P87175 · APN2_SCHPO
- ProteinDNA-(apurinic or apyrimidinic site) endonuclease 2
- Geneapn2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids523 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA. Provides the majority of the AP-endonuclease (APE) activity. Repairs phleomycin D1-induced DNA damage. Plays a role in oxidative damage repair.
Catalytic activity
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Probably binds two magnesium or manganese ions per subunit.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 42 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 151 | |||||
Sequence: Y | ||||||
Active site | 191 | Proton donor/acceptor | ||||
Sequence: D | ||||||
Binding site | 191 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 193 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Site | 193 | Transition state stabilizer | ||||
Sequence: N | ||||||
Site | 269 | Important for catalytic activity | ||||
Sequence: D | ||||||
Binding site | 294 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 295 | Interaction with DNA substrate | ||||
Sequence: H | ||||||
Binding site | 458 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 461 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 484 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 508 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | DNA-(apurinic or apyrimidinic site) endonuclease activity | |
Molecular Function | double-stranded DNA 3'-5' DNA exonuclease activity | |
Molecular Function | endonuclease activity | |
Molecular Function | phosphodiesterase I activity | |
Molecular Function | phosphoric diester hydrolase activity | |
Molecular Function | zinc ion binding | |
Biological Process | base-excision repair | |
Biological Process | DNA repair |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA-(apurinic or apyrimidinic site) endonuclease 2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionP87175
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 402 | No change in activity; when associated with A-403. | ||||
Sequence: F → A | ||||||
Mutagenesis | 403 | No change in activity; when associated with A-402. | ||||
Sequence: F → A | ||||||
Mutagenesis | 456 | No change in activity; when associated with A-457 and A-458. | ||||
Sequence: P → A | ||||||
Mutagenesis | 457 | No change in activity; when associated with A-456 and A-458. | ||||
Sequence: L → A | ||||||
Mutagenesis | 458 | No change in activity; when associated with A-456 and A-457. | ||||
Sequence: C → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000200019 | 1-523 | DNA-(apurinic or apyrimidinic site) endonuclease 2 | |||
Sequence: MRILSWNVNGIQNPFNYFPWNKKNSYKEIFQELQADVICVQELKMQKDSFPQQYAVVEGFDSYFTFPKIRKGYSGVGFYVKKDVAIPVKAEEGITGILPVRGQKYSYSEAPEHEKIGFFPKDIDRKTANWIDSEGRCILLDFQMFILIGVYCPVNSGENRLEYRRAFYKALRERIERLIKEGNRKIILVGDVNILCNPIDTADQKDIIRESLIPSIMESRQWIRDLLLPSRLGLLLDIGRIQHPTRKGMFTCWNTRLNTRPTNYGTRIDYTLATPDLLPWVQDADIMAEVMGSDHCPVYLDLKEEYEGKKLSNFLSHSKEPPLLSTAHHSAYRPSKNIHSMFQHFNSMKKNKNNSPTQSENVSASASSGSSPTVSRANSVIDVDAYPPEKRRRKEQSKLLSFFAKQKEEKEETNKTEDVSIEVLDNNNESDIGLTVKKKVENGNAWKQIFSERAPPLCEGHKEPCKYLTVRKPGINYGRKFWICARPVGELIKNSNAVSEEDTQPFQCRFFIWDSDWRANSKD |
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 348-378 | Polar residues | ||||
Sequence: MKKNKNNSPTQSENVSASASSGSSPTVSRAN | ||||||
Region | 348-392 | Disordered | ||||
Sequence: MKKNKNNSPTQSENVSASASSGSSPTVSRANSVIDVDAYPPEKRR | ||||||
Zinc finger | 458-517 | GRF-type | ||||
Sequence: CEGHKEPCKYLTVRKPGINYGRKFWICARPVGELIKNSNAVSEEDTQPFQCRFFIWDSDW |
Sequence similarities
Belongs to the DNA repair enzymes AP/ExoA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length523
- Mass (Da)60,313
- Last updated1997-07-01 v1
- ChecksumB2A79AE61579FA1C
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 348-378 | Polar residues | ||||
Sequence: MKKNKNNSPTQSENVSASASSGSSPTVSRAN |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY483158 EMBL· GenBank· DDBJ | AAR83752.1 EMBL· GenBank· DDBJ | mRNA | ||
CU329671 EMBL· GenBank· DDBJ | CAB09119.1 EMBL· GenBank· DDBJ | Genomic DNA |