=Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12. |journal=Science |volume=265 |issue= 5172 |pages= 674–6 |year= 1994 |pmid= 7518616 |doi=
*cite journal | author=Peattie DA, Hsiao K, Benasutti M, Lippke JA |title=Three distinct messenger RNAs can encode the human immunosuppressant-binding protein FKBP12. |journal=Gene |volume=150 |issue= 2 |pages= 251–7 |year= 1995 |pmid= 7529739 |doi=
*cite journal | author=Yang WM, Inouye CJ, Seto E |title=Cyclophilin A and FKBP12 interact with YY1 and alter its transcriptional activity. |journal=J. Biol. Chem. |volume=270 |issue= 25 |pages= 15187–93 |year= 1995 |pmid= 7541038 |doi=
*cite journal | author=Kawamura A, Su MS |title=Interaction of FKBP12-FK506 with calcineurin A at the B subunit-binding domain. |journal=J. Biol. Chem. |volume=270 |issue= 26 |pages= 15463–6 |year= 1995 |pmid= 7541044 |doi=
*cite journal | author=Griffith JP, Kim JL, Kim EE, "et al." |title=X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex. |journal=Cell |volume=82 |issue= 3 |pages= 507–22 |year= 1995 |pmid= 7543369 |doi=
*cite journal | author=Van Duyne GD, Standaert RF, Karplus PA, "et al." |title=Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. |journal=J. Mol. Biol. |volume=229 |issue= 1 |pages= 105–24 |year= 1993 |pmid= 7678431 |doi= 10.1006/jmbi.1993.1012

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