KEGG   PATHWAY: fab03410
Entry
fab03410                    Pathway                                
Name
Base excision repair - Ficedula albicollis (collared flycatcher)
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
fab03410  Base excision repair
fab03410

Other DBs
GO: 0006284 0006285 0006286 0006287 0006288
Organism
Ficedula albicollis (collared flycatcher) [GN:fab]
Gene
101813974  OGG1; 8-oxoguanine DNA glycosylase [KO:K03660] [EC:3.2.2.- 4.2.99.18]
101818534  NTHL1; nth like DNA glycosylase 1 [KO:K10773] [EC:3.2.2.- 4.2.99.18]
101818856  NEIL1; nei like DNA glycosylase 1 [KO:K10567] [EC:3.2.2.- 4.2.99.18]
101816176  NEIL2; nei like DNA glycosylase 2 [KO:K10568] [EC:3.2.2.- 4.2.99.18]
101816896  NEIL3; nei like DNA glycosylase 3 [KO:K10569] [EC:3.2.2.- 4.2.99.18]
101818923  UNG; uracil DNA glycosylase [KO:K03648] [EC:3.2.2.27]
101812578  MUTYH; mutY DNA glycosylase [KO:K03575] [EC:3.2.2.31]
101809810  MPG; N-methylpurine DNA glycosylase [KO:K03652] [EC:3.2.2.21]
101814817  MBD4; methyl-CpG binding domain 4, DNA glycosylase [KO:K10801] [EC:3.2.2.-]
101813146  TDG; thymine DNA glycosylase [KO:K20813] [EC:3.2.2.29]
101808472  TDP1; tyrosyl-DNA phosphodiesterase 1 [KO:K10862] [EC:3.1.4.-]
101818872  POLB; DNA polymerase beta [KO:K02330] [EC:2.7.7.7 4.2.99.-]
101812248  POLL; DNA polymerase lambda [KO:K03512] [EC:2.7.7.7 4.2.99.-]
101821040  HMGB1; high mobility group box 1 [KO:K10802]
101822111  PARP1; poly(ADP-ribose) polymerase 1 [KO:K24070] [EC:2.4.2.30]
101808625  PARP3; poly [ADP-ribose] polymerase 3 [KO:K10798] [EC:2.4.2.30]
101810550  PARG; poly(ADP-ribose) glycohydrolase [KO:K07759] [EC:3.2.1.143]
101810696  ADPRHL2; ADP-ribosylhydrolase like 2 [KO:K11687] [EC:3.2.1.143]
101807349  APTX; aprataxin [KO:K10863] [EC:3.6.1.70 3.6.1.71 3.6.1.72]
101807741  XRCC1; X-ray repair cross complementing 1 [KO:K10803]
101810621  POLG; DNA polymerase gamma, catalytic subunit [KO:K02332] [EC:2.7.7.7]
107604015  POLG2; DNA polymerase gamma 2, accessory subunit [KO:K02333]
101808635  LIG3; DNA ligase 3 [KO:K10776] [EC:6.5.1.1]
101805692  POLD2; DNA polymerase delta 2, accessory subunit [KO:K02328]
101819521  POLD3; DNA polymerase delta 3, accessory subunit [KO:K03504]
101818590  POLD4; DNA polymerase delta 4, accessory subunit [KO:K03505]
101811602  POLE; DNA polymerase epsilon, catalytic subunit [KO:K02324] [EC:2.7.7.7]
101807958  POLE2; DNA polymerase epsilon 2, accessory subunit [KO:K02325] [EC:2.7.7.7]
101819577  POLE3; DNA polymerase epsilon 3, accessory subunit [KO:K02326] [EC:2.7.7.7]
101819262  POLE4; DNA polymerase epsilon 4, accessory subunit [KO:K03506] [EC:2.7.7.7]
101812857  PCNA; proliferating cell nuclear antigen [KO:K04802]
101816055  RFC1; replication factor C subunit 1 [KO:K10754]
101812058  RFC2; replication factor C subunit 2 [KO:K10755]
101809861  RFC4; replication factor C subunit 4 [KO:K10755]
101817693  RFC3; replication factor C subunit 3 [KO:K10756]
101820558  RFC5; replication factor C subunit 5 [KO:K10756]
101810419  FEN1; flap structure-specific endonuclease 1 [KO:K04799] [EC:3.1.-.-]
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]
  Journal
Tanpakushitsu Kakusan Koso 46:916-23 (2001)
KO pathway
ko03410   
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