ID:PIN4_HUMAN DESCRIPTION: RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4; EC=5.2.1.8; AltName: Full=Parvulin-14; Short=Par14; Short=hPar14; AltName: Full=Parvulin-17; Short=Par17; Short=hPar17; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin4; Short=PPIase Pin4; AltName: Full=Peptidyl-prolyl cis/trans isomerase EPVH; Short=hEPVH; AltName: Full=Rotamase Pin4; FUNCTION: Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA. FUNCTION: Isoform 2 binds to double-stranded DNA. CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0). SUBUNIT: Isoform 1 is found in pre-ribosomal ribonucleoprotein (pre-rRNP) complexes (By similarity). SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleolus. Cytoplasm, cytoskeleton, spindle. Cytoplasm. Note=Colocalizes in the nucleolus during interphase and on the spindle apparatus during mitosis with NPM1. SUBCELLULAR LOCATION: Isoform 2: Mitochondrion. Mitochondrion matrix. Note=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. TISSUE SPECIFICITY: Isoform 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. DOMAIN: The PPIase domain enhances mitochondrial targeting. PTM: Phosphorylated. 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. PTM: Isoform 2 is sumoylated with SUMO2 and SUMO3. SIMILARITY: Belongs to the PpiC/parvulin rotamase family. PIN4 subfamily. SIMILARITY: Contains 1 PpiC domain. SEQUENCE CAUTION: Sequence=AAH05234.2; Type=Erroneous initiation; Sequence=AAH70288.1; Type=Erroneous initiation; Sequence=AAI04654.1; Type=Erroneous initiation; Sequence=AAI11395.1; Type=Erroneous initiation;
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 Q9Y237
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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.