PIN1 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0042177Biological processnegative regulation of protein catabolic process
GO_0010468Biological processregulation of gene expression
GO_0060392Biological processnegative regulation of SMAD protein signal transduction
GO_0030512Biological processnegative regulation of transforming growth factor beta receptor signaling pathway
GO_0043547Biological processpositive regulation of GTPase activity
GO_0035307Biological processpositive regulation of protein dephosphorylation
GO_0090263Biological processpositive regulation of canonical Wnt signaling pathway
GO_0032092Biological processpositive regulation of protein binding
GO_1902430Biological processnegative regulation of amyloid-beta formation
GO_0070373Biological processnegative regulation of ERK1 and ERK2 cascade
GO_0001932Biological processregulation of protein phosphorylation
GO_0001934Biological processpositive regulation of protein phosphorylation
GO_0032465Biological processregulation of cytokinesis
GO_0030182Biological processneuron differentiation
GO_0046785Biological processmicrotubule polymerization
GO_0050821Biological processprotein stabilization
GO_0001666Biological processresponse to hypoxia
GO_1900180Biological processregulation of protein localization to nucleus
GO_0032091Biological processnegative regulation of protein binding
GO_0050808Biological processsynapse organization
GO_2000146Biological processnegative regulation of cell motility
GO_0031647Biological processregulation of protein stability
GO_0000413Biological processprotein peptidyl-prolyl isomerization
GO_0045944Biological processpositive regulation of transcription by RNA polymerase II
GO_0007088Biological processregulation of mitotic nuclear division
GO_0098978Cellular componentglutamatergic synapse
GO_0030496Cellular componentmidbody
GO_0016607Cellular componentnuclear speck
GO_0005654Cellular componentnucleoplasm
GO_0005829Cellular componentcytosol
GO_0099524Cellular componentpostsynaptic cytosol
GO_0005737Cellular componentcytoplasm
GO_0036064Cellular componentciliary basal body
GO_0005634Cellular componentnucleus
GO_0031434Molecular functionmitogen-activated protein kinase kinase binding
GO_0032794Molecular functionGTPase activating protein binding
GO_0003755Molecular functionpeptidyl-prolyl cis-trans isomerase activity
GO_0008013Molecular functionbeta-catenin binding
GO_0016859Molecular functioncis-trans isomerase activity
GO_0003774Molecular functioncytoskeletal motor activity
GO_0050816Molecular functionphosphothreonine residue binding
GO_0048156Molecular functiontau protein binding
GO_1990757Molecular functionubiquitin ligase activator activity
GO_0051219Molecular functionphosphoprotein binding
GO_0050815Molecular functionphosphoserine residue binding
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene namePIN1
Protein namePeptidyl-prolyl cis-trans isomerase (EC 5.2.1.8)
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase Pin1) (PPIase Pin1) (Rotamase Pin1)
Prolyl isomerase
Peptidylprolyl cis/trans isomerase, NIMA-interacting 1
Synonyms
DescriptionFUNCTION: 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 . 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 . 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 . Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner . 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 . 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) . 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 . .

AccessionsK7EP26
Q13526
Q49AR7
ENST00000587625.5
Q8NFL2
ENST00000591777.1
K7EMU7
ENST00000586352.5
ENST00000247970.9
ENST00000588695.5
K7EN45