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cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits have been identified in humans. The protein encoded by this gene is a member of the Ser/Thr protein kinase family and is a catalytic subunit of cAMP-dependent protein kinase. Several alternatively spliced transcript variants encoding distinct isoforms have been observed.
, cAMP-dependent protein kinase catalytic beta subunit isoform 4ab
, cAMP-dependent protein kinase catalytic subunit beta
, protein kinase A catalytic subunit beta
, p70 S6 kinase
, protein kinase, cAMP-dependent, catalytic, beta a
, C-beta subunit
, protein kinase, cAMP-dependent, catalytic, beta
, cAMP-dependent protein kinase C beta