Q3ULW8 · PARP3_MOUSE
- ProteinProtein mono-ADP-ribosyltransferase PARP3
- GeneParp3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids533 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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).
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
- L-aspartyl-[protein] + NAD+ = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamide
- L-glutamyl-[protein] + NAD+ = 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + nicotinamide
- L-lysyl-[protein] + NAD+ = H+ + N6-(ADP-D-ribosyl)-L-lysyl-[protein] + nicotinamide
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein mono-ADP-ribosyltransferase PARP3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ3ULW8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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
- Cellular component
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).
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.
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000446170 | 1-533 | Protein mono-ADP-ribosyltransferase PARP3 | |||
Sequence: MAPKRKASVQTEGSKKRRQGTEEEDSFRSTAEALRAAPADNRVIRVDPSCPFSRNPGIQVHEDYDCTLNQTNIGNNNNKFYIIQLLEEGSRFFCWNRWGRVGEVGQSKMNHFTCLEDAKKDFKKKFWEKTKNKWEERDRFVAQPNKYTLIEVQGEAESQEAVVKALSPQVYSGPVRTVVKPCSLDPATQNLITNIFSKEMFKNAMTLMNLDVKKMPLGKLTKQQIARGFEALEALEEAMKNPTGDGQSLEELSSCFYTVIPHNFGRSRPPPINSPDVLQAKKDMLLVLADIELAQTLQAAPGEEEEKVEEVPHPLDRDYQLLRCQLQLLDSGESEYKAIQTYLKQTGNSYRCPDLRHVWKVNREGEGDRFQAHSKLGNRRLLWHGTNVAVVAAILTSGLRIMPHSGGRVGKGIYFASENSKSAGYVTTMHCGGHQVGYMFLGEVALGKEHHITIDDPSLKSPPSGFDSVIARGQTEPDPAQDIELELDGQPVVVPQGPPVQCPSFKSSSFSQSEYLIYKESQCRLRYLLEIHL | ||||||
Modified residue | 6 | N6-(ADP-ribosyl)lysine | ||||
Sequence: K | ||||||
Modified residue | 12 | ADP-ribosyl glutamic acid | ||||
Sequence: E | ||||||
Modified residue | 24 | ADP-ribosyl glutamic acid | ||||
Sequence: E | ||||||
Modified residue | 32 | ADP-ribosyl glutamic acid | ||||
Sequence: E | ||||||
Modified residue | 138 | ADP-ribosyl aspartic acid | ||||
Sequence: D | ||||||
Modified residue | 160 | ADP-ribosyl glutamic acid | ||||
Sequence: E | ||||||
Modified residue | 230 | ADP-ribosyl glutamic acid | ||||
Sequence: E | ||||||
Modified residue | 309 | ADP-ribosyl glutamic acid | ||||
Sequence: E | ||||||
Modified residue | 310 | ADP-ribosyl glutamic acid | ||||
Sequence: E |
Post-translational modification
Auto-ADP-ribosylated.
Keywords
- PTM
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-30 | Disordered | ||||
Sequence: MAPKRKASVQTEGSKKRRQGTEEEDSFRST | ||||||
Compositional bias | 9-30 | Basic and acidic residues | ||||
Sequence: VQTEGSKKRRQGTEEEDSFRST | ||||||
Motif | 14-18 | Nuclear localization signal | ||||
Sequence: SKKRR | ||||||
Domain | 57-147 | WGR | ||||
Sequence: GIQVHEDYDCTLNQTNIGNNNNKFYIIQLLEEGSRFFCWNRWGRVGEVGQSKMNHFTCLEDAKKDFKKKFWEKTKNKWEERDRFVAQPNKY | ||||||
Domain | 181-299 | PARP alpha-helical | ||||
Sequence: PCSLDPATQNLITNIFSKEMFKNAMTLMNLDVKKMPLGKLTKQQIARGFEALEALEEAMKNPTGDGQSLEELSSCFYTVIPHNFGRSRPPPINSPDVLQAKKDMLLVLADIELAQTLQA | ||||||
Domain | 313-533 | PARP catalytic | ||||
Sequence: HPLDRDYQLLRCQLQLLDSGESEYKAIQTYLKQTGNSYRCPDLRHVWKVNREGEGDRFQAHSKLGNRRLLWHGTNVAVVAAILTSGLRIMPHSGGRVGKGIYFASENSKSAGYVTTMHCGGHQVGYMFLGEVALGKEHHITIDDPSLKSPPSGFDSVIARGQTEPDPAQDIELELDGQPVVVPQGPPVQCPSFKSSSFSQSEYLIYKESQCRLRYLLEIHL |
Sequence similarities
Belongs to the ARTD/PARP family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- Name1
- Length533
- Mass (Da)59,949
- Last updated2005-10-11 v1
- ChecksumDC6EB55D4985766F
Q3ULW8-2
- Name2
- Differences from canonical
- 165-169: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A5H1ZRL5 | A0A5H1ZRL5_MOUSE | Parp3 | 202 | ||
A0A5H1ZRL8 | A0A5H1ZRL8_MOUSE | Parp3 | 171 | ||
A0A5H1ZRP0 | A0A5H1ZRP0_MOUSE | Parp3 | 351 |
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 9-30 | Basic and acidic residues | ||||
Sequence: VQTEGSKKRRQGTEEEDSFRST | ||||||
Sequence conflict | 17 | in Ref. 2; BAC31826 and 4; AAH14870/AAH58754 | ||||
Sequence: R → Q | ||||||
Alternative sequence | VSP_060032 | 165-169 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 171 | in Ref. 2; BAC31826 and 4; AAH14870/AAH58754 | ||||
Sequence: Y → D | ||||||
Sequence conflict | 294 | in Ref. 4; AAH14870/AAH58754 | ||||
Sequence: A → V | ||||||
Sequence conflict | 354 | in Ref. 2; BAC31826 and 4; AAH14870/AAH58754 | ||||
Sequence: D → N | ||||||
Sequence conflict | 446 | in Ref. 2; BAE28191 | ||||
Sequence: L → I | ||||||
Sequence conflict | 464 | in Ref. 2; BAC31826 and 4; AAH14870/AAH58754 | ||||
Sequence: S → P |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |