{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nThe human kinome has been comprehensively catalogued to reveal the full complement of protein kinases encoded by the human genome. In this large‐scale analysis, 518 putative kinase genes were identified—including many not previously characterized—and their chromosomal distributions were mapped extensively with a view toward linking specific kinases to disease states and cancer‐associated genomic changes."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " Although the study does not explicitly mention “RSKR,” its focus on kinase families suggests that conserved motifs—potentially including sequences such as RSKR—could serve as key determinants in substrate recognition and catalytic regulation within these enzymes.\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn a related vein, detailed biochemical characterization of a mouse aldo-keto reductase (AKR1CL) has delineated its role as a highly specific NADPH‐dependent prostaglandin D2 11‑ketoreductase. The enzyme exhibits strict substrate specificity—principally reducing PGD2 and catalyzing the reverse reaction for 9α,11β‐PGF2—by virtue of critical active site residues (e.g., P85), whose mutation broadens substrate scope."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " While the abstract does not directly reference “RSKR,” the precision with which molecular determinants govern substrate selection in AKR1CL may be conceptually analogous to the way conserved peptide motifs (such as RSKR) function in other enzymatic systems, notably in ensuring proper regulation and selectivity in catalytic processes.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "G Manning, D B Whyte, R Martinez, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The protein kinase complement of the human genome."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Science (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/science.1075762"}], "href": "https://doi.org/10.1126/science.1075762"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12471243"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12471243"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Satoshi Endo, Toshiyuki Matsunaga, Akira Hara "}, {"type": "b", "children": [{"type": "t", "text": "Mouse Akr1cl gene product is a prostaglandin D"}, {"type": "a", "children": [{"type": "t", "text": "sub"}], "href": "sub"}, {"type": "t", "text": "2"}, {"type": "a", "children": [{"type": "t", "text": "/sub"}], "href": "/sub"}, {"type": "t", "text": " 11-ketoreductase with strict substrate specificity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Arch Biochem Biophys (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.abb.2019.108096"}], "href": "https://doi.org/10.1016/j.abb.2019.108096"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31479646"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31479646"}]}]}]}