| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.7.11.- |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.7.-.- |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.-.-.- |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/2000/01/rdf-schema#comment | "Certain R2C2 combinations can be localized to particular subcellular regions by their association with diverse species of 'A Kinase-Anchoring Proteins' (AKAPs)."xsd:string |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme has been characterized from many organisms. Humans have three C units (Calpha, Cbeta, and Cgamma) encoded by the paralogous genes PRKACA, PRKACB and PRKACG, respectively, and four R subunits (R1alpha, RIbeta, RIIalpha and RIIbeta), encoded by PKRAR1A, PKRAR1B, PKRAR2A and PKRAR2B, respectively. Yeast (Saccharomyces cerevisiae) has three C subunits (Tpk1, Tpk2, and Tpk3) encoded by the paralogous genes TPK1, TPK2 and TPK3, respectively, and a single R subunit (Bcy1) encoded by the BCY1 gene."xsd:string |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/2000/01/rdf-schema#comment | "Activity requires phosphorylation of a conserved Thr in the activation loop (T-loop) sequence (Thr(198) in human Calpha; Thr(224) in budding yeast Tpk2), installed by auto-phosphorylation or by the 3-phosphoinositide-dependent protein kinase-1 (PDPK1)."xsd:string |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/2000/01/rdf-schema#comment | "Some validated substrates of the enzyme include cAMP-response element-binding protein (CREB), phosphorylase kinase alpha subunit (PHKA), and tyrosine 3-monooxygenase (TH) in mammals; Adr1, Whi3, Nej1, and Pyk1 in yeast."xsd:string |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/2000/01/rdf-schema#comment | "Binding of cAMP activates the enzyme by causing conformational changes that release two free monomeric C subunits from a dimer of the R subunits, i.e. R2C2 + 4 cAMP = R2(cAMP)4 + 2 C."xsd:string |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/2000/01/rdf-schema#comment | "This eukaryotic enzyme recognizes the sequence -Arg-Arg-X-Ser*/Thr*-Hpo, where * indicates the phosphorylated residue and Hpo indicates a hydrophobic residue."xsd:string |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/2000/01/rdf-schema#comment | "The inactive holoenzyme is a heterotetramer composed of two regulatory (R) subunits and two catalytic (C) subunits."xsd:string |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/2000/01/rdf-schema#comment | "Each R subunit occludes the active site of a C subunit and contains two binding sites for 3',5'-cyclic-AMP (cAMP)."xsd:string |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/2004/02/skos/core#prefLabel | "cAMP-dependent protein kinase"xsd:string |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11705384 |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/21644927 |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/22964838 |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/2550680 |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/27860220 |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/33957122 |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/34663687 |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/2004/02/skos/core#altLabel | "PKA"xsd:string |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/2004/02/skos/core#altLabel | "protein kinase A"xsd:string |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://www.w3.org/2004/02/skos/core#altLabel | "PKA C"xsd:string |
| http://purl.uniprot.org/enzyme/2.7.11.11 | http://purl.uniprot.org/core/replaces | http://purl.uniprot.org/enzyme/2.7.1.37 |