Target intelligence / Profile preview

Peptidyl-prolyl cis-trans isomerase-like 4 (PPIL4)

Target: PPIL4
Molecular classification: Enzyme, Cyclophilin family (peptidylprolyl isomerase), Protein folding chaperone, RNA-binding protein (contains RNA recognition motif, RRM)

Overview

Peptidyl-prolyl cis-trans isomerase-like 4 is a protein encoded by the human PPIL4 gene on chromosome 6. It belongs to the cyclophilin family of peptidylprolyl isomerases, enzymes that catalyze the cis-trans isomerization of proline bonds in oligopeptides, aiding in rapid protein folding. PPIL4 has a cyclophilin-type isomerase domain, a lysine-rich region, nuclear targeting sequences, and an RNA recognition motif (RRM), indicating potential roles in both protein folding and RNA metabolism or transcriptional regulation. Its activity may have implications in immunosuppression, viral infection, and cancer biology, and it serves experimentally as a putative cancer biomarker.

Other names: Cyclophilin-like protein PPIL4Rotamase PPIL4PPIaseSerologically defined breast cancer antigen NY-BR-18HDCME13PCyclophilin-type peptidyl-prolyl cis-trans isomerasePeptidylprolyl isomerase (cyclophilin)-like 4Peptidyl-prolyl cis-trans isomerase-like 4PPIase (sometimes abbreviated)PPIase, Cyclophilin-like protein PPIL4Peptidylprolyl isomerase like 4

Mechanism of action

Inhibition of peptidyl-prolyl cis-trans isomerase activity (CsA and similar drugs work by binding to cyclophilin isomerase domains and blocking substrate access)

Biological functions

Protein folding (catalyzes cis-trans isomerization of proline residues)Possible transcriptional regulation (due to nuclear localization and presence of RRM domain)Ubiquitous expression, enriched in kidney, localized to nucleus

Disease associations

Cancer (reported as “serologically defined breast cancer antigen NY-BR-18,” indicating relevance as a cancer biomarker)Other (involvement in HIV-1 virion infection observed for cyclophilins, though not uniquely shown for PPIL4)

Safety considerations

Off-target effects due to cyclophilin inhibitor action on multiple family members (not unique to PPIL4 but applicable to cyclophilin-family targeting drugs)Lack of isoform specificity may complicate therapeutic windows and efficacy.No PPIL4-specific safety concerns found in currently available data.

Interacting drugs

Cyclosporin A (CsA), a pan-cyclophilin inhibitor, interacts with the cyclophilin family generally; binding specificity for PPIL4 is less established than for other isoforms but is mechanistically probable due to similar active site architecture

1 more in the full profile.

Biomarkers

NY-BR-18 (serologically defined breast cancer antigen designation)Expression of PPIL4 or cyclophilin activity in tumor samples; not established as a diagnostic biomarker, but antibody development and experimental validation underway

Beyond the preview

Go deeper on Peptidyl-prolyl cis-trans isomerase-like 4 (PPIL4).

Explore the evidence, development activity, and competitive landscape with Gosset’s full data platform.

Drug pipeline

Explore the programs pursuing this target and their development progress.

Drug candidates
Developers
Development stage

Clinical trials

Follow the clinical studies evaluating therapies directed at this target.

Trial design
Status
Readouts

Competitive landscape

Compare approaches across drug candidates, modalities, and indications.

Programs
Modalities
Indications

Literature & evidence

Investigate the research and source evidence behind target biology and development.

Publications
Sources
Analysis

Patents

Explore patent activity around therapies and technologies addressing this target.

Patents
Assignees
Technologies

Research & analysis

Connect target biology, drug development, and emerging evidence in your research.

Biology
Development news
Analysis

Bring the full picture into focus.

See how Gosset can support your research on Peptidyl-prolyl cis-trans isomerase-like 4 (PPIL4).

Explore the full profile