PPIA PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Cyclophilin; EC 5.2.1.8; Isomerase; RNA-binding
Chromosomal Location of Human Ortholog: 11 A1|11 3.97 cM
Cellular Component:  cytoplasm; extracellular region; protein-containing complex
Molecular Function:  cyclosporin A binding; isomerase activity; peptidyl-prolyl cis-trans isomerase activity; protein binding; unfolded protein binding
Biological Process:  lipid droplet organization; neuron differentiation; positive regulation of protein secretion; positive regulation of viral genome replication; protein folding; protein peptidyl-prolyl isomerization; protein refolding; regulation of viral genome replication
Reference #:  P17742 (UniProtKB)
Alt. Names/Synonyms: 2700098C05; Cphn; Cyclophilin A; Cyclosporin A-binding protein; CyP-18; CypA; OTTMUSP00000000741; Peptidyl-prolyl cis-trans isomerase A; peptidylprolyl isomerase A; Ppia; PPIase A; Rotamase A; SP18
Gene Symbols: Ppia
Molecular weight: 17,971 Da
Basal Isoelectric point: 7.73  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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PPIA

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene