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Showing Protein Peptidyl-prolyl cis-trans isomerase FKBP1A (HMDBP07685)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 5 metabolites
Identification
HMDB Protein ID HMDBP07685
Secondary Accession Numbers
  • 13394
Name Peptidyl-prolyl cis-trans isomerase FKBP1A
Synonyms
  1. 12 kDa FK506-binding protein
  2. 12 kDa FKBP
  3. FK506-binding protein 1A
  4. FKBP-12
  5. FKBP-1A
  6. Immunophilin FKBP12
  7. PPIase FKBP1A
  8. Rotamase
Gene Name FKBP1A
Protein Type Unknown
Biological Properties
General Function Involved in protein folding
Specific Function May play a role in modulation of ryanodine receptor isoform-1 (RYR-1), a component of the calcium release channel of skeletal muscle sarcoplasmic reticulum. There are four molecules of FKBP12 per skeletal muscle RYR. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides
Pathways Not Available
Reactions Not Available
GO Classification
Process
metabolic process
macromolecule metabolic process
cellular protein metabolic process
protein folding
protein metabolic process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location Chromosome:2
Locus 20p13
SNPs FKBP1A
Gene Sequence 
>327 bp
ATGGGAGTGCAGGTGGAAACCATCTCCCCAGGAGACGGGCGCACCTTCCCCAAGCGCGGC
CAGACCTGCGTGGTGCACTACACCGGGATGCTTGAAGATGGAAAGAAATTTGATTCCTCC
CGGGACAGAAACAAGCCCTTTAAGTTTATGCTAGGCAAGCAGGAGGTGATCCGAGGCTGG
GAAGAAGGGGTTGCCCAGATGAGTGTGGGTCAGAGAGCCAAACTGACTATATCTCCAGAT
TATGCCTATGGTGCCACTGGGCACCCAGGCATCATCCCACCACATGCCACTCTCGTCTTC
GATGTGGAGCTTCTAAAACTGGAATGA
Protein Properties
Number of Residues 108
Molecular Weight 11950.7
Theoretical pI 8.48
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>Peptidyl-prolyl cis-trans isomerase FKBP1A
MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGW
EEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P62942
UniProtKB/Swiss-Prot Entry Name FKB1A_HUMAN
PDB IDs
GenBank Gene ID M34539
GeneCard ID FKBP1A
GenAtlas ID FKBP1A
HGNC ID HGNC:3711
References
General References
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  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
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  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed:12665801 ]
  6. Maki N, Sekiguchi F, Nishimaki J, Miwa K, Hayano T, Takahashi N, Suzuki M: 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. 1990 Jul;87(14):5440-3. [PubMed:1695378 ]
  7. Standaert RF, Galat A, Verdine GL, Schreiber SL: Molecular cloning and overexpression of the human FK506-binding protein FKBP. Nature. 1990 Aug 16;346(6285):671-4. [PubMed:1696686 ]
  8. DiLella AG, Craig RJ: Exon organization of the human FKBP-12 gene: correlation with structural and functional protein domains. Biochemistry. 1991 Sep 3;30(35):8512-7. [PubMed:1716149 ]
  9. Peattie DA, Hsiao K, Benasutti M, Lippke JA: Three distinct messenger RNAs can encode the human immunosuppressant-binding protein FKBP12. Gene. 1994 Dec 15;150(2):251-7. [PubMed:7529739 ]
  10. Siekierka JJ, Wiederrecht G, Greulich H, Boulton D, Hung SH, Cryan J, Hodges PJ, Sigal NH: The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase. J Biol Chem. 1990 Dec 5;265(34):21011-5. [PubMed:1701173 ]
  11. Harding MW, Galat A, Uehling DE, Schreiber SL: A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase. Nature. 1989 Oct 26;341(6244):758-60. [PubMed:2477715 ]
  12. Rosen MK, Michnick SW, Karplus M, Schreiber SL: Proton and nitrogen sequential assignments and secondary structure determination of the human FK506 and rapamycin binding protein. Biochemistry. 1991 May 14;30(19):4774-89. [PubMed:1709363 ]
  13. Michnick SW, Rosen MK, Wandless TJ, Karplus M, Schreiber SL: Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin. Science. 1991 May 10;252(5007):836-9. [PubMed:1709301 ]
  14. Lepre CA, Thomson JA, Moore JM: Solution structure of FK506 bound to FKBP-12. FEBS Lett. 1992 May 4;302(1):89-96. [PubMed:1375171 ]
  15. Xu RX, Nettesheim D, Olejniczak ET, Meadows R, Gemmecker G, Fesik SW: 1H, 13C, and 15N assignments and secondary structure of the FK506 binding protein when bound to ascomycin. Biopolymers. 1993 Apr;33(4):535-50. [PubMed:7682113 ]
  16. Van Duyne GD, Standaert RF, Karplus PA, Schreiber SL, Clardy J: Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex. Science. 1991 May 10;252(5007):839-42. [PubMed:1709302 ]
  17. Van Duyne GD, Standaert RF, Karplus PA, Schreiber SL, Clardy J: Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J Mol Biol. 1993 Jan 5;229(1):105-24. [PubMed:7678431 ]
  18. Burkhard P, Taylor P, Walkinshaw MD: X-ray structures of small ligand-FKBP complexes provide an estimate for hydrophobic interaction energies. J Mol Biol. 2000 Jan 28;295(4):953-62. [PubMed:10656803 ]