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). .
Expressed in immune cells in the lung (at protein level) (PubMed:29686383). The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells.
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