The type II cAMP-dependent protein kinase (PKA) is a multifunctional kinase with a broad range of substrates. Specificity of PKA signaling is mediated by the compartmentalization of the kinase to specific sites within the cell. To maintain this specific localization, the R subunit (RII) of PKA interacts with specific RII-anchoring proteins, designated A-kinase anchoring proteins (AKAP). AKAP 3, also known as AKAP 110, FSP95, PRKA3 and SOB1, binds both PKA and PDE4A and functions as a scaffolding protein in spermatozoa to regulate local cAMP concentrations and modulate sperm functions. Expression of AKAP 3 in normal tissues is restricted to the testis, where bicarbonate stimulates tyrosine phosphorylation of AKAP 3, thereby increasing its recruitment of PKA. AKAP-3 also exhibits high expression in patients with epithelial ovarian cancer (EOC). It demonstrates tumor-restricted expression and appears to be associated with worse overall survival, which make AKAP 3 a potential target for antigen-specific immunotherapy in EOC.