"Cyclophilin D" redirects here. Not to be confused with peptidyl-prolyl cis-trans isomerase, mitochondrial (PPIF), which may also be referred to as Cyclophilin D.
negative regulation of transcription by RNA polymerase II
protein folding
positive regulation of protein secretion
positive regulation of apoptotic process
protein transport
positive regulation of viral genome replication
apoptotic process
protein-containing complex assembly
protein peptidyl-prolyl isomerization
protein refolding
negative regulation of apoptotic process
regulation of mitochondrial membrane potential
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
5481
67738
Ensembl
ENSG00000171497
ENSMUSG00000027804
UniProt
Q08752
Q9CR16
RefSeq (mRNA)
NM_005038
NM_026352 NM_001356326
RefSeq (protein)
NP_005029
NP_080628 NP_001343255
Location (UCSC)
Chr 4: 158.71 – 158.72 Mb
Chr 3: 79.5 – 79.51 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Peptidylprolyl isomerase D (cyclophilin D), also known as PPID, is an enzyme which in humans is encoded by the PPID gene on chromosome 4. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to facilitate folding or repair of proteins.[5] In addition, PPID participates in many biological processes, including mitochondrial metabolism, apoptosis, redox, and inflammation, as well as in related diseases and conditions, such as ischemic reperfusion injury, AIDS, and cancer.[6][7][8][9]
^ abcGRCh38: Ensembl release 89: ENSG00000171497 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000027804 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Entrez Gene: PPID peptidylprolyl isomerase D (cyclophilin D)".
^Kazui T, Inoue N, Yamada O, Komatsu S (Jan 1992). "Selective cerebral perfusion during operation for aneurysms of the aortic arch: a reassessment". The Annals of Thoracic Surgery. 53 (1): 109–14. doi:10.1016/0003-4975(92)90767-x. PMID 1530810.
^Yao Q, Li M, Yang H, Chai H, Fisher W, Chen C (Mar 2005). "Roles of cyclophilins in cancers and other organ systems". World Journal of Surgery. 29 (3): 276–80. doi:10.1007/s00268-004-7812-7. PMID 15706440. S2CID 11678319.
^Wang T, Yun CH, Gu SY, Chang WR, Liang DC (Aug 2005). "1.88 A crystal structure of the C domain of hCyP33: a novel domain of peptidyl-prolyl cis-trans isomerase". Biochemical and Biophysical Research Communications. 333 (3): 845–9. doi:10.1016/j.bbrc.2005.06.006. PMID 15963461.
^Stocki P, Chapman DC, Beach LA, Williams DB (Aug 2014). "Depletion of cyclophilins B and C leads to dysregulation of endoplasmic reticulum redox homeostasis". The Journal of Biological Chemistry. 289 (33): 23086–96. doi:10.1074/jbc.M114.570911. PMC 4132807. PMID 24990953.
and 22 Related for: Peptidylprolyl isomerase D information
Peptidylprolylisomerase A (PPIA), also known as cyclophilin A (CypA) or rotamase A is an enzyme that in humans is encoded by the PPIA gene on chromosome...
PPID may refer to: PeptidylprolylisomeraseD, and enzyme encoded within the PPID gene Pituitary pars intermedia dysfunction in horses. Private Personal...
In biochemistry, isomerases are a general class of enzymes that convert a molecule from one isomer to another. Isomerases facilitate intramolecular rearrangements...
PPIL4, PPIAL4, PPIL6 PPWD1 Cyclophilin A (CYPA) also known as peptidylprolylisomerase A (PPIA), which is found in the cytosol, has a beta barrel structure...
cis-trans isomerase-like 2 is an enzyme that in humans is encoded by the PPIL2 gene. This gene is a member of the cyclophilin family of peptidylprolyl isomerases...
(Jul 2001). "Molecular cloning and characterization of a novel peptidylprolylisomerase (cyclophilin)-like gene (PPIL3) from human fetal brain". Cytogenetics...
8218–24. doi:10.1021/bi00193a007. PMID 8031755. "Entrez Gene: PPIC peptidylprolylisomerase C (cyclophilin C)". Kazui T, Inoue N, Yamada O, Komatsu S (Jan...
PMID 8606777. S2CID 4258406. "Entrez Gene: PIN1 Protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1". da Costa KS, Galúcio JM, de Jesus DA...
"Complementary DNA encoding the human T-cell FK506-binding protein, a peptidylprolyl cis-trans isomerase distinct from cyclophilin". Proceedings of the National Academy...
protein disulfide isomerase (PDI), ERp29, the Hsp70 family member BiP/Grp78, calnexin, calreticulin, and the peptidylprolylisomerase family. Only properly...
the dephosphorylation of NF-AT. In detail, tacrolimus reduces peptidylprolylisomerase activity by binding to the immunophilin FKBP12 (FK506 binding protein)...
Renoir JM, Housley PR, Pratt WB (May 2001). "Evidence that the peptidylprolylisomerase domain of the hsp90-binding immunophilin FKBP52 is involved in...
mapping and identification of a mutation in the gene coding for peptidylprolylisomerase B, was published on May 11, 2007. Concurrent with publication of...
the structural information available in the PDB for UniProt: Q9C035 (Tripartite motif-containing protein 5) at the PDBe-KB. Peptidylprolylisomerase A...
biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases". PLOS Biol. 8 (7): e1000439. doi:10.1371/journal.pbio.1000439. PMC 2911226...
the inner and outer mitochondrial membranes, are still unknown. Peptidylprolylisomerase F (CYPD) is the only known required protein for MPT-driven necrosis...
individuals with bipolar disorder had lower methylation of the peptidylprolylisomerase E-like (PPIEL) gene, which can be attributed to the dopamine transmission...
isoelectric point and molecular weight of human ccdc190 isoform 1 are 9.62 and 34kD. Also, based on the analysis of SAPS, this protein seems to have more lysine...
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