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PPIA

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Protein class

Enzymes, FDA approved drug targets, Metabolic proteins, Plasma proteins

Predicted location

Intracellular, Secreted (different isoforms)

Single cell type specificity

Low cell type specificity

Immune cell specificity

Low immune cell specificity

Cell line specificity

Low cell line specificity

Interaction

Interacts with protein phosphatase PPP3CA/calcineurin A (PubMed:12218175, 12357034). Interacts with PRPF19 isoform 2 (via N-terminus) (By similarity). Interacts with isoform 2 of BSG/CD147 (PubMed:15688292, 11353871, 11943775, 21245143). Interacts with FOXO1; the interaction promotes FOXO1 dephosphorylation, nuclear accumulation and transcriptional activity (PubMed:31063815). Interacts with integrin ITGA2B:ITGB3; the interaction is ROS and peptidyl-prolyl cis-trans isomerase (PPIase) activity-dependent and is increased in the presence of thrombin (By similarity). Interacts with MAP3K5 (PubMed:26095851). Interacts with TARDBP; the interaction is dependent on the RNA-binding activity of TARDBP and the PPIase activity of PPIA/CYPA and the acetylation of PPIA/CYPA at Lys-125 favors the interaction (PubMed:25678563). Interacts with HNRNPA1, HNRNPA2B1, HNRNPC, RBMX, HNRNPK and HNRNPM (PubMed:25678563). (Microbial infection) Interacts with HIV-1 capsid protein (PubMed:20364129, 8513493). (Microbial infection) Interacts with human SARS coronavirus nucleoprotein. (Microbial infection) Interacts with measles virus nucleoprotein. (Microbial infection) Interacts with influenza A virus matrix protein 1. (Microbial infection) Interacts with HCV NS5A; the interaction stimulates RNA-binding ability of NS5A and is dependent on the peptidyl-prolyl cis-trans isomerase activity of PPIA/CYPA.

Molecular function

Isomerase, Rotamase

More Types Infomation

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For Research Use Only. Not For Clinical Use.

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