ID:PPIG_HUMAN DESCRIPTION: RecName: Full=Peptidyl-prolyl cis-trans isomerase G; Short=PPIase G; Short=Peptidyl-prolyl isomerase G; EC=188.8.131.52; AltName: Full=CASP10; AltName: Full=Clk-associating RS-cyclophilin; Short=CARS-Cyp; Short=CARS-cyclophilin; Short=SR-cyclophilin; Short=SR-cyp; Short=SRcyp; AltName: Full=Cyclophilin G; AltName: Full=Rotamase G; FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing. CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0). ENZYME REGULATION: Cyclosporin A (CsA)-sensitive. SUBUNIT: Interacts with CLK1, PNN and with the phosphorylated C- terminal domain of RNA polymerase II. SUBCELLULAR LOCATION: Nucleus matrix. Nucleus speckle. Note=Colocalizes with RNA splicing factors at nuclear speckles. TISSUE SPECIFICITY: Ubiquitous. DOMAIN: The RS domain is required for the interaction with the phosphorylated C-terminal domain of RNA polymerase II. PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
Genetic Association Studies of Complex Diseases and Disorders
Genetic Association Database (archive): PPIG CDC HuGE Published Literature: PPIG
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q13427
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.