Search results for PRKACA

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Reaction (5 results from a total of 5)

Identifier: R-HSA-5617182
Species: Homo sapiens
Compartment: sarcoplasmic reticulum membrane, cytosol
Cardiac muscle phospholamban (PLN aka PLB) modulates cardiac contractility by inhibiting the sarcoplasmic reticulum calcium pump (ATP2A2 aka SERCA). This process is dynamically regulated by beta-adrenergic stimulation and phosphorylation of PLN. Protein kinase A (PRKACA) is able to phosphorylate PLN at serine 16, relieving its inhibition of ATP2A2 and modulating cardiac contractility (Glaves et al. 2011, Ceholski et al. 2012). The ATP2B4:NOS1 complex, via cAMP, increases PRKACA activity, thereby regulating the response of the heart to beta-adrenergic agonists.
Identifier: R-HSA-5617179
Species: Homo sapiens
Compartment: cytosol
Human cardiac troponin I (TNNI3) is known to be phosphorylated at multiple amino acid residue sites by several kinases. Protein kinase A (PRKACA) can phosphorylate serine 23 and 24 sites on TNNI3. Phosphorylation of TNNI3 reduces myofilament calcium sensitivity (Mittmann et al. 1990, Keane et al. 1997, Zhang et al. 2012). Defects in TNNI3 can cause a range of cardiomyopathies (Lu et al. 2013). The ATP2B4:NOS1 complex, via cAMP, increases PRKACA activity, thereby regulating the response of the heart to beta-adrenergic agonists.
Identifier: R-HSA-111919
Species: Homo sapiens
Compartment: nucleoplasm
Protein kinase A (PKA) has two regulatory subunits and two catalytic subunits which are held together to form the holoenzyme and is activated upon binding of cAMP to the regulatory subunits. Once cAMP binds the regulatory subunits, the catalytic subunits are released to carry out phosphorylation of CREB1 at serine residue S133. Only the PKA catalytic subunit alpha, PRKACA, was directly demonstrated to phosphorylate CREB1 at S133, using recombinant mouse and rat proteins, respectively (Gonzalez and Montminy 1989). PKA catalytic subunits beta and gamma (PRKACB and PRKACG) are candidate CREB1 kinases based on indirect evidence and sequence similarity (Nagakura et al. 2002, Liang et al. 2007, James et al. 2009). PRKX is the catalytic subunit of the cAMP dependent protein kinase X, which shares the regulatory subunits and functional properties with the PKA. PRKX is highly expressed in the mouse fetal brain (Li et al. 2005) and is implicated in CREB1 phosphorylation through indirect evidence (Di Pasquale and Stacey 1998, Li et al. 2002).
Identifier: R-HSA-8986937
Species: Homo sapiens
Compartment: nucleoplasm
Calcium-dependent protein kinases, PKA and CaMK IV, activated by neuronal membrane depolarization, phosphorylate MECP2 at threonine residue T308. Only the PKA C-alpha isoform (PRKACA) was experimentally tested. T308 corresponds to T320 in the longer MECP2 splicing isoform, MECP2_e1 (MECP2B). Phosphorylation of MECP2 at threonine residue T308 is correlated with neuronal activity and inhibits binding of MECP2 to the nuclear receptor co-repressor complex (NCoR/SMRT) (Ebert et al. 2013).
Identifier: R-HSA-5624473
Species: Homo sapiens
Compartment: nucleoplasm
Protein kinase A (PKA/PRKACA) and Ribosomal protein S6 kinase alpha-5 (RPS6KA5/MSK1/SAPK1) phosphorylate serine 276 (S276) in the Rel homology domain (RHD) of nuclear p65 subunit RELA (Yoon et al. 2008, Reber et al. 2009). Few other phosphorylation sites (S311, S529 and S536) have also been proposed in RELA (Duran et al. 2003) note: in this reaction we are showing only S276 phosphorylation)). Phosphorylation of RELA subunit enhances the association of RELA with p300 and this is a prerequisite for later NF-kB modification by histone acetyltransferases (HATs) p300/CBP. Phosphorylation of RELA also cross-regulates CLEC7A (dectin-1) mediated non-canonical NF-kB pathway by forming inactive p65 and RELB dimers, that cannot bind DNA.
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