Protein:OGG1 |
Protein Summary |
 Gene summary |
| Gene name: OGG1 | ASpdb.0 ID: 4968 | Gene | Gene symbol | OGG1 | Gene ID | 4968 |
| Gene name | 8-oxoguanine DNA glycosylase |
| Synonyms | HMMH|HOGG1|MUTM|OGH1 |
| Cytomap | 3p25.3 |
| Type of gene | protein-coding |
| Description | N-glycosylase/DNA lyase8-hydroxyguanine DNA glycosylaseAP lyaseDNA-apurinic or apyrimidinic site lyaseOGG1 type 1f |
| Modification date | 20240411 |
| UniProtAcc | O15527 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | OGG1 | GO:0000978 | RNA polymerase II cis-regulatory region sequence-specific DNA binding | 27251462 |
| Gene | OGG1 | GO:0003684 | damaged DNA binding | 14706345 |
| Gene | OGG1 | GO:0005634 | nucleus | 19506022 |
| Gene | OGG1 | GO:0005654 | nucleoplasm | 17148573 |
| Gene | OGG1 | GO:0006289 | nucleotide-excision repair | 19506022 |
| Gene | OGG1 | GO:0006979 | response to oxidative stress | 17148573 |
| Gene | OGG1 | GO:0009314 | response to radiation | 17148573 |
| Gene | OGG1 | GO:0016363 | nuclear matrix | 17148573 |
| Gene | OGG1 | GO:0016607 | nuclear speck | 17148573 |
| Gene | OGG1 | GO:0032357 | oxidized purine DNA binding | 14706345 |
| Gene | OGG1 | GO:0032991 | protein-containing complex | 19506022 |
| Gene | OGG1 | GO:1901291 | negative regulation of double-strand break repair via single-strand annealing | 19506022 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| O15527-1 | O15527-1_2xhi_A.pdb | 2XHI | X-ray | 1.55 | A | 10 | 325 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| O15527 | OGG1 | O15527-1 | O15527-2 | 345 | 324 | 317 | 345 | Substitution | VLFSADLRQSRHAQEPPAKRRKGSKGPEG | VSVPRCPP | 317 | 324 |
| O15527 | OGG1 | O15527-1 | O15527-3 | 345 | 410 | 317 | 345 | Substitution | VLFSADLRQSRHAQEPPAKRRKGSKGPEG | TPPSYRCCSVPTCANPAMLRSHQQSAERVPKGRKARWGTLDKEIPQAPSPPFPTSLSPSPPSLMLGRGLPVTTSKARHPQIKQSVCTTRWGGGY | 317 | 410 |
| O15527 | OGG1 | O15527-1 | O15527-4 | 345 | 424 | 317 | 345 | Substitution | VLFSADLRQSRHAQEPPAKRRKGSKGPEG | GLLGNAFDGHQLLRPLIFCQDHLREGPPIGRGDSQGEELEPQLPSSLSSIPYGFCDHCWTKDVDDPPLVTHPSPGSRDGHMTQAWPVKVVSPLATVIGHVMQASLLAL | 317 | 424 |
| O15527 | OGG1 | O15527-1 | O15527-5 | 345 | 357 | 250 | 345 | Substitution | VADCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAKGPSPQTNKELGNFFRSLWGPYAGWAQAVLFSADLRQSRHAQEPPAKRRKGSKGPEG | GLLGNAFDGHQLLRPLIFCQDHLREGPPIGRGDSQGEELEPQLPSSLSSIPYGFCDHCWTKDVDDPPLVTHPSPGSRDGHMTQAWPVKVVSPLATVIGHVMQASLLAL | 250 | 357 |
| O15527 | OGG1 | O15527-1 | O15527-6 | 345 | 195 | 191 | 195 | Substitution | EVEAH | PWQCI | 191 | 195 |
| O15527 | OGG1 | O15527-1 | O15527-6 | 345 | 195 | 196 | 345 | Deletion | none | none | 195 | 195 |
| O15527 | OGG1 | O15527-1 | O15527-7 | 345 | 356 | 317 | 345 | Substitution | VLFSADLRQSRHAQEPPAKRRKGSKGPEG | LCQVITTFMTFLGPHRLDQMPPEELQTSSSRLGGPPWQCI | 317 | 356 |
| O15527 | OGG1 | O15527-1 | O15527-8 | 345 | 322 | 317 | 345 | Substitution | VLFSADLRQSRHAQEPPAKRRKGSKGPEG | AGSDAS | 317 | 322 |
| Multiple sequence alignment of our canonical and alternatively spliced OGG1 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of OGG1 |
| UniProt-id | ENSG | ENST | ENSP |
| O15527-1 | ENSG00000114026.22 | ENST00000344629.12 | ENSP00000342851.7 |
| O15527-2 | ENSG00000114026.22 | ENST00000339511.9 | ENSP00000345520.5 |
| O15527-3 | ENSG00000114026.22 | ENST00000302003.11 | ENSP00000305584.7 |
| O15527-4 | ENSG00000114026.22 | ENST00000302036.12 | ENSP00000306561.7 |
| O15527-5 | ENSG00000114026.22 | ENST00000352937.6 | ENSP00000344899.6 |
| O15527-6 | ENSG00000114026.22 | ENST00000383826.9 | ENSP00000373337.5 |
| O15527-7 | ENSG00000114026.22 | ENST00000302008.12 | ENSP00000305527.8 |
| O15527-8 | ENSG00000114026.22 | ENST00000449570.6 | ENSP00000403598.2 |
| UniProt-id | NM ID | NP ID |
| O15527-1 | NM_002542.5 | NP_002533.1 |
| O15527-2 | NM_016819.3 | NP_058212.1 |
| O15527-3 | NM_016820.3 | NP_058213.1 |
| O15527-4 | NM_016821.2 | NP_058214.1 |
| O15527-5 | NM_016826.2 | NP_058434.1 |
| O15527-6 | NM_016827.2 | NP_058436.1 |
| O15527-7 | NM_016828.2 | NP_058437.1 |
| O15527-8 | NM_016829.2 | NP_058438.1 |
| Amino acid sequences of our canonical and alternatively spliced OGG1 |
| accession_id | Protein sequence |
| O15527-1 | MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTP DELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHG FPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKVADCICLMALDKPQAVPVDVH |
| O15527-2 | MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTP DELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHG FPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKVADCICLMALDKPQAVPVDVH |
| O15527-3 | MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTP DELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHG FPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKVADCICLMALDKPQAVPVDVH MWHIAQRDYSWHPTTSQAKGPSPQTNKELGNFFRSLWGPYAGWAQATPPSYRCCSVPTCANPAMLRSHQQSAERVPKGRKARWGTLDKEI |
| O15527-4 | MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTP DELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHG FPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKVADCICLMALDKPQAVPVDVH MWHIAQRDYSWHPTTSQAKGPSPQTNKELGNFFRSLWGPYAGWAQAGLLGNAFDGHQLLRPLIFCQDHLREGPPIGRGDSQGEELEPQLP |
| O15527-5 | MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTP DELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHG FPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKGLLGNAFDGHQLLRPLIFCQD |
| O15527-6 | MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTP DELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHG |
| O15527-7 | MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTP DELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHG FPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKVADCICLMALDKPQAVPVDVH |
| O15527-8 | MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTP DELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHG FPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKVADCICLMALDKPQAVPVDVH |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| OGG1 (go to UniProt):O15527 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| O15527 | Region | 324 | 345 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=317;End=345 |
| O15527 | Region | 324 | 345 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=317;End=345 |
| O15527 | Region | 324 | 345 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=317;End=345 |
| O15527 | Region | 324 | 345 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=250;End=345 |
| O15527 | Region | 324 | 345 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=196;End=345 |
| O15527 | Region | 324 | 345 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=317;End=345 |
| O15527 | Region | 324 | 345 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=317;End=345 |
| O15527 | Compositional bias | 328 | 345 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=317;End=345 |
| O15527 | Compositional bias | 328 | 345 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=317;End=345 |
| O15527 | Compositional bias | 328 | 345 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=317;End=345 |
| O15527 | Compositional bias | 328 | 345 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=250;End=345 |
| O15527 | Compositional bias | 328 | 345 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=196;End=345 |
| O15527 | Compositional bias | 328 | 345 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=317;End=345 |
| O15527 | Compositional bias | 328 | 345 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=317;End=345 |
Gene Isoform Structures and Expression Levels for OGG1 |
| Gene structures of our canonical and alternative spliced genes of OGG1 * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of O15527-1 |
| 3D view using mol* of O15527-2 |
| 3D view using mol* of O15527-3 |
| 3D view using mol* of O15527-4 |
| 3D view using mol* of O15527-5 |
| 3D view using mol* of O15527-6 |
| 3D view using mol* of O15527-7 |
| 3D view using mol* of O15527-8 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of O15527-1 |
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| pLDDT distribution across the protein length of O15527-2 |
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| pLDDT distribution across the protein length of O15527-3 |
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| pLDDT distribution across the protein length of O15527-4 |
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| pLDDT distribution across the protein length of O15527-5 |
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| pLDDT distribution across the protein length of O15527-6 |
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| pLDDT distribution across the protein length of O15527-7 |
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| pLDDT distribution across the protein length of O15527-8 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of O15527-1 |
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| Ramachandran plot of O15527-2 |
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| Ramachandran plot of O15527-3 |
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| Ramachandran plot of O15527-5 |
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| Ramachandran plot of O15527-6 |
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| Ramachandran plot of O15527-7 |
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| Ramachandran plot of O15527-8 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| O15527-1 | 1.051 | 130 | 1.026 | 305.613 | 0.5 | 0.774 | 0.989 | 0.675 | 1.159 | 0.582 | 0.365 | 41,42,43,45,144,147,148,149,150,151,152,153,155,24 7,248,249,250,253,256,257,266,268,269,270,271,315, 316,319,323,326,327 |
| O15527-2 | 1.065 | 182 | 1.109 | 440.412 | 0.465 | 0.737 | 0.949 | 1.082 | 0.837 | 1.292 | 1.042 | 37,40,41,42,43,45,130,132,144,147,148,149,150,151, 152,153,155,249,250,256,257,266,268,269,270,271,27 3,312,315,316,319,320,322,323,324 |
| O15527-3 | 1.072 | 98 | 1.006 | 229.124 | 0.497 | 0.816 | 1.09 | 0.557 | 1.269 | 0.439 | 0.56 | 41,42,43,45,132,144,147,148,149,150,151,152,155,24 9,250,253,256,257,266,268,269,270,271,315,316,320, 321,324 |
| O15527-4 | 1.232 | 99 | 1.272 | 158.466 | 0.303 | 0.964 | 1.277 | 2.622 | 0.743 | 3.53 | 1.557 | 41,42,43,45,130,132,144,147,152,155,249,253,256,25 7,266,268,270,271,312,315,316,319,320,322,323,332, 333,334 |
| O15527-5 | 0.988 | 97 | 0.932 | 245.588 | 0.555 | 0.697 | 0.919 | 0.277 | 1.263 | 0.22 | 0.77 | 44,46,47,58,59,60,61,95,98,99,134,135,136,137,138, 139,163,179,180,181,182,183,184,222,229 |
| O15527-6 | 0.88 | 68 | 0.773 | 106.673 | 0.524 | 0.711 | 0.969 | 0.387 | 1.315 | 0.294 | 0.352 | 45,46,48,50,57,58,156,159,160,163,164,175,176,177, 178,179 |
| O15527-7 | 0.955 | 120 | 0.961 | 257.25 | 0.623 | 0.63 | 0.809 | 0.255 | 1.095 | 0.232 | 0.663 | 44,46,47,58,59,60,61,62,64,91,92,95,98,99,134,135, 136,137,138,139,163,179,180,181,182,183,184,185,22 1,222,229 |
| O15527-8 | 1.053 | 111 | 1.025 | 338.884 | 0.486 | 0.777 | 0.968 | 0.703 | 1.168 | 0.601 | 1.072 | 37,38,41,42,43,45,130,132,144,147,148,149,150,152, 155,249,250,253,256,257,266,268,270,271,312,315,31 6,319,320 |
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of O15527-1_O15527-1_2xhi_A.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of O15527-1_2xhi_A_O15527-2.pdb |
| 3D view using mol* of O15527-1_2xhi_A_O15527-3.pdb |
| 3D view using mol* of O15527-1_2xhi_A_O15527-4.pdb |
| 3D view using mol* of O15527-1_2xhi_A_O15527-5.pdb |
| 3D view using mol* of O15527-1_2xhi_A_O15527-6.pdb |
| 3D view using mol* of O15527-1_2xhi_A_O15527-7.pdb |
| 3D view using mol* of O15527-1_2xhi_A_O15527-8.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of O15527-1_O15527-2.pdb |
| 3D view using mol* of O15527-1_O15527-3.pdb |
| 3D view using mol* of O15527-1_O15527-4.pdb |
| 3D view using mol* of O15527-1_O15527-5.pdb |
| 3D view using mol* of O15527-1_O15527-6.pdb |
| 3D view using mol* of O15527-1_O15527-7.pdb |
| 3D view using mol* of O15527-1_O15527-8.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/O15527-1_vs_O15527-2.png |
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| ./stats/secondary_structure/figure/O15527-1_vs_O15527-3.png |
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| ./stats/secondary_structure/figure/O15527-1_vs_O15527-4.png |
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| ./stats/secondary_structure/figure/O15527-1_vs_O15527-5.png |
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| ./stats/secondary_structure/figure/O15527-1_vs_O15527-6.png |
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| ./stats/secondary_structure/figure/O15527-1_vs_O15527-7.png |
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| ./stats/secondary_structure/figure/O15527-1_vs_O15527-8.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/O15527-1_vs_O15527-2.png |
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| ./stats/relative_asa/O15527-1_vs_O15527-3.png |
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| ./stats/relative_asa/O15527-1_vs_O15527-4.png |
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| ./stats/relative_asa/O15527-1_vs_O15527-5.png |
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| ./stats/relative_asa/O15527-1_vs_O15527-6.png |
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| ./stats/relative_asa/O15527-1_vs_O15527-7.png |
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| ./stats/relative_asa/O15527-1_vs_O15527-8.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to OGG1 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to OGG1 |
| Previous studies relating to the alternative splicing of OGG1 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| OGG1 | 9681819 | Genetic polymorphisms and alternative splicing of the hOGG1 gene, that is involved in the repair of 8-hydroxyguanine in damaged DNA. | The hOGG1 gene encodes a DNA glycosylase that excises 8-hydroxyguanine (oh8Gua) from damaged DNA. Structural analyses of the hOGG1 gene and its transcripts were performed in normal and lung cancer cells. Due to a genetic polymorphism at codon 326, hOGG1-Ser326 and hOGG1-Cys326 proteins were produced in human cells. Activity in the repair of oh8Gua was greater in hOGG1-Ser326 protein than in hOGG1-Cys326 protein in the complementation assay of an E. coli mutant defective in the repair of oh8Gua. Two isoforms of hOGG1 transcripts produced by alternative splicing encoded distinct hOGG1 proteins: one with and the other without a putative nuclear localization signal. Loss of heterozygosity at the hOGG1 locus was frequently (15/ 23, 62.2%) detected in lung cancer cells, and a cell line NCI-H526 had a mutation leading to the formation of the transcripts encoding a truncated hOGG1 protein. However, the oh8Gua levels in nuclear DNA were similar among lung cancer cells and leukocytes irrespective of the type of hOGG1 proteins expressed. These results suggest that the oh8Gua levels are maintained at a steady level, even though multiple hOGG1 proteins are produced due to genetic polymorphisms, mutations and alternative splicing of the hOGG1 gene. | D008175 | Lung Neoplasms |
| OGG1 | 10775435 | The human OGG1 gene: structure, functions, and its implication in the process of carcinogenesis. | A particularly important stress for all cells is the one produced by reactive oxygen species (ROS) that are formed as byproducts of cell metabolism. Among DNA damages induced by ROS, 8-hydroxyguanine (8-OH-G) is certainly the product that has retained most of the attention in the past few years. The biological relevance of 8-OH-G in DNA has been unveiled by the study of Escherichia coli and Saccharomyces cerevisiae genes involved in the neutralization of the mutagenic effects of 8-OH-G. These genes, fpg and mutY for E. coli and OGG1 for yeast, code for DNA glycosylases. Inactivation of any of those genes leads to a spontaneous mutator phenotype, characterized by the increase in GC to TA transversions. In yeast, the OGG1 gene encodes a DNA glycosylase/AP lyase that excises 8-OH-G from DNA. In human cells, the OGG1 gene is localized on chromosome 3p25 and encodes two forms of hOgg1 protein which result from an alternative splicing of a single messenger RNA. The alpha-hOgg1 protein has a nuclear localization whereas the beta-hOgg1 is targeted to the mitochondrion. Biochemical studies on the alpha-hOgg1 protein show that it is a DNA glycosylase/AP lyase that excises 8-OH-G and Fapy-G from gamma-irradiated DNA. Several approaches have been used to study the biological role of OGG1 in mammalian cells, ranging from its overexpression in cell lines to the generation of homozygous ogg1-/- null mice. Furthermore, to explore a possible role in the prevention of cancer, the cDNA coding for alpha-hOgg1 has been sequenced in human tumors. All these results point to 8-OH-G as an endogenous source of mutations in eukaryotes and to its likely involvement in the process of carcinogenesis. A review of the recent literature on the mammalian Ogg1 proteins, the main repair system involved in the elimination of this mutagenic lesion, is presented. | D009369 | Neoplasms |
| OGG1 | 12509224 | Mitochondrial targeting of human 8-oxoguanine DNA glycosylase hOGG1 is impaired by a somatic mutation found in kidney cancer. | Oxidative damage to mitochondrial DNA (mtDNA) has been implicated as a contributing factor to the origin of many pathological processes. Among the major DNA lesions generated by oxidative stress, 8-oxoguanine (8-oxoG) has a strong mutagenic potential. The main pathway for the repair of this lesion is the base excision repair (BER) initiated by the OGG1 DNA glycosylase. In human cells alternative splicing of the hOGG1 transcript yields two forms of the protein, alpha and beta, that are localised in the nucleus and the mitochondria, respectively. We describe here a hOGG1 somatic mutation, found in a kidney cancer, that modifies the intracellular localisation of beta-hOGG1. The glycine 12 to glutamic acid substitution does not affect the enzymatic activity of the enzyme but lies in what was predicted to be a mitochondrial targeting sequence (MTS). Immunocytochemical localisation experiments show that the G12E mutant protein has diffuse cytoplasmic distribution instead of the mitochondrial localisation found for the wild-type, providing an example of a single amino acid substitution capable of disrupting a MTS. These results imply that these cancer cells are deficient in their mitochondrial 8-oxoG DNA repair activity. | D007680 | Kidney Neoplasms |
Clinically important variants in OGG1 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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