CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000474
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 N-glycosylase/DNA lyase 
Protein Synonyms/Alias
 8-oxoguanine DNA glycosylase; DNA-(apurinic or apyrimidinic site) lyase; AP lyase 
Gene Name
 OGG1 
Gene Synonyms/Alias
 MMH; MUTM; OGH1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
198EVEAHLRKLGLGYRAubiquitination[1]
289HPTTSQAKGPSPQTNubiquitination[1]
297GPSPQTNKELGNFFRubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 
Functional Description
 DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N- methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta- lyase activity that nicks DNA 3' to the lesion. 
Sequence Annotation
 ACT_SITE 249 249 Schiff-base intermediate with DNA.
 BINDING 149 149 DNA.
 BINDING 154 154 DNA.
 BINDING 204 204 DNA.
 BINDING 266 266 8-oxoguanine; via carbonyl oxygen.
 BINDING 268 268 8-oxoguanine.
 BINDING 270 270 DNA.
 BINDING 287 287 DNA.
 BINDING 315 315 8-oxoguanine.
 BINDING 319 319 8-oxoguanine.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; DNA damage; DNA repair; Glycosidase; Hydrolase; Lyase; Mitochondrion; Multifunctional enzyme; Nucleus; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 345 AA 
Protein Sequence
MPARALLPRR MGHRTLASTP ALWASIPCPR SELRLDLVLP SGQSFRWREQ SPAHWSGVLA 60
DQVWTLTQTE EQLHCTVYRG DKSQASRPTP DELEAVRKYF QLDVTLAQLY HHWGSVDSHF 120
QEVAQKFQGV RLLRQDPIEC LFSFICSSNN NIARITGMVE RLCQAFGPRL IQLDDVTYHG 180
FPSLQALAGP EVEAHLRKLG LGYRARYVSA SARAILEEQG GLAWLQQLRE SSYEEAHKAL 240
CILPGVGTKV ADCICLMALD KPQAVPVDVH MWHIAQRDYS WHPTTSQAKG PSPQTNKELG 300
NFFRSLWGPY AGWAQAGLLG NAFDGHQLLR PLIFCQDHLR EGPPIGRGDS QGEELEPQLP 360
SSLSSIPYGF CDHCWTKDVD DPPLVTHPSP GSRDGHMTQA WPVKVVSPLA TVIGHVMQAS 420
LLAL 424 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0016363; C:nuclear matrix; IDA:UniProtKB.
 GO:0016607; C:nuclear speck; IDA:UniProtKB.
 GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IEA:Compara.
 GO:0003684; F:damaged DNA binding; TAS:ProtInc.
 GO:0004519; F:endonuclease activity; TAS:ProtInc.
 GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; TAS:ProtInc.
 GO:0002526; P:acute inflammatory response; IEA:Compara.
 GO:0071276; P:cellular response to cadmium ion; IEA:Compara.
 GO:0045007; P:depurination; TAS:Reactome.
 GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
 GO:0033158; P:regulation of protein import into nucleus, translocation; IDA:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IMP:UniProtKB.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0032355; P:response to estradiol stimulus; IEA:Compara.
 GO:0045471; P:response to ethanol; IEA:Compara.
 GO:0051593; P:response to folic acid; IEA:Compara.
 GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
 GO:0009314; P:response to radiation; IDA:UniProtKB. 
Interpro
 IPR011257; DNA_glycosylase.
 IPR003265; HhH-GPD_domain.
 IPR023170; HTH_base_excis_C.
 IPR004577; Ogg.
 IPR012904; OGG_N. 
Pfam
 PF00730; HhH-GPD
 PF07934; OGG_N 
SMART
 SM00478; ENDO3c 
PROSITE
  
PRINTS