Pin1
entrez
23988
canonical
uniprot
Q9QUR7
canonical
ensembl
ENSMUSG00000032171
resolver
ensp
ENSMUSP00000034689
resolver
ensp
ENSMUSP00000336366
resolver
enst
ENSMUST00000034689
resolver
genesymbol
Pin1
resolver
uniprot
Q543B3
resolver
uniprot_entry
PIN1_MOUSE
resolver
uniprot_sec
Q543B3
resolver
amino_acid_sequence
MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGGSTVGGSSKNGQGEPAKVRCSHLLVKHSQSRRPSSWRQEKITRSKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGPFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE
uniprot
proteins
ec_number
5.2.1.8
uniprot
proteins
function
FUNCTION: Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs (PubMed:29686383, PubMed:30893596). By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes (PubMed:29686383, PubMed:30893596). Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. 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 (By similarity). 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 (By similarity). 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) (By similarity). 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 (By similarity). Acts as a negative regulator of adipocyte browning by binding to phosphorylated PRDM16, targeting PRDM16 for degradation (PubMed:30893596). {ECO:0000250|UniProtKB:Q13526, ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:29686383}.
uniprot
proteins
mass_dalton
18370
uniprot
proteins
mutagenesis
MUTAGEN 65; /note="K->A: Loss of peptidyl-prolyl cis/trans isomerase activity; abolished ability to promote degradation of PRDM16."; /evidence="ECO:0000269|PubMed:30893596
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-73 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation (By similarity). Ser-73 is dephosphorylated upon IL33-stimulation of dendritic cells (PubMed:29686383). {ECO:0000250|UniProtKB:Q13526, ECO:0000269|PubMed:29686383}.
uniprot
proteins
pubmed
10600477
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16024801
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17828269
uniprot
proteins
pubmed
19367327
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
29686383
uniprot
proteins
pubmed
30893596
uniprot
proteins
sequence_length
165
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29686383}. Nucleus speckle {ECO:0000250|UniProtKB:Q13526}. Cytoplasm {ECO:0000250|UniProtKB:Q13526}. Note=Colocalizes with NEK6 in the nucleus. Mainly localized in the nucleus but phosphorylation at Ser-73 by DAPK1 results in inhibition of its nuclear localization. {ECO:0000250|UniProtKB:Q13526}.
uniprot
proteins