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Details on Person UniProt:Q13526 PIN1
| Class:Id | ReferenceGeneProduct:69717 |
|---|---|
| _chainChangeLog | chain:1-163 added on Sat February 7 2015 |
| _displayName | UniProt:Q13526 PIN1 |
| _timestamp | 2026-02-20 22:47:31 |
| chain | chain:1-163 |
| checksum | 35391AF40B7D1E13 |
| comment | FUNCTION Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs (PubMed:21497122, PubMed:23623683, PubMed:29686383). By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes (PubMed:21497122, PubMed:22033920, PubMed:23623683). 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). Upon IL33-induced lung inflammation, catalyzes cis-trans isomerization of phosphorylated IRAK3/IRAK-M, inducing IRAK3 stabilization, nuclear translocation and expression of pro-inflammatory genes in dendritic cells (PubMed:29686383). Catalyzes cis-trans isomerization of phosphorylated phosphoglycerate kinase PGK1 under hypoxic conditions to promote its binding to the TOM complex and targeting to the mitochondrion (PubMed:26942675). Acts as a negative regulator of adipocyte browning by binding to phosphorylated PRDM16, targeting PRDM16 for degradation (By similarity).CATALYTIC ACTIVITY [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)SUBUNIT Interacts with STIL (By similarity). Interacts with KIF20B (PubMed:11470801). Interacts with NEK6 (PubMed:16476580). Interacts (via WW domain) with PRKX (PubMed:19367327). Interacts with BTK (PubMed:16644721). Interacts (via PpiC domain) with DAPK1 (PubMed:21497122). Interacts with the phosphorylated form of RAF1 (PubMed:15664191). Interacts (via WW domain) with ATCAY; upon NGF stimulation (PubMed:18628984). Interacts with PML (isoform PML-4) (PubMed:22033920). Interacts with BCL6 (PubMed:17828269). Interacts with FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation (PubMed:22608923). Directly interacts with RBBP8/CtIP; this interaction depends upon RBBP8 phosphorylation (PubMed:23623683). Interacts (via WW domain) with IRAK3/IRAK-M (when phosphorylated at 'Ser-110') in response to IL33-mediated (but not TLR4 ligand LPS) dendritic cell stimulation (PubMed:29686383). Interacts with PGK1 (when phosphorylated at 'Ser-203'); the interaction is direct, occurs under hypoxic conditions, and targets PGK1 to the mitochondrion by promoting interactions with the TOM complex (PubMed:26942675). Interacts with PRDM16 (when phosphorylated); the interaction promotes PRDM16 degradation (By similarity).INTERACTION Colocalizes with NEK6 in the nucleus (PubMed:16476580). Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization (PubMed:21497122).TISSUE SPECIFICITY Expressed in immune cells in the lung (at protein level) (PubMed:29686383). The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells.DOMAIN The WW domain is required for the interaction with STIL and KIF20B.PTM Phosphorylation at Ser-71 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation (PubMed:21497122). Ser-71 is dephosphorylated upon IL33-stimulation of dendritic cells (By similarity). |
| description | recommendedName: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 ecNumber evidence="12 15 18"5.2.1.8 alternativeName: Peptidyl-prolyl cis-trans isomerase Pin1 shortName: PPIase Pin1 alternativeName: Rotamase Pin1 |
| geneName | PIN1 |
| identifier | Q13526 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Cell cycle Cytoplasm Isomerase Nucleus Phosphoprotein Proteomics identification Reference proteome Rotamase |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20 |
| name | PIN1 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8988031] ENSEMBL:ENSG00000127445 PIN1 [Homo sapiens] |
| secondaryIdentifier | PIN1_HUMAN A8K4V9 Q53X75 |
| sequenceLength | 163 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:936016] PIN1 [nucleoplasm] [Homo sapiens] [EntityWithAccessionedSequence:9626823] PIN1 [cytosol] [Homo sapiens] |
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No pathways have been reviewed or authored by UniProt:Q13526 PIN1 (69717)
