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Protein Page:
PPIA (human)

PPIA PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Interacts with HIV-1 Capsid protein. Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase. Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. Note: This description may include information from UniProtKB.
Protein type: Cyclophilin; EC; Isomerase; RNA-binding
Chromosomal Location of Human Ortholog: 7p13
Cellular Component: cytosol; extracellular region; extracellular space; focal adhesion; membrane; nucleus
Molecular Function: peptidyl-prolyl cis-trans isomerase activity; protein binding; unfolded protein binding
Biological Process: entry into host cell; leukocyte migration; positive regulation of protein secretion; positive regulation of viral genome replication; protein folding; protein peptidyl-prolyl isomerization; regulation of viral genome replication; release of virus from host; RNA-dependent DNA replication; uncoating of virus; viral envelope fusion with host membrane; viral infectious cycle; virus assembly
Reference #:  P62937 (UniProtKB)
Alt. Names/Synonyms: Cyclophilin A; Cyclosporin A-binding protein; CYPA; CYPH; MGC117158; MGC12404; MGC23397; Peptidyl-prolyl cis-trans isomerase A; peptidylprolyl isomerase A; peptidylprolyl isomerase A (cyclophilin A); PPIA; PPIase A; Rotamase A; T cell cyclophilin
Gene Symbols: PPIA
Molecular weight: 18,012 Da
Basal Isoelectric point: 7.68  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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Protein Structure Not Found.
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