DNA Polymerase Kappa/POLK

The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity.

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.

Belongs to the DNA polymerase type-Y family.

Detected at low levels in testis, spleen, prostate and ovary. Detected at very low levels in kidney, colon, brain, heart, liver, lung, placenta, pancreas and peripheral blood leukocytes.

• Nucleus
• Detected throughout the nucleus and at replication foci (PubMed:12414988). Recruited to DNA damage sites in response to ultraviolet irradiation: N6-methyladenosine (m6A)-containing mRNAs accumulate in the vicinity of DNA damage sites and their presence is required to recruit POLK (PubMed:28297716).

DINB1, POLK, DNA polymerase kappa, DINB protein, DINP

• entrezGene:51426
• omim:605650
• swissprot:Q9UBT6

Proteins

Immunology & Infectious Disease

98809Da