Q3TIV3 · Q3TIV3_MOUSE
- ProteinPoly [ADP-ribose] polymerase
- GeneParp1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1014 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair.
Promotes AIFM1-mediated apoptosis. This form, which translocates into the cytoplasm following cleavage by caspase-3 (CASP3) and caspase-7 (CASP7) in response to apoptosis, is auto-poly-ADP-ribosylated and serves as a poly-ADP-ribose carrier to induce AIFM1-mediated apoptosis.
This cleavage form irreversibly binds to DNA breaks and interferes with DNA repair, promoting DNA damage-induced apoptosis.
Catalytic activity
- L-aspartyl-[protein] + NAD+ = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamideThis reaction proceeds in the forward direction.
- L-glutamyl-[protein] + NAD+ = 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + nicotinamideThis reaction proceeds in the forward direction.
- L-histidyl-[protein] + NAD+ = N(tele)-(ADP-D-ribosyl)-L-histidyl-[protein] + nicotinamide + H+This reaction proceeds in the forward direction.
- L-seryl-[protein] + NAD+ = O-(ADP-D-ribosyl)-L-seryl-[protein] + nicotinamide + H+This reaction proceeds in the forward direction.
- L-tyrosyl-[protein] + NAD+ = O-(ADP-D-ribosyl)-L-tyrosyl-[protein] + nicotinamide + H+This reaction proceeds in the forward direction.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | NAD binding | |
Molecular Function | NAD+-protein poly-ADP-ribosyltransferase activity | |
Molecular Function | NAD+-protein-histidine ADP-ribosyltransferase activity | |
Molecular Function | NAD+-protein-serine ADP-ribosyltransferase activity | |
Molecular Function | NAD+-protein-tyrosine ADP-ribosyltransferase activity | |
Molecular Function | nucleotidyltransferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | DNA repair | |
Biological Process | innate immune response |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePoly [ADP-ribose] polymerase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ3TIV3
Organism-specific databases
Subcellular Location
PTM/Processing
Interaction
Subunit
Interacts (when auto-poly-ADP-ribosylated) with AIFM1.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 9-93 | PARP-type | |||
Domain | 113-203 | PARP-type | |||
Region | 198-235 | Disordered | |||
Domain | 386-462 | BRCT | |||
Region | 493-521 | Disordered | |||
Compositional bias | 506-521 | Basic and acidic residues | |||
Domain | 542-638 | WGR | |||
Domain | 662-779 | PARP alpha-helical | |||
Domain | 788-1014 | PARP catalytic | |||
Sequence similarities
Belongs to the ARTD/PARP family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,014
- Mass (Da)112,711
- Last updated2005-10-11 v1
- Checksum4D2168E4CB3F4639
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 506-521 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK167699 EMBL· GenBank· DDBJ | BAE39743.1 EMBL· GenBank· DDBJ | mRNA |