EC Number   |
General Information |
Reference |
|---|
   3.1.3.32 | evolution |
differences between PfPNKP and the other PNKP Walker A box/P loops: the sequence of the P-loop consensus sequence is hGxPGxGKSTh (h is hydrophobic, x is any amino acid), whereas the sequence of the P-loop of PfPNKP is IGPPGCGKTFL. Second, the difference between glutamic acid at position 330 of PfPNKP |
723130 |
| 3.1.3.32 | malfunction |
mutations result in severe neurological disease |
705853 |
| 3.1.3.32 | malfunction |
mutations that lead to alterations in PNKP, similar to mutations in genes encoding other strand break repair proteins, are associated with a severe autosomal recessive neurological disorder |
716975 |
| 3.1.3.32 | malfunction |
pnk1pku70 and pnk1rhp51 double mutants are more sensitive to gamma-radiation than single mutants. Mutation pnk1apn2 is synthetically lethal. But the nth1pnk1apn2 and tdp1pnk1apn2 triple mutants are viable, implying that single-strand breaks with 3'-blocked termini produced by Nth1 and Tdp1 contribute to synthetic lethality |
722101 |
| 3.1.3.32 | metabolism |
aprataxin polynucleotide kinase/phosphatase-like factor (APLF) facilitates nonhomologous end joining (NHEJ) and associates with the core NHEJ components XRCC4-DNA ligase IV and Ku. The APLF-Ku interaction is functionally important in DNA repair and may be important for APLF stability |
730016 |
| 3.1.3.32 | metabolism |
interaction between XRCC1 and polynucleotide kinase 3'-phosphatase is critical for the retention of XRCC1 at DNA damage sites and DNA damage repair |
730000 |
| 3.1.3.32 | metabolism |
Pnk1 and Apn2 may function in parallel pathways essential for the repair of endogenous DNA damage |
722101 |
| 3.1.3.32 | more |
PNKP function is modulated by interaction with the DNA repair scaffold proteins XRCC1 and XRCC4, which is mediated by binding of the PNKP FHA domain to phosphorylated motifs on XRCC1 and XRCC4, overview |
716975 |
| 3.1.3.32 | more |
PNKP function is modulated by interaction with the DNA repair scaffold proteins XRCC1 and XRCC4, which is mediated by binding of the PNKP FHA domain to phosphorylated motifs on XRCC1 and XRCC4, overview. The crystal structure of murine PNKP shows that the two catalytic active sites are positioned on the same side of the protein |
716975 |
| 3.1.3.32 | physiological function |
DNA 3'-phosphatases play a unique role in repair of double strand breaks induced by DNA damaging agents, such as ionizing radioation or oxidative stress |
714696 |
