a member of the parvulin family of peptidyl-prolyl isomerases (PPIase), has been implicated in the G2-M transition of the cell cycle. Has two distinct functional domains: an N-terminal WW domain and a C-terminal PPlase domain. Pin1 interacts with a series of mitotic phosphoproteins, including Plk1, cdc25C and cdc27, catalyzing pSer-Pro or pThr/Pro cis/trans isomerizations. Displays a preference for an acidic residue n-terminal to the isomerized proline bond. Note: This description may include information from UniProtKB.
Protein type: EC 18.104.22.168; Isomerase; Nuclear receptor co-regulator
Molecular Function: beta-catenin binding; GTPase activating protein binding; mitogen-activated protein kinase kinase binding; motor activity; peptidyl-prolyl cis-trans isomerase activity; phosphoserine binding; phosphothreonine binding; protein binding
Biological Process: cell cycle; cytokine and chemokine mediated signaling pathway; innate immune response; negative regulation of interferon type I production; negative regulation of neuron apoptosis; negative regulation of protein binding; negative regulation of protein catabolic process; negative regulation of transforming growth factor beta receptor signaling pathway; neuron differentiation; positive regulation of GTPase activity; positive regulation of neuron apoptosis; positive regulation of protein amino acid dephosphorylation; positive regulation of protein amino acid phosphorylation; positive regulation of transcription from RNA polymerase II promoter; positive regulation of ubiquitin-protein ligase activity; protein peptidyl-prolyl isomerization; protein stabilization; regulation of cytokinesis; regulation of mitosis; synapse organization and biogenesis
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.