KEGG   PATHWAY: ko03410Help
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
BRITE hierarchy
Pathway map
ko03410  Base excision repair
ko03410

Ortholog table
Module
M00262  DNA polymerase delta complex [PATH:ko03410]
M00296  BER complex [PATH:ko03410]
Disease
H01025  Familial adenomatous polyposis
H02014  Ataxia-telangiectasia-like syndrome
Other DBs
BSID: 451
GO: 0006284 0006285 0006286 0006287 0006288
Orthology
K10563  formamidopyrimidine-DNA glycosylase [EC:4.2.99.18 3.2.2.23]
K05522  endonuclease VIII [EC:4.2.99.18 3.2.2.-]
K03660  N-glycosylase/DNA lyase [EC:4.2.99.18 3.2.2.-]
K10773  endonuclease III [EC:4.2.99.18]
K10567  endonuclease VIII-like 1 [EC:4.2.99.18 3.2.2.-]
K10568  endonuclease VIII-like 2 [EC:4.2.99.18 3.2.2.-]
K10569  endonuclease VIII-like 3
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]
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]
K01142  exodeoxyribonuclease III [EC:3.1.11.2]
K01151  deoxyribonuclease IV [EC:3.1.21.2]
K10771  AP endonuclease 1 [EC:4.2.99.18]
K10772  AP endonuclease 2 [EC:4.2.99.18]
K02335  DNA polymerase I [EC:2.7.7.7]
K07462  single-stranded-DNA-specific exonuclease [EC:3.1.-.-]
K02330  DNA polymerase beta [EC:4.2.99.- 2.7.7.7]
K03512  DNA polymerase lambda [EC:4.2.99.- 2.7.7.7]
K10802  high mobility group protein B1
K10803  DNA-repair protein XRCC1
K04802  proliferating cell nuclear antigen
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]
K01972  DNA ligase (NAD+) [EC:6.5.1.2]
K10747  DNA ligase 1 [EC:6.5.1.7 6.5.1.6 6.5.1.1]
K10776  DNA ligase 3 [EC:6.5.1.1]
K10798  poly [ADP-ribose] polymerase [EC:2.4.2.30]
K04799  flap endonuclease-1 [EC:3.-.-.-]
Reference
  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
  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
  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
  Authors
Ikeda S, Seki S.
  Title
[Base excision repair: DNA glycosylase and AP endonuclease] Japanese
  Journal
Tanpakushitsu Kakusan Koso 46:916-23 (2001)
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