Structured Summary
Abstract
A highly-conserved peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated SERINE- or THREONINE-PROLINE (pSer/Thr-Pro) motifs and causes conformational changes in certain proteins associated with the CELL CYCLE. It displays a preference for an acidic residue N-terminal to the isomerized proline bond and regulates MITOSIS, possibly by attenuating the mitosis-promoting activity of NIMA-RELATED KINASE 1.
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Synonyms
9 entry terms
- PIN1 Protein
- Peptidyl-Prolyl Cis-Trans Isomerase Pin1
- Pin1 Peptidylprolyl Isomerase
- Isomerase, NIMA-Interacting Peptidylprolyl
- Isomerase, Pin1 Peptidylprolyl
- NIMA Interacting Peptidylprolyl Isomerase
- Peptidyl Prolyl Cis Trans Isomerase Pin1
- Peptidylprolyl Isomerase, NIMA-Interacting
- Peptidylprolyl Isomerase, Pin1
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Aspects Covered
29 allowable subheadings
Indexed with the subheadings administration & dosage, adverse effects, analysis, antagonists & inhibitors, biosynthesis, blood, cerebrospinal fluid, chemical synthesis, chemistry, classification, deficiency, drug effects, economics, genetics, history, immunology, isolation & purification, metabolism, pharmacokinetics, pharmacology, physiology, poisoning, radiation effects, standards, supply & distribution, therapeutic use, toxicity, ultrastructure, urine.
MeSH Record
History Note
2017 (1996)
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AMA Style
References
- National Library of Medicine. NIMA-Interacting Peptidylprolyl Isomerase. Medical Subject Headings (MeSH). 2026. Unique ID D000072340. http://id.nlm.nih.gov/mesh/2026/D000072340
- NIMA-Interacting Peptidylprolyl Isomerase. In: Wikidata. https://www.wikidata.org/wiki/Q21116190