Pin 1, or peptidyl-prolyl cis/trans isomerase (PPIase), isomerizes only phospho-Serine/Threonine-Proline motifs. The enzyme binds to a subset of proteins and thus plays a role as a post phosphorylation control in regulating protein function. Studies have shown that the deregulation of Pin1 may play a pivotal role in various diseases.

Mar 30, 2025 · PIN1 (Peptidylprolyl Cis/Trans Isomerase, NIMA-Interacting 1) is a Protein Coding gene. Diseases associated with PIN1 include Alzheimer's Disease and Breast Cancer. Among its related pathways are Gene expression (Transcription) and Signaling by Rho GTPases.

Jun 3, 2016 · PIN1 is overactivated in cancers and it promotes cancer and cancer stem cells by disrupting the balance of oncogenes and tumour suppressors.

Pin1 is the only peptidyl–prolyl isomerase (PPIase) that can recognize and isomerize phosphorylated Ser/Thr-Pro peptide bonds. Pin1 catalyzes a structural change in phosphorylated Ser/Thr-Pro motifs that can modulate protein function …

Aug 29, 2018 · Pin1 is the only known peptidyl-prolyl cis – trans isomerase (PPIase) that specifically recognizes and isomerizes the phosphorylated Serine/Threonine-Proline (pSer/Thr-Pro) motif. The...

Apr 5, 2007 · PIN1 is a peptidyl-prolyl isomerase that can alter the conformation of phosphoproteins and so affect protein function and/or stability. PIN1 regulates a number of proteins important for...

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) is an evolutionally conserved and unique enzyme that specifically catalyzes the cis-trans isomerization of phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif and, subsequently, ...

Pin1 promotes EMT progression and disruption of basement membrane, and consequently enhances intravasation of cancer cells into the circulation system. Pin1 enhances the expression of the invasion and metastasis-associated factors leading to increased migration of circulating tumor cells (CTCs).

Pin1 regulates cytokinesis and may under pathologic levels stimulate tumorigenesis. Cytosolic SULT4A1 interacts with PIN1. Pin1 is an important regulator of Rel/NF-kappaB transforming activity and may be a potential therapeutic target in Rel/NF-kappaB-dependent leukemia/lymphomas.

Learn more about PIN1 enzyme research. Visit our website for more details on scientific studies about this substance. Discovering unique signaling mechanisms and therapeutics