KEGG   PATHWAY: sfm03410
Entry
sfm03410                    Pathway                                

Name
Base excision repair - Scleropages formosus (Asian bonytongue)
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
sfm03410  Base excision repair
sfm03410

Other DBs
GO: 0006284 0006285 0006286 0006287 0006288
Organism
Scleropages formosus (Asian bonytongue) [GN:sfm]
Gene
108940258  ogg1; N-glycosylase/DNA lyase [KO:K03660] [EC:3.2.2.- 4.2.99.18]
108939127  nthl1; endonuclease III-like protein 1 [KO:K10773] [EC:4.2.99.18]
108925953  neil3; endonuclease 8-like 3 isoform X1 [KO:K10569]
108932554  ung; uracil-DNA glycosylase [KO:K03648] [EC:3.2.2.27]
108933863  uracil-DNA glycosylase-like [KO:K03648] [EC:3.2.2.27]
108918353  smug1; single-strand selective monofunctional uracil DNA glycosylase [KO:K10800] [EC:3.2.2.-]
108935851  mpg; DNA-3-methyladenine glycosylase isoform X1 [KO:K03652] [EC:3.2.2.21]
108940251  mbd4; methyl-CpG-binding domain protein 4 [KO:K10801] [EC:3.2.2.-]
108920955  G/T mismatch-specific thymine DNA glycosylase-like [KO:K20813] [EC:3.2.2.29]
108920957  G/T mismatch-specific thymine DNA glycosylase-like [KO:K20813] [EC:3.2.2.29]
108935940  apex1; DNA-(apurinic or apyrimidinic site) lyase [KO:K10771] [EC:4.2.99.18]
108940012  uncharacterized protein LOC108940012 isoform X1 [KO:K10771] [EC:4.2.99.18]
108918403  apex2; DNA-(apurinic or apyrimidinic site) lyase 2 [KO:K10772] [EC:4.2.99.18]
108920118  polb; DNA polymerase beta [KO:K02330] [EC:2.7.7.7 4.2.99.-]
108933662  poll; DNA polymerase lambda [KO:K03512] [EC:2.7.7.7 4.2.99.-]
108936270  high mobility group protein B1-like [KO:K10802]
108941932  high mobility group protein B1-like [KO:K10802]
108919203  xrcc1; DNA repair protein XRCC1 [KO:K10803]
108933423  proliferating cell nuclear antigen-like [KO:K04802]
108940373  proliferating cell nuclear antigen [KO:K04802]
108941735  pold1; DNA polymerase delta catalytic subunit [KO:K02327] [EC:2.7.7.7]
108940334  pold2; DNA polymerase delta subunit 2 [KO:K02328]
108924799  pold3; DNA polymerase delta subunit 3 isoform X1 [KO:K03504]
108925891  pold4; DNA polymerase delta subunit 4 [KO:K03505]
108932609  pole; DNA polymerase epsilon catalytic subunit A [KO:K02324] [EC:2.7.7.7]
108941466  pole2; DNA polymerase epsilon subunit 2 [KO:K02325] [EC:2.7.7.7]
108922695  pole3; DNA polymerase epsilon subunit 3 [KO:K02326] [EC:2.7.7.7]
108921530  pole4; DNA polymerase epsilon subunit 4 [KO:K03506] [EC:2.7.7.7]
108937809  lig1; DNA ligase 1 isoform X1 [KO:K10747] [EC:6.5.1.1 6.5.1.6 6.5.1.7]
108928279  lig3; DNA ligase 3 [KO:K10776] [EC:6.5.1.1]
108923980  parp1; poly [ADP-ribose] polymerase 1 [KO:K24070] [EC:2.4.2.30]
108923435  parp3; protein mono-ADP-ribosyltransferase PARP3 [KO:K10798] [EC:2.4.2.30]
108937870  parp2; poly [ADP-ribose] polymerase 2 isoform X1 [KO:K10798] [EC:2.4.2.30]
108927667  fen1; flap endonuclease 1 [KO:K04799] [EC:3.-.-.-]
108933391  probable flap endonuclease 1 homolog isoform X1 [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
ko03410   
LinkDB

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