Gene content    
PIN1 ( by HUGO)
Peptidylprolyl Cis/Trans Isomerase, NIMA-Interacting 1
Oncogene
Peptidylprolyl Cis/Trans Isomerase
NIMA-Interacting 1
Protein (Peptidyl-Prolyl Cis/Trans Isomerase) NIMA-Interacting 1
Rotamase Pin1
PPIase Pin1
EC 5.2.1.8
DOD
UBL5
Peptidyl-Prolyl Cis-Trans Isomerase NIMA-Interacting 1
Peptidyl-Prolyl Cis-Trans Isomerase Pin1
NCBI: 19p13    Ensembl: 19p13.2
PIN1_HUMANSize: 163 amino acidsMass: 18243 Da

  • Subunit: Interacts with STIL. Interacts with KIF20B. Interacts with NEK6. Interacts (via WW domain) with PRKX. Interacts with BTK. Interacts (via PpiC domain) with DAPK1. Interacts with the phosphorylated form of RAF1. Interacts (via WW domain) with ATCAY; upon NGF stimulation. Interacts with PML (isoform PML-4) and BCL-6 Selected PDB 3D structures from [IMAGE] and Proteopedia [IMAGE] for PIN1 (see all 55): 1F8A (3D) [IMAGE] 1I6C (3D) [IMAGE] 1I8G (3D) [IMAGE] 1I8H (3D) [IMAGE] 1NMV (3D) [IMAGE] 1NMW (3D) [IMAGE]
  • Tissue specificity: The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells [IMAGE] Pathway & Disease-focused RT2 Profiler PCR Arrays including PIN1: Antiviral Response in human mouse rat Liver Cancer in human mouse rat Pri
  • 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. Catalyzes pSer/Thr-Pro cis/trans isomerizations. 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
                          
    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. Catalyzes pSer/Thr-Pro cis/trans isomerizations. 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
  • Catalytic activity:
    Peptidylproline (omega=180) = peptidylproline (omega=0)
  • Similarity:
    Contains 1 PpiC domain
                          
    Contains 1 WW domain [IMAGE]
  • Protein Domain/Family    
    Source ID Domain Name Type
    InterProIPR000297PPIase_PpiCPpiC-type peptidyl-prolyl cis-trans isomeraseDomain
    IPR001202WW_domWW/Rsp5/WWPDomain
    BlocksIPB000297PpiC-type peptidyl-prolyl cis-trans isomerasePpiC-type peptidyl-prolyl cis-trans isomerase
    IPB002349WW domain signatureWW domain signature

    Gene Ontology    
    Type Term Evidence Source Pub
    Biological Process negative regulation of transforming growth factor beta receptor signaling pathway IDA GOA 19122240
    positive regulation of protein phosphorylation IGI GOA 19638580
    positive regulation of ubiquitin-protein transferase activity IDA GOA 19122240
    protein peptidyl-prolyl isomerization IDA GOA 19122240
    regulation of cytokinesis IMP GOA 19638580
    regulation of cytokinesis IGI GOA 19638580
    regulation of mitosis TAS GOA 10391244
    regulation of pathway-restricted SMAD protein phosphorylation IDA GOA 19122240
    Cellular Component midbody IDA GOA 19638580
    Molecular Function peptidyl-prolyl cis-trans isomerase activity IDA GOA 19122240
    phosphoserine binding IDA GOA 10037602
    phosphothreonine binding IPI GOA 10037602
    phosphothreonine binding IDA GOA 10037602
    protein binding IPI GOA 11470801

    PIN1 cross reference    
    PubMed OMIM Entrez Gene NCKU SNP Nucleotide UniProt Genome Data Viewer HomoloGene