Q3TIV3 · Q3TIV3_MOUSE

  • Protein
    Poly [ADP-ribose] polymerase
  • Gene
    Parp1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    4/5

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

GO annotations

AspectTerm
Cellular Componentchromosome
Cellular Componentnucleus
Molecular FunctionDNA binding
Molecular FunctionNAD binding
Molecular FunctionNAD+-protein poly-ADP-ribosyltransferase activity
Molecular FunctionNAD+-protein-histidine ADP-ribosyltransferase activity
Molecular FunctionNAD+-protein-serine ADP-ribosyltransferase activity
Molecular FunctionNAD+-protein-tyrosine ADP-ribosyltransferase activity
Molecular Functionnucleotidyltransferase activity
Molecular Functionzinc ion binding
Biological ProcessDNA repair
Biological Processinnate immune response

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Poly [ADP-ribose] polymerase
  • EC number

Gene names

    • Name
      Parp1

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q3TIV3

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts (when auto-poly-ADP-ribosylated) with AIFM1.

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain9-93PARP-type
Domain113-203PARP-type
Region198-235Disordered
Domain386-462BRCT
Region493-521Disordered
Compositional bias506-521Basic and acidic residues
Domain542-638WGR
Domain662-779PARP alpha-helical
Domain788-1014PARP catalytic

Sequence similarities

Belongs to the ARTD/PARP family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,014
  • Mass (Da)
    112,711
  • Last updated
    2005-10-11 v1
  • Checksum
    4D2168E4CB3F4639
MAEASERLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRQPDVEVDGFSELRWDDQQKVKKTAEAGGVAGKGQDGSGGKAEKTLGDFLAEYAKSNRSMCKGCLEKIEKGQMRLSKKMVDPEKPQLGMIDRWYHPTCFVKKRDELGFRPEYSASQLKGFSLLSAEDKEALKKQLPAIKNEGKRKGDEVDGTDEVAKKKSKKGKDKDSSKLEKALKAQNELIWNIKDELKKACSTNDLKELLIFNQQQVPSGESAILDRVADGMAFGALLPCKECSGQLVFKSDAYYCTGDVTAWTKCMVKTQNPSRKEWVTPKEFREISYLKKLKVKKQDRIFPPESSAPAPLALPLSVTSAPTAVNSSAPADKPLSNMKILTLGKLSQNKDEAKAVIEKLGGKLTGSANKASLCISTKKEVEKMSKKMEEVKAANVRVVCEDFLQDVSASTKSLQELLSAHSLSSWGAEVKAEPGEVVASKGKSAAPSKKSKGAVKEEGVNKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKESRYWIFRSWGRVGTVIGSNKLEQMPSKEDAVEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVKPGTKSKLPKPVQELVGMIFDVESMKKALVEYEIDLQKMPLGKLSRRQIQAAYSILSEVQQAVSQGSSESQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEVIRKYVKNTHATTHNAYDLEVIDIFKIEREGESQRYKPFRQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSASITLEGVEVPLGTGIPSGVNDTCLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias506-521Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK167699
EMBL· GenBank· DDBJ
BAE39743.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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