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. Author manuscript; available in PMC: 2022 Sep 6.
Published in final edited form as: Cell Rep. 2022 Aug 16;40(7):111203. doi: 10.1016/j.celrep.2022.111203

Table 1.

PKA pathway phosphoproteomic changes in STK25−/− compared with wild type

Function Protein descriptions Fold change Phosphorylation sites Protein accessions
PKA regulatory subunits PRKAR1A cAMP-dependent protein kinase type I alpharegulatory subunit 0.17 S77, S83 P10644

PRKAR2A cAMP-dependent protein kinase type II-alpha regulatory subunit 3.03 S78 P13861

catalytic subunit PRKACA cAMP-dependent protein kinase catalytic subunit alpha 0.79 S339 P17612

PKA targets contractility Ca2+ handling MYBPC3 myosin-binding protein C, cardiac type 100.03 T498 Q14896

TNNT2 troponin T, cardiac muscle 6.18 S132 P45379

5.75 S285

5.02 S189

RYR2 isoform 2 of ryanodine receptor 2 2.51 S2808 Q92736

2.14 S4368

CACNA1C isoform 2 of voltage-dependent L-type calcium channel subunit alpha 1C 1.65 S1756 Q13936

energy metabolism PHKG2 phosphorylase b kinase gamma catalytic chain 3.48 T325 P15735
GSK3α glycogen synthase kinase-3 alpha 2.50 S21 P49840

gene expression CREB1 cyclic AMP-responsive element-binding protein 1 0.79 S271 P16220

Fold change represents a ratio of STK25−/−/STK25+/+. Phosphorylation sites, description, and accession numbers for each uniprot ID are listed. All changes met a significance threshold of a false discovery rate (FDR)-corrected q value <0.05.