PARP3
entrez
10039
canonical
uniprot
Q9Y6F1
canonical
ensembl
ENSG00000041880
resolver
ensp
ENSP00000381740
resolver
ensp
ENSP00000395951
resolver
ensp
ENSP00000401511
resolver
ensp
ENSP00000417396
resolver
ensp
ENSP00000580710
resolver
genesymbol
PARP3
resolver
genesymbol_syn
ADPRT3
resolver
genesymbol_syn
ADPRTL3
resolver
hgnc
HGNC:273
resolver
uniprot
Q8NER9
resolver
uniprot
Q96CG2
resolver
uniprot
Q9UG81
resolver
uniprot_entry
PARP3_HUMAN
resolver
uniprot_sec
Q8NER9
resolver
uniprot_sec
Q96CG2
resolver
uniprot_sec
Q9UG81
resolver
activity_regulation
ACTIVITY REGULATION: Mono-ADP-ribosyltransferase activity of PARP3 is selectively inhibited by ME0328 compound; ME0328 does not inhibit other ARTD/PARP enzymes, such as PARP1 (PubMed:23742272). Mono-ADP-ribosyltransferase is strongly inhibited by KU0058948 compound (PubMed:19354255). {ECO:0000269|PubMed:19354255, ECO:0000269|PubMed:23742272}.
uniprot
proteins
amino_acid_sequence
MAPKPKPWVQTEGPEKKKGRQAGREEDPFRSTAEALKAIPAEKRIIRVDPTCPLSSNPGTQVYEDYNCTLNQTNIENNNNKFYIIQLLQDSNRFFTCWNRWGRVGEVGQSKINHFTRLEDAKKDFEKKFREKTKNNWAERDHFVSHPGKYTLIEVQAEDEAQEAVVKVDRGPVRTVTKRVQPCSLDPATQKLITNIFSKEMFKNTMALMDLDVKKMPLGKLSKQQIARGFEALEALEEALKGPTDGGQSLEELSSHFYTVIPHNFGHSQPPPINSPELLQAKKDMLLVLADIELAQALQAVSEQEKTVEEVPHPLDRDYQLLKCQLQLLDSGAPEYKVIQTYLEQTGSNHRCPTLQHIWKVNQEGEEDRFQAHSKLGNRKLLWHGTNMAVVAAILTSGLRIMPHSGGRVGKGIYFASENSKSAGYVIGMKCGAHHVGYMFLGEVALGREHHINTDNPSLKSPPPGFDSVIARGHTEPDPTQDTELELDGQQVVVPQGQPVPCPEFSSSTFSQSEYLIYQESQCRLRYLLEVHL
uniprot
proteins
ec_number
2.4.2.-
uniprot
proteins
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:16924674, PubMed:19354255, PubMed:20064938, PubMed:21211721, PubMed:21270334, PubMed:23742272, PubMed:24598253, PubMed:25043379, PubMed:28447610). Mediates mono-ADP-ribosylation of glutamate, aspartate or lysine residues on target proteins (PubMed:20064938, PubMed:25043379). In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (PubMed:25043379). 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 (PubMed:16924674, PubMed:24598253). ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks (PubMed:16924674, PubMed:21211721, PubMed:21270334). Involved in single-strand break repair by catalyzing mono-ADP-ribosylation of histone H2B on 'Glu-2' (H2BE2ADPr) of nucleosomes containing nicked DNA (PubMed:27530147). Cooperates with the XRCC5-XRCC6 (Ku80-Ku70) heterodimer to limit end-resection thereby promoting accurate NHEJ (PubMed:24598253). Suppresses G-quadruplex (G4) structures in response to DNA damage (PubMed:28447610). Associates with a number of DNA repair factors and is involved in the response to exogenous and endogenous DNA strand breaks (PubMed:16924674, PubMed:21211721, 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) (PubMed:21211721). May link the DNA damage surveillance network to the mitotic fidelity checkpoint (PubMed:16924674). Acts as a negative regulator of immunoglobulin class switch recombination, probably by controlling the level of AICDA /AID on the chromatin (By similarity). 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 (PubMed:29361132, PubMed:29520010). {ECO:0000250|UniProtKB:Q3ULW8, ECO:0000269|PubMed:16924674, ECO:0000269|PubMed:19354255, ECO:0000269|PubMed:20064938, ECO:0000269|PubMed:21211721, ECO:0000269|PubMed:21270334, ECO:0000269|PubMed:23742272, ECO:0000269|PubMed:24598253, ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:27530147, ECO:0000269|PubMed:28447610, ECO:0000269|PubMed:29361132, ECO:0000269|PubMed:29520010}.
uniprot
proteins
mass_dalton
60089
uniprot
proteins
mutagenesis
MUTAGEN 83; /note="Y->A: Does not affect activation by nicked DNA, while it prevents activation by a 3'-overhang substrate."; /evidence="ECO:0000269|PubMed:27530147"; MUTAGEN 101; /note="W->L: Reduced activity on nicked DNA."; /evidence="ECO:0000269|PubMed:27530147"; MUTAGEN 103; /note="R->N: Abolished activation by nicked DNA."; /evidence="ECO:0000269|PubMed:27530147
uniprot
proteins
post_translational_modification
PTM: Auto-mono-ADP-ribosylated. {ECO:0000269|PubMed:20064938, ECO:0000269|PubMed:25043379}.
uniprot
proteins
protein_family
ARTD/PARP family
uniprot
proteins
pubmed
10329013
uniprot
proteins
pubmed
12640039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16924674
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19354255
uniprot
proteins
pubmed
20064938
uniprot
proteins
pubmed
20106667
uniprot
proteins
pubmed
21211721
uniprot
proteins
pubmed
21270334
uniprot
proteins
pubmed
23742272
uniprot
proteins
pubmed
24188023
uniprot
proteins
pubmed
24598253
uniprot
proteins
pubmed
25043379
uniprot
proteins
pubmed
27530147
uniprot
proteins
pubmed
28447610
uniprot
proteins
pubmed
29361132
uniprot
proteins
pubmed
29520010
uniprot
proteins
sequence_length
533
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16924674}. Chromosome {ECO:0000269|PubMed:21270334, ECO:0000269|PubMed:27530147, ECO:0000269|PubMed:28447610}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10329013}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:10329013}. 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 (PubMed:16924674). In response to DNA damage, localizes to sites of double-strand break (PubMed:21270334, PubMed:28447610). Also localizes to single-strand breaks (PubMed:27530147). Preferentially localized to the daughter centriole (PubMed:10329013). {ECO:0000269|PubMed:10329013, ECO:0000269|PubMed:16924674, ECO:0000269|PubMed:21270334, ECO:0000269|PubMed:27530147, ECO:0000269|PubMed:28447610}.
uniprot
proteins