| Modification Notes |
Cyclophilins are conserved, ubiquitous and abundant cytosolic peptidyl-prolyl cis-trans isomerases that accelerate the isomerization of XaaPro peptide bonds and the refolding of proteins. Cyclophilin G, also known as CARS-Cyp (Clk-associating RS-cyclophilin), SRcyp (SR-cyclophilin), CASP10, PPIase G or Rotamase G, is a ubiquitously expressed member of the Moca family of cyclophilins. Localizing to the nucleus and, during interphase, nuclear speckles, Cyclophilin G contains an N-terminal cyclophilin-type domain, an acidic serine-rich region, five Cdc2-type phosphorylation sites and a series of serine-arginine repeats throughout the C-terminus. Cyclophilin G is phosphorylated during mitosis by the Cdc2-cyclin B complex, suggesting that its function is cell cycle-regulated. In addition, Cyclophilin G is capable of interacting with Pinin and the C-terminus of the largest subunit of RNA polymerase II (Pol II). Cyclophilin G may participate in pre-mRNA splicing by regulating the subnuclear localization of SR/SR-like protein family members. |