NIMA-Interacting Peptidylprolyl Isomerase [peptidylprolylisomerasa Pin1]
- Terms
-
NIMA-interacting 1 peptidyl-prolyl cis-trans isomeráza
NIMA-interacting 1 peptidyl-prolyl cis-trans izomeráza
peptidyl-prolyl cis-trans isomeráza Pin1
peptidyl-prolyl cis-trans izomeráza Pin1
PIN1 protein
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Peptidyl-Prolyl Cis-Trans Isomerase Pin1
Pin1 Peptidylprolyl Isomerase
PIN1 Protein
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.
- DUI
- D000072340 MeSH Browser
- CUI
- M0502575
- History note
- 2017 (1996)
- Public note
- 2017; NIMA-INTERACTING PEPTIDYLPROLYL ISOMERASE was indexed under PEPTIDYLPROLYL ISOMERASE 1997-2016; and under AMINO ACID ISOMERASES 1996-1997
Allowable subheadings
- AD
- administration & dosage
- AE
- adverse effects
- AN
- analysis
- AI
- antagonists & inhibitors
- BI
- biosynthesis
- BL
- blood
- CF
- cerebrospinal fluid
- CS
- chemical synthesis
- CH
- chemistry
- CL
- classification
- DF
- deficiency
- DE
- drug effects
- EC
- economics
- GE
- genetics
- HI
- history
- IM
- immunology
- IP
- isolation & purification
- ME
- metabolism
- PK
- pharmacokinetics
- PD
- pharmacology
- PH
- physiology
- PO
- poisoning
- RE
- radiation effects
- ST
- standards
- SD
- supply & distribution
- TU
- therapeutic use
- TO
- toxicity
- UL
- ultrastructure
- UR
- urine
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