PPID

Entrez Summary: N/A
UniProt Summary: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. 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. May be involved in hepatitis C virus (HCV) replication and release. {ECO:0000269|PubMed:11350175, ECO:0000269|PubMed:18708059, ECO:0000269|PubMed:19932913, ECO:0000269|PubMed:21711559, ECO:0000269|PubMed:22681779, ECO:0000269|PubMed:23220213, ECO:0000269|PubMed:9659917}.

Pfam Domains GO Terms

Compound Hit Most Correlated Genes in Chemogenomics Tissues where Essential in the Avana Dataset (DepMap 20Q1)

Global Fraction of Cell Lines Where Essential: 0/739

Tissue	Fraction Of Cell Lines Where Essential
1290807.0	0/1
909776.0	0/1
bile duct	0/28
blood	0/28
bone	0/26
breast	0/33
central nervous system	0/56
cervix	0/4
colorectal	0/17
esophagus	0/13
fibroblast	0/1
gastric	0/16
kidney	0/21
liver	0/20
lung	0/75
lymphocyte	0/16
ovary	0/26
pancreas	0/24
peripheral nervous system	0/16
plasma cell	0/15
prostate	0/1
skin	0/24
soft tissue	0/9
thyroid	0/2
upper aerodigestive	0/22
urinary tract	0/29
uterus	0/5

Expression Distribution

cellular response to UV-A
viral release from host cell
response to UV-A
exit from host
movement in environment of other organism involved in symbiotic interaction
movement in host environment
exit from host cell
lipid droplet organization
cyclosporin A binding
positive regulation of viral genome replication
protein refolding
Hsp90 protein binding
Hsp70 protein binding
estrogen receptor binding
peptidyl-prolyl cis-trans isomerase activity
protein peptidyl-prolyl isomerization
chaperone-mediated protein folding
heat shock protein binding
peptidyl-proline modification
positive regulation of viral life cycle
cellular response to UV
regulation of viral genome replication
positive regulation of viral process
cellular response to light stimulus
unfolded protein binding
response to UV
regulation of viral life cycle
interaction with host
cellular response to radiation
viral life cycle
regulation of viral process
regulation of symbiosis, encompassing mutualism through parasitism
protein folding
positive regulation of protein secretion
positive regulation of peptide secretion
response to light stimulus
cellular response to abiotic stimulus
cellular response to environmental stimulus
transcription factor binding
positive regulation of secretion by cell