ENTRY ko03410 Pathway NAME Base excision repair DESCRIPTION Base excision repair (BER) is the predominant DNA damage repair pathway for the processing of small base lesions, derived from oxidation and alkylation damages. BER is normally defined as DNA repair initiated by lesion-specific DNA glycosylases and completed by either of the two sub-pathways: short-patch BER where only one nucleotide is replaced and long-patch BER where 2-13 nucleotides are replaced. Each sub-pathway of BER relies on the formation of protein complexes that assemble at the site of the DNA lesion and facilitate repair in a coordinated fashion. This process of complex formation appears to provide an increase in specificity and efficiency to the BER pathway, thereby facilitating the maintenance of genome integrity by preventing the accumulation of highly toxic repair intermediates. CLASS Genetic Information Processing; Replication and repair PATHWAY_MAP ko03410 Base excision repair DBLINKS GO: 0006284 0006285 0006286 0006287 0006288 ORTHOLOGY K03660 N-glycosylase/DNA lyase [EC:3.2.2.- 4.2.99.18] K10773 endonuclease III [EC:3.2.2.- 4.2.99.18] K10567 endonuclease VIII-like 1 [EC:3.2.2.- 4.2.99.18] K10568 endonuclease VIII-like 2 [EC:3.2.2.- 4.2.99.18] K10569 endonuclease VIII-like 3 [EC:3.2.2.- 4.2.99.18] K03648 uracil-DNA glycosylase [EC:3.2.2.27] K10800 single-strand selective monofunctional uracil DNA glycosylase [EC:3.2.2.-] K03575 A/G-specific adenine glycosylase [EC:3.2.2.31] K03652 DNA-3-methyladenine glycosylase [EC:3.2.2.21] K10801 methyl-CpG-binding domain protein 4 [EC:3.2.2.-] K20813 thymine-DNA glycosylase [EC:3.2.2.29] K10771 AP endonuclease 1 [EC:3.1.11.2] K08073 bifunctional polynucleotide phosphatase/kinase [EC:3.1.3.32 2.7.1.78] K10862 tyrosyl-DNA phosphodiesterase 1 [EC:3.1.4.-] K02330 DNA polymerase beta [EC:2.7.7.7 4.2.99.-] K03512 DNA polymerase lambda [EC:2.7.7.7 4.2.99.-] K10802 high mobility group protein B1 K24070 poly [ADP-ribose] polymerase 1 [EC:2.4.2.30] K10798 poly [ADP-ribose] polymerase 2/3/4 [EC:2.4.2.30] K07759 poly(ADP-ribose) glycohydrolase [EC:3.2.1.143] K11687 poly(ADP-ribose) glycohydrolase ARH3 [EC:3.2.1.143] K10863 aprataxin [EC:3.6.1.70 3.6.1.71 3.6.1.72] K10803 DNA-repair protein XRCC1 K02332 DNA polymerase gamma 1 [EC:2.7.7.7] K02333 DNA polymerase gamma 2 K10776 DNA ligase 3 [EC:6.5.1.1] K02327 DNA polymerase delta subunit 1 [EC:2.7.7.7] K02328 DNA polymerase delta subunit 2 K03504 DNA polymerase delta subunit 3 K03505 DNA polymerase delta subunit 4 K02324 DNA polymerase epsilon subunit 1 [EC:2.7.7.7] K02325 DNA polymerase epsilon subunit 2 [EC:2.7.7.7] K02326 DNA polymerase epsilon subunit 3 [EC:2.7.7.7] K03506 DNA polymerase epsilon subunit 4 [EC:2.7.7.7] K04802 proliferating cell nuclear antigen K10754 replication factor C subunit 1 K10755 replication factor C subunit 2/4 K10756 replication factor C subunit 3/5 K04799 flap endonuclease-1 [EC:3.1.-.-] K10747 DNA ligase 1 [EC:6.5.1.1 6.5.1.6 6.5.1.7] K10563 formamidopyrimidine-DNA glycosylase [EC:3.2.2.23 4.2.99.18] K05522 endonuclease VIII [EC:3.2.2.- 4.2.99.18] K01247 DNA-3-methyladenine glycosylase II [EC:3.2.2.21] K13529 AraC family transcriptional regulator, regulatory protein of adaptative response / DNA-3-methyladenine glycosylase II [EC:3.2.2.21] K01246 DNA-3-methyladenine glycosylase I [EC:3.2.2.20] K03649 double-stranded uracil-DNA glycosylase [EC:3.2.2.28] K21929 uracil-DNA glycosylase [EC:3.2.2.27] K01142 exodeoxyribonuclease III [EC:3.1.11.2] K01151 deoxyribonuclease IV [EC:3.1.21.2] K02335 DNA polymerase I [EC:2.7.7.7] K07462 single-stranded-DNA-specific exonuclease [EC:3.1.-.-] K01972 DNA ligase (NAD+) [EC:6.5.1.2] REFERENCE PMID:17893748 AUTHORS Krwawicz J, Arczewska KD, Speina E, Maciejewska A, Grzesiuk E. TITLE Bacterial DNA repair genes and their eukaryotic homologues: 1. Mutations in genes involved in base excision repair (BER) and DNA-end processors and their implication in mutagenesis and human disease. JOURNAL Acta Biochim Pol 54:413-34 (2007) REFERENCE PMID:17337257 AUTHORS Almeida KH, Sobol RW. TITLE A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification. JOURNAL DNA Repair (Amst) 6:695-711 (2007) DOI:10.1016/j.dnarep.2007.01.009 REFERENCE PMID:21665970 AUTHORS Moen MN, Knaevelsrud I, Haugland GT, Grosvik K, Birkeland NK, Klungland A, Bjelland S TITLE Uracil-DNA glycosylase of Thermoplasma acidophilum directs long-patch base excision repair, which is promoted by deoxynucleoside triphosphates and ATP/ADP, into short-patch repair. JOURNAL J Bacteriol 193:4495-508 (2011) DOI:10.1128/JB.00233-11 REFERENCE PMID:11436317 AUTHORS Ikeda S, Seki S. TITLE [Base excision repair: DNA glycosylase and AP endonuclease] JOURNAL Tanpakushitsu Kakusan Koso 46:916-23 (2001) ///