PIN1 Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation. Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner. Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN. May facilitate the ubiquitination and proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR). The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells. Note: This description may include information from UniProtKB.
Protein type: EC; Isomerase; Nuclear receptor co-regulator
Chromosomal Location of Human Ortholog: 19p13.2
Cellular Component:  cytoplasm; cytosol; glutamatergic synapse; midbody; mitochondrion; neuron projection; nuclear speck; nucleoplasm; nucleus; postsynaptic cytosol
Molecular Function:  beta-catenin binding; GTPase activating protein binding; mitogen-activated protein kinase kinase binding; motor activity; peptidyl-prolyl cis-trans isomerase activity; phosphoprotein binding; phosphoserine residue binding; phosphothreonine residue binding; protein binding; tau protein binding
Biological Process:  cell cycle; negative regulation of cell motility; negative regulation of ERK1 and ERK2 cascade; negative regulation of neuron apoptotic process; negative regulation of protein binding; negative regulation of protein catabolic process; negative regulation of transforming growth factor beta receptor signaling pathway; negative regulation of type I interferon production; neuron differentiation; positive regulation of canonical Wnt signaling pathway; positive regulation of cell growth involved in cardiac muscle cell development; positive regulation of GTPase activity; positive regulation of neuron apoptotic process; positive regulation of protein binding; positive regulation of protein dephosphorylation; positive regulation of protein phosphorylation; positive regulation of transcription by RNA polymerase II; positive regulation of ubiquitin-protein transferase activity; protein peptidyl-prolyl isomerization; protein stabilization; regulation of cytokinesis; regulation of gene expression; regulation of mitotic nuclear division; regulation of pathway-restricted SMAD protein phosphorylation; regulation of protein localization to nucleus; regulation of protein phosphorylation; regulation of signal transduction by p53 class mediator; synapse organization
Reference #:  Q13526 (UniProtKB)
Alt. Names/Synonyms: DOD; Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; Peptidyl-prolyl cis-trans isomerase Pin1; peptidyl-prolyl cis/trans isomerase, NIMA-interacting; peptidylprolyl cis/trans isomerase, NIMA-interacting 1; PIN1; PPIase Pin1; prolyl isomerase; protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1; protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1; protein interacting with never in mitosis A1; Rotamase Pin1; UBL5
Gene Symbols: PIN1
Molecular weight: 18,243 Da
Basal Isoelectric point: 8.95  Predict pI for various phosphorylation states
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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Protein Structure Not Found.

Cross-references to other databases:  STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  NURSA