Because of a lapse in government funding, the information on this website may not be up to date, transactions submitted via the website may not be processed, and the agency may not be able to respond to inquiries until appropriations are enacted. The NIH Clinical Center (the research hospital of NIH) is open. For more details about its operating status, please visit cc.nih.gov. Updates regarding government operating status and resumption of normal operations can be found at opm.gov.

NLM Logo

NIMA-Interacting Peptidylprolyl Isomerase MeSH Descriptor Data 2025


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 Numbers
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
NIMA-Interacting Peptidylprolyl Isomerase Preferred
page delivered in 0.116s