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
Base excision repair
ko03410

All organismsOrtholog table
Module
M00262  
DNA polymerase delta complex [PATH:ko03410]
M00296  
BER complex [PATH:ko03410]
Disease
H01025  
Familial adenomatous polyposis
Other DBs
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]
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.-]
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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