catalytic activity:Peptidylproline (omega=180) = peptidylproline (omega=0). domain:The RS domain is required for the interaction with the phosphorylated C-terminal domain of RNA polymerase II. enzyme regulation:Cyclosporin A (CsA)-sensitive. PPIases accelerate the folding of proteins. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. 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. PTM:Phosphorylated upon DNA damage, probably by ATM or ATR. Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain. subcellular location:Colocalizes with RNA splicing factors at nuclear speckles. subunit:Interacts with CLK1, PNN and with the phosphorylated C-terminal domain of RNA polymerase II. tissue specificity:Ubiquitous.
Immunogen
Synthesized peptide derived from human protein . at AA range: 290-370