Protein (peptidylprolyl cis/trans isomerase) NIMA interacting, 4 (parvulin)
FunctionIsoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA. Isoform 2 binds to double-stranded DNA.
Tissue specificityIsoform 2 is much more stable than isoform 1 (at protein level). Ubiquitous. Isoform 1 and isoform 2 are expressed in kidney, liver, blood vessel, brain, mammary gland, skeletal muscle, small intestine and submandibularis. Isoform 1 transcripts are much more abundant than isoform 2 in each tissue analyzed.
Sequence similaritiesBelongs to the ppiC/parvulin rotamase family. PIN4 subfamily. Contains 1 PpiC domain.
Post-translational modificationsPhosphorylated. Isoform 1 phosphorylation occurs both in the nucleus and the cytoplasm. Isoform 1 phosphorylation at Ser-19 does not affect its PPIase activity but is required for nuclear localization, and the dephosphorylation is a prerequisite for the binding to DNA. The unphosphorylated isoform 1 associates with the pre-rRNP complexes in the nucleus. Isoform 2 is sumoylated by SUMO2 and SUMO3.
Cellular localizationMitochondrion. Mitochondrion matrix. Imported in a time- and membrane potential-dependent manner to the mitochondrial matrix, but without concomitant processing of the protein. Directed to mitochondria by a novel N-terminal domain that functions as non-cleavable mitochondrial targeting peptide and Nucleus > nucleolus. Cytoplasm > cytoskeleton > spindle. Cytoplasm. Colocalizes in the nucleolus during interphase and on the spindle apparatus during mitosis with NPM1.