PPID report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0061077Biological processchaperone-mediated protein folding
GO_0000122Biological processnegative regulation of transcription by RNA polymerase II
GO_0045070Biological processpositive regulation of viral genome replication
GO_0065003Biological processprotein-containing complex assembly
GO_0050714Biological processpositive regulation of protein secretion
GO_0006457Biological processprotein folding
GO_0034389Biological processlipid droplet organization
GO_0019076Biological processviral release from host cell
GO_0006915Biological processapoptotic process
GO_0015031Biological processprotein transport
GO_0043065Biological processpositive regulation of apoptotic process
GO_0071492Biological processcellular response to UV-A
GO_0000413Biological processprotein peptidyl-prolyl isomerization
GO_0005730Cellular componentnucleolus
GO_0005654Cellular componentnucleoplasm
GO_0005829Cellular componentcytosol
GO_0005737Cellular componentcytoplasm
GO_0005634Cellular componentnucleus
GO_0008134Molecular functiontranscription factor binding
GO_0003755Molecular functionpeptidyl-prolyl cis-trans isomerase activity
GO_0051879Molecular functionHsp90 protein binding
GO_0031072Molecular functionheat shock protein binding
GO_0030331Molecular functionnuclear estrogen receptor binding
GO_0030544Molecular functionHsp70 protein binding
GO_0005515Molecular functionprotein binding
GO_0016018Molecular functioncyclosporin A binding

IV. Literature review

[source]
Gene namePPID
Protein namePeptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8)
Peptidylprolyl isomerase D
Peptidyl-prolyl cis-trans isomerase D (PPIase D) (EC 5.2.1.8) (40 kDa peptidyl-prolyl cis-trans isomerase) (Cyclophilin-40) (CYP-40) (Cyclophilin-related protein) (Rotamase D)
peptidylprolyl isomerase (EC 5.2.1.8)
SynonymsCYPD
CYP40
DescriptionFUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding . Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis. Promotes cell viability in anaplastic lymphoma kinase-positive anaplastic large-cell lymphoma (ALK+ ALCL) cell lines. .; FUNCTION: (Microbial infection) May be involved in hepatitis C virus (HCV) replication and release. .

FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. .

AccessionsH0Y8J0
Q6FGM6
ENST00000512699.1
Q08752
ENST00000507213.1
H0Y969
ENST00000307720.4
Q05DH6