| Gene |
PIN1
|
| Protein Name |
PIN1_HUMAN |
| Organism |
Homo sapiens (Human) |
| Alternative name(s) |
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase Pin1) (PPIase Pin1) (Rotamase Pin1) |
| Protein Family |
N/A |
| NCBI Gene ID |
5300
|
| UniProt ID |
Q13526
|
| Enzyme Class |
5.2.1.8 |
| Molecular Weight |
18243 |
| Protein Length |
163 |
| Protein Domain |
InterPro |
Pfam
|
| 3D Structure |
PDBe |
PDBj |
RCSB PDB |
DrugPort
ModBase |
SwissModel
|
| Gene Expression |
Gene Expression Atlas
|
| Function and Disease |
OMIM |
| Protein-protein Interaction Database |
STRING |
IntAct |
MINT
|
| Kinase Database |
Phospho.ELM
|
PhosphoSite
| NetworKIN
|
| Catalytic Activity (UniProt annotation) |
Peptidylproline (omega=180) = peptidylproline (omega=0). |
| Localization |
Nucleus |
| Function (UniProt annotation) |
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:0000413; GO:0001932; GO:0001934; GO:0003755; GO:0003774; GO:0005634; GO:0005654; GO:0005737; GO:0005739; GO:0005829; GO:0007049; GO:0007088; GO:0008013; GO:0010468; GO:0016607; GO:0030182; GO:0030496; GO:0030512; GO:0031434; GO:0032091; GO:0032092; GO:0032465; GO:0032480; GO:0032794; GO:0035307; GO:0042177; GO:0043005; GO:0043524; GO:0043525; GO:0043547; GO:0045944; GO:0050808; GO:0050815; GO:0050816; GO:0050821; GO:0051219; GO:0051443; GO:0060393; GO:0061051; GO:0070373; GO:0090263; GO:0098978; GO:0099524; GO:1900180; GO:1901796; GO:2000146 |
