PPID

Peptidylprolyl isomerase D (cyclophilin D)
File:PBB Protein PPID image.jpg PDB rendering based on 1ihg.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1ihg​, 1iip​
Identifiers
Symbols	PPID ; CYP-40; CYPD; MGC33096
External IDs	Template:OMIM5 Template:MGI HomoloGene: 31283
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO
RNA expression pattern
File:PBB GE PPID 204186 s at tn.png
File:PBB GE PPID 204185 x at tn.png
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

PPID may also refer to Private Personal Identifier, a standard SAML assertion.

Peptidylprolyl isomerase D (cyclophilin D), also known as PPID, is a human gene.

The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein has been shown to possess PPIase activity and, similar to other family members, can bind to the immunosuppressant cyclosporin A.

Further reading

• Kieffer LJ, Thalhammer T, Handschumacher RE (1992). "Isolation and characterization of a 40-kDa cyclophilin-related protein". J. Biol. Chem. 267 (8): 5503–7. PMID 1544925.CS1 maint: Multiple names: authors list (link)
• Hoffmann K, Kakalis LT, Anderson KS; et al. (1995). "Expression of human cyclophilin-40 and the effect of the His141-->Trp mutation on catalysis and cyclosporin A binding". Eur. J. Biochem. 229 (1): 188–93. PMID 7744028.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kieffer LJ, Seng TW, Li W; et al. (1993). "Cyclophilin-40, a protein with homology to the P59 component of the steroid receptor complex. Cloning of the cDNA and further characterization". J. Biol. Chem. 268 (17): 12303–10. PMID 8509368.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yokoi H, Shimizu Y, Anazawa H; et al. (1996). "The structure and complete nucleotide sequence of the human cyclophilin 40 (PPID) gene". Genomics. 35 (3): 448–55. doi:10.1006/geno.1996.0384. PMID 8812478.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. PMID 8889548.CS1 maint: Multiple names: authors list (link)
• Silverstein AM, Galigniana MD, Chen MS; et al. (1997). "Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin". J. Biol. Chem. 272 (26): 16224–30. PMID 9195923.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Young JC, Obermann WM, Hartl FU (1998). "Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90". J. Biol. Chem. 273 (29): 18007–10. PMID 9660753.CS1 maint: Multiple names: authors list (link)
• Mark PJ, Ward BK, Kumar P; et al. (2001). "Human cyclophilin 40 is a heat shock protein that exhibits altered intracellular localization following heat shock". Cell Stress Chaperones. 6 (1): 59–70. PMID 11525244.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ward BK, Allan RK, Mok D; et al. (2002). "A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90". J. Biol. Chem. 277 (43): 40799–809. doi:10.1074/jbc.M207097200. PMID 12145316.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• McStay GP, Clarke SJ, Halestrap AP (2002). "Role of critical thiol groups on the matrix surface of the adenine nucleotide translocase in the mechanism of the mitochondrial permeability transition pore". Biochem. J. 367 (Pt 2): 541–8. doi:10.1042/BJ20011672. PMID 12149099.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gevaert K, Goethals M, Martens L; et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Schubert A, Grimm S (2004). "Cyclophilin D, a component of the permeability transition-pore, is an apoptosis repressor". Cancer Res. 64 (1): 85–93. PMID 14729611.
• Machida K, Osada H (2004). "Molecular interaction between cyclophilin D and adenine nucleotide translocase in cytochrome c release: does it determine whether cytochrome c release is dependent on permeability transition or not?". Ann. N. Y. Acad. Sci. 1010: 182–5. PMID 15033717.
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Carrello A, Allan RK, Morgan SL; et al. (2005). "Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70". Cell Stress Chaperones. 9 (2): 167–81. PMID 15497503.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Barrios-Rodiles M, Brown KR, Ozdamar B; et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. doi:10.1126/science.1105776. PMID 15761153.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Machida K, Ohta Y, Osada H (2006). "Suppression of apoptosis by cyclophilin D via stabilization of hexokinase II mitochondrial binding in cancer cells". J. Biol. Chem. 281 (20): 14314–20. doi:10.1074/jbc.M513297200. PMID 16551620.CS1 maint: Multiple names: authors list (link)
• Mok D, Allan RK, Carrello A; et al. (2006). "The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains". FEBS Lett. 580 (11): 2761–8. doi:10.1016/j.febslet.2006.04.039. PMID 16650407.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)