PIN1 | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
 
image/svg+xmlExtracellular space Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi Apparatus Nucleus Mitochondrion None Substrate Localization legend

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Sequence Viewer
Gene
Synonyms
-
Protein Name
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
UniProt ID
Q13526 [go to UniProt ] [go to PDBe-KB ]
Ensembl Gene ID
NCBI Gene ID
Molecular Weight
18243
Protein Length
163
Protein Domain
3D Structure
(PDB ID : 1f8a)
Target by Small Molecules
Protein-protein Interaction Database
Gene Expression
Drugs and Diseases
Enzyme Class
5.2.1.8; (BRENDA)
Catalytic Site
Catalytic Activity
[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Localization
Nucleus,Nucleus speckle,Cytoplasm;
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).
Gene Ontology
GO:0005737; GO:0005829; GO:0098978; GO:0030496; GO:0005739; GO:0043005; GO:0016607; GO:0005654; GO:0005634; GO:0099524; GO:0008013; GO:0032794; GO:0031434; GO:0003774; GO:0003755; GO:0051219; GO:0050815; GO:0050816; GO:0048156; GO:0007049; GO:2000146; GO:0070373; GO:0043524; GO:0032091; GO:0042177; GO:0030512; GO:0032480; GO:0030182; GO:0090263; GO:0061051; GO:0043547; GO:0043525; GO:0032092; GO:0035307; GO:0001934; GO:0045944; GO:0051443; GO:0000413; GO:0050821; GO:0032465; GO:0010468; GO:0007088; GO:0060393; GO:1900180; GO:0001932; GO:1901796; GO:0050808
 
Gene Ontology