Overview
| Uniprot ID | Q13526 |
|---|
| Protein Name | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 |
|---|
| Gene Name | PIN1 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 117 |
FSDCSSAKARGDLGA |
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)
Protein Sequence
10
MADEEKLPPG
20
WEKRMSRSSG
30
RVYYFNHITN
40
ASQWERPSGN
50
SSSGGKNGQG
60
EPARVRCSHL
70
LVKHSQSRRP
80
SSWRQEKITR
90
TKEEALELIN
100
GYIQKIKSGE
110
EDFESLASQF
120
SDCSSAKARG
130
DLGAFSRGQM
140
QKPFEDASFA
150
LRTGEMSGPV
160
FTDSGIHIIL
RTE
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0036064 |
ciliary basal body |
| Molecular Function |
GO:0032794 |
GTPase activating protein binding |
| Molecular Function |
GO:0031434 |
mitogen-activated protein kinase kinase binding |
| Molecular Function |
GO:0003755 |
peptidyl-prolyl cis-trans isomerase activity |
| Molecular Function |
GO:0051219 |
phosphoprotein binding |
| Molecular Function |
GO:0050815 |
phosphoserine residue binding |
| Molecular Function |
GO:0050816 |
phosphothreonine residue binding |
| Molecular Function |
GO:0048156 |
tau protein binding |
| Molecular Function |
GO:1990757 |
ubiquitin ligase activator activity |
| Biological Process |
GO:0071456 |
cellular response to hypoxia |
| Biological Process |
GO:1902430 |
negative regulation of amyloid-beta formation |
| Biological Process |
GO:1903444 |
negative regulation of brown fat cell differentiation |
| Biological Process |
GO:2000146 |
negative regulation of cell motility |
| Biological Process |
GO:0070373 |
negative regulation of ERK1 and ERK2 cascade |
| Biological Process |
GO:0042177 |
negative regulation of protein catabolic process |
| Biological Process |
GO:0060392 |
negative regulation of SMAD protein signal transduction |
| Biological Process |
GO:0030512 |
negative regulation of transforming growth factor beta receptor signaling pathway |
| Biological Process |
GO:0030182 |
neuron differentiation |
| Biological Process |
GO:0090263 |
positive regulation of canonical Wnt signaling pathway |
| Biological Process |
GO:0001934 |
positive regulation of protein phosphorylation |
| Biological Process |
GO:0045944 |
positive regulation of transcription by RNA polymerase II |
| Biological Process |
GO:0031648 |
protein destabilization |
| Biological Process |
GO:0000413 |
protein peptidyl-prolyl isomerization |
| Biological Process |
GO:0050821 |
protein stabilization |
| Biological Process |
GO:0006626 |
protein targeting to mitochondrion |
| Biological Process |
GO:0032465 |
regulation of cytokinesis |
| Biological Process |
GO:0010468 |
regulation of gene expression |
| Biological Process |
GO:0007088 |
regulation of mitotic nuclear division |
| Biological Process |
GO:1900180 |
regulation of protein localization to nucleus |
| Biological Process |
GO:0031647 |
regulation of protein stability |
| Biological Process |
GO:0001666 |
response to hypoxia |
| Biological Process |
GO:0007266 |
Rho protein signal transduction |
| Biological Process |
GO:0050808 |
synapse organization |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0098978 |
glutamatergic synapse |
| Cellular Component |
GO:0030496 |
midbody |
| Cellular Component |
GO:0016607 |
nuclear speck |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0099524 |
postsynaptic cytosol |
| Molecular Function |
GO:0008013 |
beta-catenin binding |
| Molecular Function |
GO:0016859 |
cis-trans isomerase activity |
| Molecular Function |
GO:0003774 |
cytoskeletal motor activity |
Reference
[1] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.