FKBP1A

From Wikipedia, the free encyclopedia

FK506 binding protein 1A, 12kDa

PDB rendering based on 1a7x.

Available structures: 1a7x, 1b6c, 1bkf, 1bl4, 1d6o, 1d7h, 1d7i, 1d7j, 1eym, 1f40, 1fap, 1fkb, 1fkd, 1fkf, 1fkg, 1fkh, 1fki, 1fkj, 1fkk, 1fkl, 1fkr, 1fks, 1fkt, 1j4h, 1j4i, 1j4r, 1nsg, 1qpf, 1qpl, 1tco, 2dg3, 2dg4, 2dg9, 2fap, 2fke, 3fap, 4fap

Identifiers

Symbol(s)

FKBP1A; FKBP-12; FKBP1; FKBP12; FKBP12C; PKC12; PKCI2; PPIASE

External IDs

OMIM: 186945 MGI: 95541 HomoloGene: 626

Gene ontology
Molecular Function:	• peptidyl-prolyl cis-trans isomerase activity • receptor activity • protein binding • isomerase activity
Biological Process:	• protein folding • positive regulation of I-kappaB kinase/NF-kappaB cascade

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_000801 (mRNA)
NP_000792 (protein)

NM_008019 (mRNA)
NP_032045 (protein)

Location

Chr 20: 1.3 - 1.32 Mb

n/a

Pubmed search

[1]

[2]

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

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.^[1]

[edit] References

^ Entrez Gene: FKBP1A FK506 binding protein 1A, 12kDa.

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