MeSH Browser

MeSH Heading: NIMA-Interacting Peptidylprolyl Isomerase
Tree Number(s): D08.811.399.325.500.700
Unique ID: D000072340
RDF Unique Identifier: http://id.nlm.nih.gov/mesh/D000072340
Scope Note: 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.
Entry Term(s): PIN1 Protein; Peptidyl-Prolyl Cis-Trans Isomerase Pin1; Pin1 Peptidylprolyl Isomerase
Registry Number: 0
Related Numbers: EC 5.2.1.8
Public MeSH Note: 2017; NIMA-INTERACTING PEPTIDYLPROLYL ISOMERASE was indexed under PEPTIDYLPROLYL ISOMERASE 1997-2016; and under AMINO ACID ISOMERASES 1996-1997
History Note: 2017 (1996)
Date Established: 2017/01/01
Date of Entry: 2016/07/08
Revision Date: 2016/05/27

Allowable Qualifiers: administration & dosage (AD)

adverse effects (AE)

analysis (AN)

antagonists & inhibitors (AI)

biosynthesis (BI)

blood (BL)

cerebrospinal fluid (CF)

chemical synthesis (CS)

chemistry (CH)

classification (CL)

deficiency (DF)

drug effects (DE)

economics (EC)

genetics (GE)

history (HI)

immunology (IM)

isolation & purification (IP)

metabolism (ME)

pharmacokinetics (PK)

pharmacology (PD)

physiology (PH)

poisoning (PO)

radiation effects (RE)

standards (ST)

supply & distribution (SD)

therapeutic use (TU)

toxicity (TO)

ultrastructure (UL)

urine (UR)

Concept UI: M0502575
Registry Number: 0
Related Numbers: EC 5.2.1.8
Scope Note: 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.
Terms: NIMA-Interacting Peptidylprolyl Isomerase Preferred Term
Term UI T000899333
Date04/19/2016
LexicalTag ABX
ThesaurusID NLM (2006); PIN1 Protein
Term UI T000900468
Date05/06/2016
LexicalTag ABX
ThesaurusID NLM (2017); Pin1 Peptidylprolyl Isomerase
Term UI T000899334
Date04/19/2016
LexicalTag ABX
ThesaurusID NLM (2006); Peptidyl-Prolyl Cis-Trans Isomerase Pin1
Term UI T000899332
Date04/19/2016
LexicalTag ABX
ThesaurusID NLM (2017)

NIMA-Interacting Peptidylprolyl Isomerase MeSH Descriptor Data 2024