DNA polymerase kappa; DINB protein; DINP (POLK, DINB1)
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Function
- DNA polymerase specifically involved in DNA repair
- translesion synthesis
- other high-fidelity DNA polymerases cannot proceed
- DNA synthesis stalls
- inserts the correct base causes frequent base transitions, transversions and frameshifts.
- lacks 3'-5' proofreading exonuclease activity
- forms a Schiff base with 5'-deoxyribose phosphate at abasic sites
- does not have lyase activity
- binds REV1L, PCNA
- Optimum pH is 6.5-7.5;
- Optimum temperature is 37 degrees Celsius
Structure
- the catalytic core consists of fingers, palm & thumb subdomains, but the fingers & 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 & nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation & low processivity
- belongs to the DNA polymerase type-Y family
- contains 2 UBZ-type Zn+2 fingers
- contains 1 umuC domain
Compartment
nucleus, replication foci
Alternative splicing
named isoforms=4
Expression
- expressed at low levels in testis, spleen, prostate, ovary > kidney, colon, brain, heart, liver, lung, placenta, pancreas, peripheral blood leukocytes
Notes
- the catalytic core allows higher rates of misincorporation than high-fidelity polymerases & relatively low processivity
More general terms
References
- ↑ UniProt http://www.uniprot.org/uniprot/Q9UBT6.html
- ↑ NIEHS-SNPs http://egp.gs.washington.edu/data/polk/