KEGG   PATHWAY: hsa03410Help
Entry
hsa03410                    Pathway                                

Name
Base excision repair - Homo sapiens (human)
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
hsa03410

All organismsOrtholog table
Module
DNA polymerase delta complex [PATH:hsa03410]
BER complex [PATH:hsa03410]
Disease
H01025  
Familial adenomatous polyposis
Drug
D09692  
Veliparib (USAN/INN)
D09730  
Olaparib (JAN/USAN/INN)
D09913  
Iniparib (USAN/INN)
D10079  
Rucaparib (USAN/INN)
D10157  
Rucaparib phosphate (USAN)
Other DBs
Organism
Homo sapiens (human) [GN:hsa]
Gene
4968  
OGG1; 8-oxoguanine DNA glycosylase [KO:K03660] [EC:4.2.99.18 3.2.2.-]
4913  
NTHL1; nth like DNA glycosylase 1 [KO:K10773] [EC:4.2.99.18]
79661  
NEIL1; nei like DNA glycosylase 1 [KO:K10567] [EC:4.2.99.18 3.2.2.-]
252969  
NEIL2; nei like DNA glycosylase 2 [KO:K10568] [EC:4.2.99.18 3.2.2.-]
55247  
NEIL3; nei like DNA glycosylase 3 [KO:K10569]
7374  
UNG; uracil DNA glycosylase [KO:K03648] [EC:3.2.2.27]
23583  
SMUG1; single-strand-selective monofunctional uracil-DNA glycosylase 1 [KO:K10800] [EC:3.2.2.-]
4595  
MUTYH; mutY DNA glycosylase [KO:K03575] [EC:3.2.2.-]
4350  
MPG; N-methylpurine DNA glycosylase [KO:K03652] [EC:3.2.2.21]
8930  
MBD4; methyl-CpG binding domain 4, DNA glycosylase [KO:K10801] [EC:3.2.2.-]
6996  
TDG; thymine DNA glycosylase [KO:K20813] [EC:3.2.2.29]
328  
APEX1; apurinic/apyrimidinic endodeoxyribonuclease 1 [KO:K10771] [EC:4.2.99.18]
27301  
APEX2; apurinic/apyrimidinic endodeoxyribonuclease 2 [KO:K10772] [EC:4.2.99.18]
5423  
POLB; DNA polymerase beta [KO:K02330] [EC:4.2.99.- 2.7.7.7]
27343  
POLL; DNA polymerase lambda [KO:K03512] [EC:4.2.99.- 2.7.7.7]
3146  
HMGB1; high mobility group box 1 [KO:K10802]
7515  
XRCC1; X-ray repair cross complementing 1 [KO:K10803]
5111  
PCNA; proliferating cell nuclear antigen [KO:K04802]
5424  
POLD1; DNA polymerase delta 1, catalytic subunit [KO:K02327] [EC:2.7.7.7]
5425  
POLD2; DNA polymerase delta 2, accessory subunit [KO:K02328]
10714  
POLD3; DNA polymerase delta 3, accessory subunit [KO:K03504]
57804  
POLD4; DNA polymerase delta 4, accessory subunit [KO:K03505]
5426  
POLE; DNA polymerase epsilon, catalytic subunit [KO:K02324] [EC:2.7.7.7]
5427  
POLE2; DNA polymerase epsilon 2, accessory subunit [KO:K02325] [EC:2.7.7.7]
54107  
POLE3; DNA polymerase epsilon 3, accessory subunit [KO:K02326] [EC:2.7.7.7]
56655  
POLE4; DNA polymerase epsilon 4, accessory subunit [KO:K03506] [EC:2.7.7.7]
3978  
LIG1; DNA ligase 1 [KO:K10747] [EC:6.5.1.7 6.5.1.6 6.5.1.1]
3980  
LIG3; DNA ligase 3 [KO:K10776] [EC:6.5.1.1]
10038  
PARP2; poly(ADP-ribose) polymerase 2 [KO:K10798] [EC:2.4.2.30]
142  
PARP1; poly(ADP-ribose) polymerase 1 [KO:K10798] [EC:2.4.2.30]
10039  
PARP3; poly(ADP-ribose) polymerase family member 3 [KO:K10798] [EC:2.4.2.30]
143  
PARP4; poly(ADP-ribose) polymerase family member 4 [KO:K10798] [EC:2.4.2.30]
2237  
FEN1; flap structure-specific endonuclease 1 [KO:K04799] [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)
KO pathway
 
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