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 K01142 xthA, xth; exodeoxyribonuclease III [EC:3.1.11.2] K01151 nfo; deoxyribonuclease IV [EC:3.1.21.2] K01246 tag; DNA-3-methyladenine glycosylase I [EC:3.2.2.20] K01247 alkA; DNA-3-methyladenine glycosylase II [EC:3.2.2.21] K01972 E6.5.1.2, ligA, ligB; DNA ligase (NAD+) [EC:6.5.1.2] K02324 POLE; DNA polymerase epsilon subunit 1 [EC:2.7.7.7] K02325 POLE2; DNA polymerase epsilon subunit 2 [EC:2.7.7.7] K02326 POLE3; DNA polymerase epsilon subunit 3 [EC:2.7.7.7] K02327 POLD1; DNA polymerase delta subunit 1 [EC:2.7.7.7] K02328 POLD2; DNA polymerase delta subunit 2 K02330 POLB; DNA polymerase beta [EC:2.7.7.7 4.2.99.-] K02332 POLG; DNA polymerase gamma 1 [EC:2.7.7.7] K02333 POLG2; DNA polymerase gamma 2 K02335 polA; DNA polymerase I [EC:2.7.7.7] K03504 POLD3; DNA polymerase delta subunit 3 K03505 POLD4; DNA polymerase delta subunit 4 K03506 POLE4; DNA polymerase epsilon subunit 4 [EC:2.7.7.7] K03512 POLL; DNA polymerase lambda [EC:2.7.7.7 4.2.99.-] K03575 mutY; A/G-specific adenine glycosylase [EC:3.2.2.31] K03648 UNG, UDG; uracil-DNA glycosylase [EC:3.2.2.27] K03649 mug; double-stranded uracil-DNA glycosylase [EC:3.2.2.28] K03652 MPG; DNA-3-methyladenine glycosylase [EC:3.2.2.21] K03660 OGG1; N-glycosylase/DNA lyase [EC:3.2.2.- 4.2.99.18] K04799 FEN1, RAD2; flap endonuclease-1 [EC:3.1.-.-] K04802 PCNA; proliferating cell nuclear antigen K05522 nei; endonuclease VIII [EC:3.2.2.- 4.2.99.18] K07462 recJ; single-stranded-DNA-specific exonuclease [EC:3.1.-.-] K07759 PARG; poly(ADP-ribose) glycohydrolase [EC:3.2.1.143] K08073 PNKP; bifunctional polynucleotide phosphatase/kinase [EC:3.1.3.32 2.7.1.78] K10563 mutM, fpg; formamidopyrimidine-DNA glycosylase [EC:3.2.2.23 4.2.99.18] K10567 NEIL1; endonuclease VIII-like 1 [EC:3.2.2.- 4.2.99.18] K10568 NEIL2; endonuclease VIII-like 2 [EC:3.2.2.- 4.2.99.18] K10569 NEIL3; endonuclease VIII-like 3 [EC:3.2.2.- 4.2.99.18] K10747 LIG1; DNA ligase 1 [EC:6.5.1.1 6.5.1.6 6.5.1.7] K10754 RFC1; replication factor C subunit 1 K10755 RFC2_4; replication factor C subunit 2/4 K10756 RFC3_5; replication factor C subunit 3/5 K10771 APEX1; AP endonuclease 1 [EC:3.1.11.2] K10773 NTHL1, nth; endonuclease III [EC:3.2.2.- 4.2.99.18] K10776 LIG3; DNA ligase 3 [EC:6.5.1.1] K10798 PARP3_4; protein mono-ADP-ribosyltransferase 3/4 [EC:2.4.2.-] K10800 SMUG1; single-strand selective monofunctional uracil DNA glycosylase [EC:3.2.2.-] K10801 MBD4; methyl-CpG-binding domain protein 4 [EC:3.2.2.-] K10802 HMGB1; high mobility group protein B1 K10803 XRCC1; DNA-repair protein XRCC1 K10862 TDP1; tyrosyl-DNA phosphodiesterase 1 [EC:3.1.4.-] K10863 APTX; aprataxin [EC:3.6.1.70 3.6.1.71 3.6.1.72] K11687 ADPRHL2; poly(ADP-ribose) glycohydrolase ARH3 [EC:3.2.1.143] K13529 ada-alkA; AraC family transcriptional regulator, regulatory protein of adaptative response / DNA-3-methyladenine glycosylase II [EC:3.2.2.21] K20813 TDG; thymine-DNA glycosylase [EC:3.2.2.29] K21929 udg; uracil-DNA glycosylase [EC:3.2.2.27] K24070 PARP1; poly [ADP-ribose] polymerase 1 K28005 PARP2; poly [ADP-ribose] polymerase 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) ///