Pathway candidateNCBI-verifiedprotein-coding

PPID

peptidylprolyl isomerase D

NCBI Gene: 5481 Ensembl GeneCards UniProt: Q08752

Pathway candidate — not linked to PFS or PSSD by any record here

PPID is in the library because it belongs to the receptor chaperones family. No study, report or commentary in the corpus names it, so a variant in PPID is not, by itself, evidence of anything related to post-drug syndromes.

Gene summary

A protein-coding gene on chromosome 4 (steroid receptor chaperones). 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.

Source: NCBI Gene, accessed 2026-10-07.

Protein reference (UniProt)

Protein: Peptidyl-prolyl cis-trans isomerase D
Function (excerpt): 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.
Subcellular location: Cytoplasm; Nucleus, nucleolus; Nucleus, nucleoplasm.
Tissue specificity: Widely expressed.

Source: UniProtKB/Swiss-Prot Q08752, release 2026_03, licensed CC BY 4.0. This is the protein’s normal biology, not evidence about post-drug syndromes; associated conditions are inherited disorders of the gene, not PFS, PSSD or PRSD.

Why its pathway is in the library

Chaperone/co-chaperone control of steroid-receptor folding and sensitivity is a regulatory layer above the receptors themselves, tied to stress-axis signaling.

Written for the whole receptor chaperones family, not for PPID specifically.

Mentioned in 0 corpus records

No corpus record names PPID directly yet. It is in the library because it sits in a pathway the corpus tracks (Receptor chaperones).

Also in steroid receptor chaperones

All 14 genes

Browse by family on the gene families page.

Gene summary

Source: NCBI Gene, accessed 2026-10-07.

Protein reference (UniProt)

Protein: Peptidyl-prolyl cis-trans isomerase D
Function (excerpt): 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.
Subcellular location: Cytoplasm; Nucleus, nucleolus; Nucleus, nucleoplasm.
Tissue specificity: Widely expressed.