Endogenous

PIN1

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

PIN1 ;
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 ;
Peptidyl-prolyl cis-trans isomerase Pin1 ;
PPIase Pin1 ;
Rotamase Pin1

Peptidyl-prolyl cis/trans isomerases (PPIases) catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds. This gene encodes one of the PPIases, which specifically binds to phosphorylated ser/thr-pro motifs to catalytically regulate the post-phosphorylation conformation of its substrates. The conformational regulation catalyzed by this PPIase has a profound impact on key proteins involved in the regulation of cell growth, genotoxic and other stress responses, the immune response, induction and maintenance of pluripotency, germ cell development, neuronal differentiation, and survival. This enzyme also plays a key role in the pathogenesis of Alzheimer's disease and many cancers. Multiple alternatively spliced transcript variants have been found for this gene.[provided by RefSeq, Jun 2011],

Catalytic activity:Peptidylproline (omega=180) = peptidylproline (omega=0).,Domain:The WW domain is required for the interaction with STIL and MPHOSPH1.,Function:Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzing pSer/Thr-Pro cis/trans isomerizations.,PTM:Phosphorylated upon DNA damage, probably by ATM or ATR.,similarity:Contains 1 PpiC domain.,similarity:Contains 1 WW domain.,subunit:Interacts with STIL (By similarity). Interacts with MPHOSPH1.,

Nucleus . Nucleus speckle . Cytoplasm . Colocalizes with NEK6 in the nucleus (PubMed:16476580). Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization (PubMed:21497122). .

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