PIN1
entrez
5300
canonical
uniprot
Q13526
canonical
ensembl
ENSG00000127445
resolver
ensp
ENSP00000247970
resolver
ensp
ENSP00000466962
resolver
enst
ENST00000247970
resolver
enst
ENST00000588695
resolver
genesymbol
PIN1
resolver
hgnc
HGNC:8988
resolver
uniprot
A8K4V9
resolver
uniprot
Q53X75
resolver
uniprot_entry
PIN1_HUMAN
resolver
uniprot_sec
A8K4V9
resolver
uniprot_sec
Q53X75
resolver
amino_acid_sequence
MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQGEPARVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE
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: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). {ECO:0000250|UniProtKB:Q9QUR7, ECO:0000269|PubMed:15664191, ECO:0000269|PubMed:16644721, ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:21497122, ECO:0000269|PubMed:22033920, ECO:0000269|PubMed:22608923, ECO:0000269|PubMed:23623683, ECO:0000269|PubMed:26942675, ECO:0000269|PubMed:27561354, ECO:0000269|PubMed:29686383}.
uniprot
proteins
mass_dalton
18243
uniprot
proteins
mutagenesis
MUTAGEN 23; /note="Y->A: Reduced affinity for KIF20B."; /evidence="ECO:0000269|PubMed:11470801"; MUTAGEN 34; /note="W->A: Loss of binding to phosphorylated target proteins, including to phosphorylated RBBP8/CtIP; decrease in DNA repair of double-strand breaks by homologous recombination less efficient than that observed with wild-type protein. Abolishes interaction with IRAK3/IRAK-M. Abolishes IL33-mediated increase of IRAK3/IRAK-M protein levels."; /evidence="ECO:0000269|PubMed:22608923, ECO:0000269|PubMed:23623683, ECO:0000269|PubMed:29686383"; MUTAGEN 63; /note="K->A: Loss of peptidyl-prolyl cis/trans isomerase activity. No effect on the interaction with IRAK3/IRAK-M. Abolishes IL33-mediated increase of IRAK3/IRAK-M protein levels."; /evidence="ECO:0000269|PubMed:22608923, ECO:0000269|PubMed:29686383"; MUTAGEN 71; /note="S->D,E: Loss of peptidyl-prolyl cis/trans isomerase activity, nuclear localization and cellular function."; /evidence="ECO:0000269|PubMed:21497122"; MUTAGEN 113; /note="C->A: Loss of peptidyl-prolyl cis/trans isomerase activity; decrease in DNA repair of double-strand breaks by homologous recombination slightly less efficient than that observed with wild-type protein. No effect on RBBP8/CtIP."; /evidence="ECO:0000269|PubMed:23623683, ECO:0000269|PubMed:26942675
uniprot
proteins
post_translational_modification
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). {ECO:0000250|UniProtKB:Q9QUR7, ECO:0000269|PubMed:21497122}.
uniprot
proteins
pubmed
11470801
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15664191
uniprot
proteins
pubmed
16476580
uniprot
proteins
pubmed
16644721
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17828269
uniprot
proteins
pubmed
18628984
uniprot
proteins
pubmed
19367327
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21497122
uniprot
proteins
pubmed
22033920
uniprot
proteins
pubmed
22608923
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23623683
uniprot
proteins
pubmed
26942675
uniprot
proteins
pubmed
27561354
uniprot
proteins
pubmed
29686383
uniprot
proteins
pubmed
8606777
uniprot
proteins
pubmed
9200606
uniprot
proteins
sequence_length
163
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16476580, ECO:0000269|PubMed:23623683}. Nucleus speckle {ECO:0000269|PubMed:21497122}. Cytoplasm {ECO:0000269|PubMed:21497122}. Note=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). {ECO:0000269|PubMed:16476580}.
uniprot
proteins