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Descriptor English: NIMA-Interacting Peptidylprolyl Isomerase
Descriptor Spanish: Peptidilprolil Isomerasa de Interacción con NIMA
Descriptor peptidilprolil isomerasa de interacción con NIMA
Entry term(s) peptidil-prolil cis-trans isomerasa Pin1
peptidilprolil isomerasa Pin1
proteína PIN1
Scope note: Isomerasa peptidil-prolil cis-trans (PPlasa) muy conservada que se une e isomeriza motivos específicos SERINA o TREONINA- PROLINA (pSer-Thr-Pro) y produce cambios conformacionales en algunas proteínas asociadas al CICLO CELULAR. Muestra preferencia por un residuo ácido N-terminal, en lugar de por el enlace de prolina isomerizada, y regula la MITOSIS, posiblemente atenuando la actividad promotora de la mitosis de la QUINASA 1 RELACIONADA CON NIMA.
Descriptor Portuguese: Peptidilprolil Isomerase de Interação com NIMA
Descriptor French: NIMA-interacting peptidylprolyl isomerase
Entry term(s): Isomerase, NIMA-Interacting Peptidylprolyl
Isomerase, Pin1 Peptidylprolyl
NIMA Interacting Peptidylprolyl Isomerase
PIN1 Protein
Peptidyl Prolyl Cis Trans Isomerase Pin1
Peptidyl-Prolyl Cis-Trans Isomerase Pin1
Peptidylprolyl Isomerase, NIMA-Interacting
Peptidylprolyl Isomerase, Pin1
Pin1 Peptidylprolyl Isomerase
Tree number(s): D08.811.399.325.500.700
RDF Unique Identifier: https://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.
Allowable Qualifiers: AD administration & dosage
AE adverse effects
AI antagonists & inhibitors
AN analysis
BI biosynthesis
BL blood
CF cerebrospinal fluid
CH chemistry
CL classification
CS chemical synthesis
DE drug effects
DF deficiency
EC economics
GE genetics
HI history
IM immunology
IP isolation & purification
ME metabolism
PD pharmacology
PH physiology
PK pharmacokinetics
PO poisoning
RE radiation effects
SD supply & distribution
ST standards
TO toxicity
TU therapeutic use
UL ultrastructure
UR urine
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)
DeCS ID: 56495
Unique ID: D000072340
Documents indexed in the Virtual Health Library (VHL): Click here to access the VHL documents
Date Established: 2017/01/01
Date of Entry: 2016/07/08
Revision Date: 2016/05/27
NIMA-Interacting Peptidylprolyl Isomerase - Preferred
Concept UI M0502575
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.
Preferred term NIMA-Interacting Peptidylprolyl Isomerase
Entry term(s) Isomerase, NIMA-Interacting Peptidylprolyl
Isomerase, Pin1 Peptidylprolyl
NIMA Interacting Peptidylprolyl Isomerase
PIN1 Protein
Peptidyl Prolyl Cis Trans Isomerase Pin1
Peptidyl-Prolyl Cis-Trans Isomerase Pin1
Peptidylprolyl Isomerase, NIMA-Interacting
Peptidylprolyl Isomerase, Pin1
Pin1 Peptidylprolyl Isomerase



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