Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Q13526)

Uniprot ID	Q13526
Protein Name	Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
Gene Name	PIN1
Species	Homo sapiens (Human)

Signal peptide^(a)	N	Secretome P^(b)
Function	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 (PubMed:21497122, PubMed:22033920, Ref. 21). 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 (PubMed:16644721). 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 (PubMed:15664191). Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner (PubMed:17828269). 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 (PubMed:22608923). 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) (PubMed:23623683, PubMed:27561354). .
GO - Molecular function	beta-catenin binding : IPI:ParkinsonsUK-UCL GTPase activating protein binding : IPI:BHF-UCL mitogen-activated protein kinase kinase binding : IPI:BHF-UCL motor activity : ISS:ParkinsonsUK-UCL peptidyl-prolyl cis-trans isomerase activity : IDA:BHF-UCL phosphoprotein binding : ISS:ARUK-UCL phosphoserine residue binding : IDA:BHF-UCL phosphothreonine residue binding : IDA:BHF-UCL
GO - Biological process	cell cycle : IEA:UniProtKB-KW negative regulation of cell motility : IDA:BHF-UCL negative regulation of ERK1 and ERK2 cascade : IDA:BHF-UCL negative regulation of neuron apoptotic process : IEA:Ensembl negative regulation of protein binding : IDA:ParkinsonsUK-UCL negative regulation of protein catabolic process : IDA:ParkinsonsUK-UCL negative regulation of transforming growth factor beta receptor signaling pathway : IDA:BHF-UCL negative regulation of type I interferon production : TAS:Reactome neuron differentiation : ISS:ParkinsonsUK-UCL positive regulation of canonical Wnt signaling pathway : IDA:ParkinsonsUK-UCL positive regulation of cell growth involved in cardiac muscle cell development : IEA:Ensembl positive regulation of GTPase activity : IMP:BHF-UCL positive regulation of neuron apoptotic process : IEA:Ensembl positive regulation of protein dephosphorylation : TAS:ARUK-UCL positive regulation of protein phosphorylation : IGI:MGI positive regulation of transcription by RNA polymerase II : IDA:ParkinsonsUK-UCL positive regulation of ubiquitin-protein transferase activity : IDA:BHF-UCL protein peptidyl-prolyl isomerization : TAS:ParkinsonsUK-UCL protein stabilization : IDA:ParkinsonsUK-UCL regulation of cytokinesis : IMP:MGI regulation of mitotic nuclear division : TAS:ProtInc regulation of pathway-restricted SMAD protein phosphorylation : IDA:BHF-UCL regulation of protein localization to nucleus : IDA:ParkinsonsUK-UCL regulation of signal transduction by p53 class mediator : TAS:Reactome synapse organization : ISS:ParkinsonsUK-UCL

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^{(a) The Signal peptide D-score cutoff for "YES"(having signal peptide) is 0.45.}
^{(b) Non-classically secreted proteins should obtain an NN-score(Neural Networks score) exceeding the normal threshold of 0.5, but not at the same time be predicted to contain a signal peptide.}