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Beschreibung

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (UniProt: Q13526, also known as EC: 5.2.1.8, Peptidyl-prolyl cis-trans isomerase Pin1, PPIase Pin1, Rotamase Pin1) is encoded by the PIN1 gene (Gene ID: 5300) in human. PPIase binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. Isomerization of phosphorylated Ser or Thr residues may alter protein confirmation and, subsequently, modify activity. By inducing conformational changes in a subset of phosphorylated proteins, it acts as a molecular switch in multiple cellular processes. PPIase is mainly localized in the nucleus, but phosphorylation at Serine 71 by death-associated protein kinase 1 (DAPK1) results in inhibition of its nuclear localization and its catalytic activity. It contains a WW domain (aa 5-39) and a peptidylprolyl isomerase C (PpiC) domain (aa 52-163). WW domain is shown to be essential for the interaction with STIL and KIF20B. PPIase displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. PPIase is reported to regulate mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. It is overexpressed in many human breast cancers, and has been shown to modify numerous proteins including p53, NF-kB, c-Jun, cyclin D1, and beta-catenin.