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HMDB Protein ID HMDBP10691
Secondary Accession Numbers
  • 16952
Name Peptidyl-prolyl cis-trans isomerase A
  1. Cyclophilin A
  2. Cyclosporin A-binding protein
  3. PPIase A
  4. Rotamase A
Gene Name PPIA
Protein Type Enzyme
Biological Properties
General Function Involved in peptidyl-prolyl cis-trans isomerase activity
Specific Function 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
catalytic activity
cis-trans isomerase activity
peptidyl-prolyl cis-trans isomerase activity
isomerase activity
metabolic process
macromolecule metabolic process
cellular protein metabolic process
protein folding
protein metabolic process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location Chromosome:7
Locus 7p13
Gene Sequence
>498 bp
Protein Properties
Number of Residues 165
Molecular Weight 18012.4
Theoretical pI 7.97
Pfam Domain Function
  • None
Transmembrane Regions
  • None
Protein Sequence
>Peptidyl-prolyl cis-trans isomerase A
GenBank ID Protein 30309
UniProtKB/Swiss-Prot ID P62937
UniProtKB/Swiss-Prot Entry Name PPIA_HUMAN
GenBank Gene ID Y00052
GeneCard ID PPIA
GenAtlas ID PPIA
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  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. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed:16916647 ]
  4. 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 ]
  5. Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. doi: 10.1021/pr800468j. Epub 2008 Sep 10. [PubMed:18781797 ]
  6. Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J: Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC. Proteomics. 2005 Sep;5(14):3589-99. [PubMed:16097034 ]
  7. Huai Q, Kim HY, Liu Y, Zhao Y, Mondragon A, Liu JO, Ke H: Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. Proc Natl Acad Sci U S A. 2002 Sep 17;99(19):12037-42. Epub 2002 Sep 6. [PubMed:12218175 ]
  8. Jin L, Harrison SC: Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13522-6. Epub 2002 Sep 30. [PubMed:12357034 ]
  9. Haendler B, Hofer-Warbinek R, Hofer E: Complementary DNA for human T-cell cyclophilin. EMBO J. 1987 Apr;6(4):947-50. [PubMed:3297675 ]
  10. Haendler B, Hofer E: Characterization of the human cyclophilin gene and of related processed pseudogenes. Eur J Biochem. 1990 Jul 5;190(3):477-82. [PubMed:2197089 ]
  11. Meier U, Beier-Hellwig K, Klug J, Linder D, Beier HM: Identification of cyclophilin A from human decidual and placental tissue in the first trimester of pregnancy. Hum Reprod. 1995 May;10(5):1305-10. [PubMed:7657784 ]
  12. Liu J, Chen CM, Walsh CT: Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue. Biochemistry. 1991 Mar 5;30(9):2306-10. [PubMed:2001362 ]
  13. Luban J, Bossolt KL, Franke EK, Kalpana GV, Goff SP: Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B. Cell. 1993 Jun 18;73(6):1067-78. [PubMed:8513493 ]
  14. Kallen J, Spitzfaden C, Zurini MG, Wider G, Widmer H, Wuthrich K, Walkinshaw MD: Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy. Nature. 1991 Sep 19;353(6341):276-9. [PubMed:1896075 ]
  15. Ke HM, Zydowsky LD, Liu J, Walsh CT: Crystal structure of recombinant human T-cell cyclophilin A at 2.5 A resolution. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9483-7. [PubMed:1946361 ]
  16. Pflugl G, Kallen J, Schirmer T, Jansonius JN, Zurini MG, Walkinshaw MD: X-ray structure of a decameric cyclophilin-cyclosporin crystal complex. Nature. 1993 Jan 7;361(6407):91-4. [PubMed:8421501 ]
  17. Mikol V, Kallen J, Pflugl G, Walkinshaw MD: X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 A resolution. J Mol Biol. 1993 Dec 20;234(4):1119-30. [PubMed:8263916 ]
  18. Zhao Y, Ke H: Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization. Biochemistry. 1996 Jun 11;35(23):7356-61. [PubMed:8652511 ]
  19. Vajdos FF, Yoo S, Houseweart M, Sundquist WI, Hill CP: Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein. Protein Sci. 1997 Nov;6(11):2297-307. [PubMed:9385632 ]
  20. Kallen J, Mikol V, Taylor P, Walkinshaw MD: X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A. J Mol Biol. 1998 Oct 23;283(2):435-49. [PubMed:9769216 ]
  21. Theriault Y, Logan TM, Meadows R, Yu L, Olejniczak ET, Holzman TF, Simmer RL, Fesik SW: Solution structure of the cyclosporin A/cyclophilin complex by NMR. Nature. 1993 Jan 7;361(6407):88-91. [PubMed:8421500 ]
  22. Ottiger M, Zerbe O, Guntert P, Wuthrich K: The NMR solution conformation of unligated human cyclophilin A. J Mol Biol. 1997 Sep 12;272(1):64-81. [PubMed:9299338 ]