Q3ULW8 · PARP3_MOUSE

  • Protein
    Protein mono-ADP-ribosyltransferase PARP3
  • Gene
    Parp3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins and plays a key role in the response to DNA damage (PubMed:21270334, PubMed:24598253).
Mediates mono-ADP-ribosylation of glutamate, aspartate or lysine residues on target proteins (By similarity).
In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (By similarity).
Involved in DNA repair by mediating mono-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism, such as histone H2B, XRCC5 and XRCC6 (By similarity).
ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks (By similarity).
Involved in single-strand break repair by catalyzing mono-ADP-ribosylation of histone H2B on 'Glu-2' (H2BE2ADPr) of nucleosomes containing nicked DNA (By similarity).
Cooperates with the XRCC5-XRCC6 (Ku80-Ku70) heterodimer to limit end-resection thereby promoting accurate NHEJ (By similarity).
Suppresses G-quadruplex (G4) structures in response to DNA damage (By similarity).
Associates with a number of DNA repair factors and is involved in the response to exogenous and endogenous DNA strand breaks (PubMed:21270334).
Together with APLF, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ) (By similarity).
May link the DNA damage surveillance network to the mitotic fidelity checkpoint (By similarity).
Acts as a negative regulator of immunoglobulin class switch recombination, probably by controlling the level of AICDA /AID on the chromatin (PubMed:26000965).
In addition to proteins, also able to ADP-ribosylate DNA: mediates DNA mono-ADP-ribosylation of DNA strand break termini via covalent addition of a single ADP-ribose moiety to a 5'- or 3'-terminal phosphate residues in DNA containing multiple strand breaks (By similarity).

Catalytic activity

GO annotations

AspectTerm
Cellular Componentcentriole
Cellular Componentcentrosome
Cellular Componentcytoplasm
Cellular Componentintercellular bridge
Cellular Componentnuclear body
Cellular Componentnucleolus
Cellular Componentsite of double-strand break
Molecular FunctionNAD DNA ADP-ribosyltransferase activity
Molecular FunctionNAD+ ADP-ribosyltransferase activity
Molecular FunctionNAD+- protein-aspartate ADP-ribosyltransferase activity
Molecular FunctionNAD+- protein-lysine ADP-ribosyltransferase activity
Molecular FunctionNAD+-protein ADP-ribosyltransferase activity
Molecular FunctionNAD+-protein-glutamate ADP-ribosyltransferase activity
Molecular Functionnucleotidyltransferase activity
Biological ProcessDNA ADP-ribosylation
Biological Processdouble-strand break repair
Biological Processnegative regulation of isotype switching
Biological Processpositive regulation of DNA ligation
Biological Processpositive regulation of double-strand break repair via nonhomologous end joining
Biological Processprotein auto-ADP-ribosylation
Biological Processprotein localization to site of double-strand break
Biological Processregulation of mitotic spindle organization
Biological Processtelomere maintenance

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein mono-ADP-ribosyltransferase PARP3
  • EC number
  • Alternative names
    • ADP-ribosyltransferase diphtheria toxin-like 3
      (ARTD3
      )
    • DNA ADP-ribosyltransferase PARP3
      (EC:2.4.2.-
      ) . EC:2.4.2.- (UniProtKB | ENZYME | Rhea)
    • NAD(+) ADP-ribosyltransferase 3
      (ADPRT-3
      )
    • Poly [ADP-ribose] polymerase 3
      (PARP-3
      )
    • Poly[ADP-ribose] synthase 3
      (pADPRT-3
      )

Gene names

    • Name
      Parp3
    • Synonyms
      Adprt3

Organism names

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

Accessions

  • Primary accession
    Q3ULW8
  • Secondary accessions
    • A0A1L1SRP6
    • E9PX17
    • E9Q992
    • Q3UGL7
    • Q8BHN6

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Chromosome
Note: Almost exclusively localized in the nucleus and appears in numerous small foci and a small number of larger foci whereas a centrosomal location has not been detected. In response to DNA damage, localizes to sites of double-strand break. Also localizes to single-strand breaks. Preferentially localized to the daughter centriole.

Keywords

Phenotypes & Variants

Disruption phenotype

No visible phenotype in normal conditions, but mutant mice are sensitive to ionizing radiation (PubMed:21270334).
In B-cells, class switch recombination is increased, while somatic hypermutation is unaffected, due to increased occupancy of Aicda/Aid at the donor switch region (PubMed:26000965).

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 28 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004461701-533Protein mono-ADP-ribosyltransferase PARP3
Modified residue6N6-(ADP-ribosyl)lysine
Modified residue12ADP-ribosyl glutamic acid
Modified residue24ADP-ribosyl glutamic acid
Modified residue32ADP-ribosyl glutamic acid
Modified residue138ADP-ribosyl aspartic acid
Modified residue160ADP-ribosyl glutamic acid
Modified residue230ADP-ribosyl glutamic acid
Modified residue309ADP-ribosyl glutamic acid
Modified residue310ADP-ribosyl glutamic acid

Post-translational modification

Auto-ADP-ribosylated.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with PARP1; leading to activate PARP1 in absence of DNA. Interacts with PRKDC. Interacts with XRCC5/Ku80; the interaction is dependent on nucleic acids. Interacts with XRCC6/Ku70; the interaction is dependent on nucleic acids. Interacts with EZH2, HDAC1, HDAC2, SUZ12, YY1, LRIG3 and LIG4.

Protein-protein interaction databases

Chemistry

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias, motif, domain.

TypeIDPosition(s)Description
Region1-30Disordered
Compositional bias9-30Basic and acidic residues
Motif14-18Nuclear localization signal
Domain57-147WGR
Domain181-299PARP alpha-helical
Domain313-533PARP catalytic

Sequence similarities

Belongs to the ARTD/PARP family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q3ULW8-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    533
  • Mass (Da)
    59,949
  • Last updated
    2005-10-11 v1
  • Checksum
    DC6EB55D4985766F
MAPKRKASVQTEGSKKRRQGTEEEDSFRSTAEALRAAPADNRVIRVDPSCPFSRNPGIQVHEDYDCTLNQTNIGNNNNKFYIIQLLEEGSRFFCWNRWGRVGEVGQSKMNHFTCLEDAKKDFKKKFWEKTKNKWEERDRFVAQPNKYTLIEVQGEAESQEAVVKALSPQVYSGPVRTVVKPCSLDPATQNLITNIFSKEMFKNAMTLMNLDVKKMPLGKLTKQQIARGFEALEALEEAMKNPTGDGQSLEELSSCFYTVIPHNFGRSRPPPINSPDVLQAKKDMLLVLADIELAQTLQAAPGEEEEKVEEVPHPLDRDYQLLRCQLQLLDSGESEYKAIQTYLKQTGNSYRCPDLRHVWKVNREGEGDRFQAHSKLGNRRLLWHGTNVAVVAAILTSGLRIMPHSGGRVGKGIYFASENSKSAGYVTTMHCGGHQVGYMFLGEVALGKEHHITIDDPSLKSPPSGFDSVIARGQTEPDPAQDIELELDGQPVVVPQGPPVQCPSFKSSSFSQSEYLIYKESQCRLRYLLEIHL

Q3ULW8-2

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A5H1ZRL5A0A5H1ZRL5_MOUSEParp3202
A0A5H1ZRL8A0A5H1ZRL8_MOUSEParp3171
A0A5H1ZRP0A0A5H1ZRP0_MOUSEParp3351

Features

Showing features for compositional bias, sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Compositional bias9-30Basic and acidic residues
Sequence conflict17in Ref. 2; BAC31826 and 4; AAH14870/AAH58754
Alternative sequenceVSP_060032165-169in isoform 2
Sequence conflict171in Ref. 2; BAC31826 and 4; AAH14870/AAH58754
Sequence conflict294in Ref. 4; AAH14870/AAH58754
Sequence conflict354in Ref. 2; BAC31826 and 4; AAH14870/AAH58754
Sequence conflict446in Ref. 2; BAE28191
Sequence conflict464in Ref. 2; BAC31826 and 4; AAH14870/AAH58754

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF368233
EMBL· GenBank· DDBJ
AAN62793.1
EMBL· GenBank· DDBJ
mRNA
AY046316
EMBL· GenBank· DDBJ
AAL08055.1
EMBL· GenBank· DDBJ
mRNA
AY046317
EMBL· GenBank· DDBJ
AAL08056.1
EMBL· GenBank· DDBJ
mRNA
AK044223
EMBL· GenBank· DDBJ
BAC31826.1
EMBL· GenBank· DDBJ
mRNA
AK147868
EMBL· GenBank· DDBJ
BAE28191.1
EMBL· GenBank· DDBJ
mRNA
AK170541
EMBL· GenBank· DDBJ
BAE41867.1
EMBL· GenBank· DDBJ
mRNA
AK145259
EMBL· GenBank· DDBJ
BAE26330.1
EMBL· GenBank· DDBJ
mRNA
AC151729
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC014870
EMBL· GenBank· DDBJ
AAH14870.1
EMBL· GenBank· DDBJ
mRNA
BC058754
EMBL· GenBank· DDBJ
AAH58754.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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