PPIE Involved in pre-mRNA splicing as component of the spliceosome. Combines RNA-binding and PPIase activities. Binds mRNA and has a preference for single-stranded RNA molecules with poly-A and poly-U stretches, suggesting it binds to the poly(A)-region in the 3'-UTR of mRNA molecules. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in proteins. Inhibits KMT2A activity; this requires proline isomerase activity. Belongs to the cyclophilin-type PPIase family. PPIase E subfamily. Found in all the examined tissues including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. 3 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Cyclophilin; EC 5.2.1.8; Isomerase; RNA splicing; Spliceosome
Chromosomal Location of Human Ortholog: 4|4 D2.2
Cellular Component:  catalytic step 2 spliceosome; cytosol; nuclear speck; nucleus; spliceosomal complex; U2-type catalytic step 2 spliceosome
Molecular Function:  cyclosporin A binding; isomerase activity; mRNA binding; nucleic acid binding; peptidyl-prolyl cis-trans isomerase activity; poly(A) binding; RNA binding; unfolded protein binding
Biological Process:  mRNA processing; mRNA splicing, via spliceosome; positive regulation of viral genome replication; protein folding; protein peptidyl-prolyl isomerization; protein refolding; regulation of transcription, DNA-templated; RNA splicing
Reference #:  Q9QZH3 (UniProtKB)
Alt. Names/Synonyms: 2010010D16Rik; Cyclophilin E; Cyclophilin-33; Cyp33; OTTMUSP00000009312; Peptidyl-prolyl cis-trans isomerase E; peptidylprolyl isomerase E (cyclophilin E); PPIase E; Ppie; Rotamase E
Gene Symbols: Ppie
Molecular weight: 33,449 Da
Basal Isoelectric point: 5.41  Predict pI for various phosphorylation states
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PPIE

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  BioGPS  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene