PIN1 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; 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; 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 or siRNAs 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