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POLK (DNA polymerase kappa) is an enzyme. The public catalogues list it as a DNA repair gene, and the evidence so far is association rather than a proven role. Tied to Prostate cancer.
DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts.
Open Targets scores its association with cancer at 0.58 (direct and indirect evidence; datatypes literature 0.85, genetic association 0.00, somatic mutation 0.91).
In plain words · POLK (DNA polymerase kappa) is an enzyme. The public catalogues list it as a DNA repair gene, and the evidence so far is association rather than a proven role. Tied to Prostate cancer.
POLK (DNA polymerase kappa) is an enzyme. The public catalogues list it as a DNA repair gene, and the evidence so far is association rather than a proven role. Tied to Prostate cancer.
DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls.
No product in this corpus aims at POLK yet. Inhibitors are shaped to fit the enzyme's active site so the reaction the cancer relies on stops.
First described 1999. Earliest sequence paper UniProt cites for the protein: Ogi et al, Genes Cells, 1999, "Mutation enhancement by DINB1, a mammalian homologue of the Escherichia coli mutagenesis protein dinB". Source.
Sources: HGNC HGNC:9183 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt Q9UBT6 (protein name, function text, keywords and locations (REST API)); Open Targets ENSG00000122008 (association with cancer (MONDO_0004992) 0.58; per-cancer scores at or above 0.5: prostate cancer 0.56 (GraphQL API, CC0))
DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. Location: Nucleus (UniProt). Locus 5q13.3 (HGNC).
Query for this target: (TITLE:"POLK" OR ABSTRACT:"POLK" OR TITLE:"DNA polymerase kappa" OR ABSTRACT:"DNA polymerase kappa" OR TITLE:"DINB1" OR ABSTRACT:"DINB1") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about POLK, not a curated reading list.
Shares Synthetic lethality: paired dependencies, DNA damage response & homologous recombination, Double-strand break repair: HR versus end joining, Open Targets Platform.
Shares Double-strand break repair: HR versus end joining, Open Targets Platform.
Shares Double-strand break repair: HR versus end joining, Open Targets Platform.
Shares Synthetic lethality: paired dependencies, Double-strand break repair: HR versus end joining.
Shares DNA damage response & homologous recombination, Double-strand break repair: HR versus end joining, Prostate cancer.
Shares DNA damage response & homologous recombination, Prostate cancer.
Shares DNA damage response & homologous recombination, Double-strand break repair: HR versus end joining, Prostate cancer.
Shares Synthetic lethality: paired dependencies, Double-strand break repair: HR versus end joining, Prostate cancer.