PARP3_HUMAN
ID PARP3_HUMAN Reviewed; 533 AA.
AC Q9Y6F1; Q8NER9; Q96CG2; Q9UG81;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, sequence version 4.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP3 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000269|PubMed:16924674, ECO:0000269|PubMed:25043379};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 3 {ECO:0000303|PubMed:20106667};
DE Short=ARTD3 {ECO:0000303|PubMed:20106667};
DE AltName: Full=DNA ADP-ribosyltransferase PARP3 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000269|PubMed:29361132};
DE AltName: Full=IRT1;
DE AltName: Full=NAD(+) ADP-ribosyltransferase 3 {ECO:0000303|PubMed:20106667};
DE Short=ADPRT-3 {ECO:0000303|PubMed:20106667};
DE AltName: Full=Poly [ADP-ribose] polymerase 3 {ECO:0000303|PubMed:12640039, ECO:0000303|PubMed:20106667};
DE Short=PARP-3 {ECO:0000303|PubMed:12640039};
DE Short=hPARP-3 {ECO:0000303|PubMed:12640039};
DE AltName: Full=Poly[ADP-ribose] synthase 3 {ECO:0000303|PubMed:20106667};
DE Short=pADPRT-3 {ECO:0000303|PubMed:20106667};
GN Name=PARP3 {ECO:0000303|PubMed:10329013, ECO:0000312|HGNC:HGNC:273};
GN Synonyms=ADPRT3 {ECO:0000303|PubMed:20106667}, ADPRTL3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=10329013; DOI=10.1006/geno.1999.5799;
RA Johansson M.;
RT "A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of
RT two novel poly(ADP-ribose) polymerase homologues.";
RL Genomics 57:442-445(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
RC TISSUE=Frontal cortex;
RX PubMed=12640039; DOI=10.1242/jcs.00341;
RA Augustin A., Spenlehauer C., Dumond H., Menissier-de Murcia J., Piel M.,
RA Schmit A.-C., Apiou F., Vonesch J.-L., Kock M., Bornens M., de Murcia G.M.;
RT "PARP-3 localizes preferentially to the daughter centriole and interferes
RT with the G1/S cell cycle progression.";
RL J. Cell Sci. 116:1551-1562(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Koch-Nolte F.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-533 (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRKDC; PARP1; EZH2;
RP XRCC5; XRCC6; HDAC1; HDAC2; SUZ12; YY1; LRIG3 AND LIG4.
RX PubMed=16924674; DOI=10.1002/jcb.21051;
RA Rouleau M., McDonald D., Gagne P., Ouellet M.E., Droit A., Hunter J.M.,
RA Dutertre S., Prigent C., Hendzel M.J., Poirier G.G.;
RT "PARP-3 associates with polycomb group bodies and with components of the
RT DNA damage repair machinery.";
RL J. Cell. Biochem. 100:385-401(2007).
RN [8]
RP NOMENCLATURE.
RX PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
RA Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
RT "Toward a unified nomenclature for mammalian ADP-ribosyltransferases.";
RL Trends Biochem. Sci. 35:208-219(2010).
RN [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH PARP1, AND
RP AUTO-ADP-RIBOSYLATION.
RX PubMed=20064938; DOI=10.1074/jbc.m109.077834;
RA Loseva O., Jemth A.S., Bryant H.E., Schueler H., Lehtioe L., Karlberg T.,
RA Helleday T.;
RT "PARP-3 is a mono-ADP-ribosylase that activates PARP-1 in the absence of
RT DNA.";
RL J. Biol. Chem. 285:8054-8060(2010).
RN [10]
RP FUNCTION.
RX PubMed=21211721; DOI=10.1016/j.molcel.2010.12.006;
RA Rulten S.L., Fisher A.E., Robert I., Zuma M.C., Rouleau M., Ju L.,
RA Poirier G., Reina-San-Martin B., Caldecott K.W.;
RT "PARP-3 and APLF function together to accelerate nonhomologous end-
RT joining.";
RL Mol. Cell 41:33-45(2011).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21270334; DOI=10.1073/pnas.1016574108;
RA Boehler C., Gauthier L.R., Mortusewicz O., Biard D.S., Saliou J.M.,
RA Bresson A., Sanglier-Cianferani S., Smith S., Schreiber V., Boussin F.,
RA Dantzer F.;
RT "Poly(ADP-ribose) polymerase 3 (PARP3), a newcomer in cellular response to
RT DNA damage and mitotic progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2783-2788(2011).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND ADP-RIBOSYLATION AT LYS-6; GLU-12;
RP GLU-15; GLU-26; GLU-34; LYS-37; ASP-141; GLU-163; ASP-210; GLU-231;
RP GLU-309; GLU-310; GLU-344 AND GLU-449.
RX PubMed=25043379; DOI=10.1038/ncomms5426;
RA Vyas S., Matic I., Uchima L., Rood J., Zaja R., Hay R.T., Ahel I.,
RA Chang P.;
RT "Family-wide analysis of poly(ADP-ribose) polymerase activity.";
RL Nat. Commun. 5:4426-4426(2014).
RN [13]
RP FUNCTION, AND INTERACTION WITH XRCC5 AND XRCC6.
RX PubMed=24598253; DOI=10.1093/nar/gku174;
RA Beck C., Boehler C., Guirouilh Barbat J., Bonnet M.E., Illuzzi G.,
RA Ronde P., Gauthier L.R., Magroun N., Rajendran A., Lopez B.S., Scully R.,
RA Boussin F.D., Schreiber V., Dantzer F.;
RT "PARP3 affects the relative contribution of homologous recombination and
RT nonhomologous end-joining pathways.";
RL Nucleic Acids Res. 42:5616-5632(2014).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29361132; DOI=10.1093/nar/gkx1318;
RA Zarkovic G., Belousova E.A., Talhaoui I., Saint-Pierre C., Kutuzov M.M.,
RA Matkarimov B.T., Biard D., Gasparutto D., Lavrik O.I., Ishchenko A.A.;
RT "Characterization of DNA ADP-ribosyltransferase activities of PARP2 and
RT PARP3: new insights into DNA ADP-ribosylation.";
RL Nucleic Acids Res. 46:2417-2431(2018).
RN [15]
RP FUNCTION.
RX PubMed=29520010; DOI=10.1038/s41598-018-22673-3;
RA Belousova E.A., Ishchenko A.A., Lavrik O.I.;
RT "Dna is a new target of Parp3.";
RL Sci. Rep. 8:4176-4176(2018).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 178-532 IN COMPLEX WITH THE
RP INHIBITOR 3-AMINOBENZOIC ACID.
RG Structural genomics consortium (SGC);
RT "Human poly(ADP-ribose) polymerase 3, catalytic fragment in complex with an
RT inhibitor 3-aminobenzoic acid.";
RL Submitted (APR-2007) to the PDB data bank.
RN [17]
RP STRUCTURE BY NMR OF 41-157.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the WGR domain from human poly [ADP-ribose]
RT polymerase-3.";
RL Submitted (APR-2008) to the PDB data bank.
CC -!- FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-
CC ribosylation of target proteins and plays a key role in the response to
CC DNA damage (PubMed:16924674, PubMed:20064938, PubMed:21211721,
CC PubMed:21270334, PubMed:25043379, PubMed:24598253). Mediates mono-ADP-
CC ribosylation of glutamate, aspartate or lysine residues on target
CC proteins (PubMed:20064938, PubMed:25043379). In contrast to PARP1 and
CC PARP2, it is not able to mediate poly-ADP-ribosylation
CC (PubMed:25043379). Associates with a number of DNA repair factors and
CC is involved in the response to exogenous and endogenous DNA strand
CC breaks (PubMed:16924674, PubMed:21211721, PubMed:21270334). Together
CC with APLF, promotes the retention of the LIG4-XRCC4 complex on
CC chromatin and accelerate DNA ligation during non-homologous end-joining
CC (NHEJ) (PubMed:21211721). Cooperates with the XRCC5-XRCC6 (Ku80-Ku70)
CC heterodimer to limit end-resection thereby promoting accurate NHEJ
CC (PubMed:24598253). Involved in DNA repair by mediating mono-ADP-
CC ribosylation of a limited number of acceptor proteins involved in
CC chromatin architecture and in DNA metabolism, such as XRCC5 and XRCC6
CC (PubMed:16924674, PubMed:24598253). ADP-ribosylation follows DNA damage
CC and appears as an obligatory step in a detection/signaling pathway
CC leading to the reparation of DNA strand breaks (PubMed:16924674,
CC PubMed:21211721, PubMed:21270334). May link the DNA damage surveillance
CC network to the mitotic fidelity checkpoint (PubMed:16924674). In
CC addition to proteins, also able to ADP-ribosylate DNA: mediates DNA
CC mono-ADP-ribosylation of DNA strand break termini via covalent addition
CC of a single ADP-ribose moiety to a 5'- or 3'-terminal phosphate
CC residues in DNA containing multiple strand breaks (PubMed:29361132,
CC PubMed:29520010). Acts as a negative regulator of immunoglobulin class
CC switch recombination, probably by controlling the level of AICDA /AID
CC on the chromatin (By similarity). {ECO:0000250|UniProtKB:Q3ULW8,
CC ECO:0000269|PubMed:16924674, ECO:0000269|PubMed:20064938,
CC ECO:0000269|PubMed:21211721, ECO:0000269|PubMed:21270334,
CC ECO:0000269|PubMed:24598253, ECO:0000269|PubMed:25043379,
CC ECO:0000269|PubMed:29361132, ECO:0000269|PubMed:29520010}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC Evidence={ECO:0000269|PubMed:25043379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425;
CC Evidence={ECO:0000269|PubMed:25043379};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
CC glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
CC Evidence={ECO:0000269|PubMed:25043379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225;
CC Evidence={ECO:0000269|PubMed:25043379};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + NAD(+) = H(+) + N(6)-(ADP-D-ribosyl)-L-
CC lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58220, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:15088, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142515; Evidence={ECO:0000269|PubMed:25043379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58221;
CC Evidence={ECO:0000269|PubMed:25043379};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=130 uM for NAD(+) {ECO:0000269|PubMed:20064938};
CC -!- SUBUNIT: Interacts with PARP1; leading to activate PARP1 in absence of
CC DNA (PubMed:16924674, PubMed:20064938). Interacts with PRKDC
CC (PubMed:16924674). Interacts with XRCC5/Ku80; the interaction is
CC dependent on nucleic acids (PubMed:16924674, PubMed:24598253).
CC Interacts with XRCC6/Ku70; the interaction is dependent on nucleic
CC acids (PubMed:16924674, PubMed:24598253). Interacts with EZH2, HDAC1,
CC HDAC2, SUZ12, YY1, LRIG3 and LIG4 (PubMed:16924674).
CC {ECO:0000269|PubMed:16924674, ECO:0000269|PubMed:20064938,
CC ECO:0000269|PubMed:24598253}.
CC -!- INTERACTION:
CC Q9Y6F1-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-14609301, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16924674}. Chromosome
CC {ECO:0000269|PubMed:21270334}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:10329013}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:10329013}. Note=Almost exclusively localized in the
CC nucleus and appears in numerous small foci and a small number of larger
CC foci whereas a centrosomal location has not been detected
CC (PubMed:16924674). In response to DNA damage, localizes to sites of
CC double-strand break (PubMed:21270334). Preferentially localized to the
CC daughter centriole (PubMed:10329013). {ECO:0000269|PubMed:10329013,
CC ECO:0000269|PubMed:16924674, ECO:0000269|PubMed:21270334}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Short;
CC IsoId=Q9Y6F1-1; Sequence=Displayed;
CC Name=2; Synonyms=Long;
CC IsoId=Q9Y6F1-2; Sequence=VSP_007863;
CC -!- TISSUE SPECIFICITY: Widely expressed; the highest levels are in the
CC kidney, skeletal muscle, liver, heart and spleen; also detected in
CC pancreas, lung, placenta, brain, leukocytes, colon, small intestine,
CC ovary, testis, prostate and thymus. {ECO:0000269|PubMed:10329013}.
CC -!- PTM: Auto-mono-ADP-ribosylated. {ECO:0000269|PubMed:20064938,
CC ECO:0000269|PubMed:25043379}.
CC -!- MISCELLANEOUS: [Isoform 1]: More abundant isoform.
CC {ECO:0000269|PubMed:16924674}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; AF083068; AAD29855.1; -; mRNA.
DR EMBL; AY126341; AAM95460.1; -; mRNA.
DR EMBL; Y16836; CAC79988.1; -; mRNA.
DR EMBL; AC115284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014260; AAH14260.1; -; mRNA.
DR EMBL; AL050034; CAB43246.1; -; mRNA.
DR CCDS; CCDS43097.1; -. [Q9Y6F1-1]
DR CCDS; CCDS46839.1; -. [Q9Y6F1-1]
DR PIR; T08713; T08713.
DR RefSeq; NP_001003931.3; NM_001003931.3. [Q9Y6F1-1]
DR RefSeq; NP_005476.4; NM_005485.5. [Q9Y6F1-1]
DR RefSeq; XP_005264836.2; XM_005264779.4.
DR RefSeq; XP_016860979.1; XM_017005490.1. [Q9Y6F1-1]
DR PDB; 2EOC; NMR; -; A=41-157.
DR PDB; 3C49; X-ray; 2.80 A; A=178-532.
DR PDB; 3C4H; X-ray; 2.10 A; A=178-532.
DR PDB; 3CE0; X-ray; 2.80 A; A=178-532.
DR PDB; 3FHB; X-ray; 2.30 A; A=178-532.
DR PDB; 4GV0; X-ray; 1.90 A; A=178-532.
DR PDB; 4GV2; X-ray; 1.80 A; A=178-532.
DR PDB; 4GV4; X-ray; 1.80 A; A=178-532.
DR PDB; 4L6Z; X-ray; 2.00 A; A=178-532.
DR PDB; 4L70; X-ray; 2.00 A; A=178-532.
DR PDB; 4L7L; X-ray; 2.10 A; A=178-532.
DR PDB; 4L7N; X-ray; 1.80 A; A=178-532.
DR PDB; 4L7O; X-ray; 2.00 A; A=178-532.
DR PDB; 4L7P; X-ray; 2.30 A; A=178-532.
DR PDB; 4L7R; X-ray; 2.20 A; A=178-532.
DR PDB; 4L7U; X-ray; 2.80 A; A=178-532.
DR PDBsum; 2EOC; -.
DR PDBsum; 3C49; -.
DR PDBsum; 3C4H; -.
DR PDBsum; 3CE0; -.
DR PDBsum; 3FHB; -.
DR PDBsum; 4GV0; -.
DR PDBsum; 4GV2; -.
DR PDBsum; 4GV4; -.
DR PDBsum; 4L6Z; -.
DR PDBsum; 4L70; -.
DR PDBsum; 4L7L; -.
DR PDBsum; 4L7N; -.
DR PDBsum; 4L7O; -.
DR PDBsum; 4L7P; -.
DR PDBsum; 4L7R; -.
DR PDBsum; 4L7U; -.
DR AlphaFoldDB; Q9Y6F1; -.
DR SMR; Q9Y6F1; -.
DR BioGRID; 115351; 24.
DR IntAct; Q9Y6F1; 2.
DR STRING; 9606.ENSP00000381740; -.
DR BindingDB; Q9Y6F1; -.
DR ChEMBL; CHEMBL5083; -.
DR DrugBank; DB07677; 2-methyl-3,5,7,8-tetrahydro-4H-thiopyrano[4,3-d]pyrimidin-4-one.
DR DrugBank; DB08058; 4-[3-(1,4-diazepan-1-ylcarbonyl)-4-fluorobenzyl]phthalazin-1(2H)-one.
DR DrugBank; DB08348; N~2~,N~2~-DIMETHYL-N~1~-(6-OXO-5,6-DIHYDROPHENANTHRIDIN-2-YL)GLYCINAMIDE.
DR DrugBank; DB09074; Olaparib.
DR DrugBank; DB12332; Rucaparib.
DR DrugCentral; Q9Y6F1; -.
DR GuidetoPHARMACOLOGY; 2864; -.
DR iPTMnet; Q9Y6F1; -.
DR PhosphoSitePlus; Q9Y6F1; -.
DR BioMuta; PARP3; -.
DR DMDM; 224471880; -.
DR EPD; Q9Y6F1; -.
DR jPOST; Q9Y6F1; -.
DR MassIVE; Q9Y6F1; -.
DR MaxQB; Q9Y6F1; -.
DR PaxDb; Q9Y6F1; -.
DR PeptideAtlas; Q9Y6F1; -.
DR PRIDE; Q9Y6F1; -.
DR ProteomicsDB; 86661; -. [Q9Y6F1-1]
DR ProteomicsDB; 86662; -. [Q9Y6F1-2]
DR Antibodypedia; 7395; 316 antibodies from 37 providers.
DR DNASU; 10039; -.
DR Ensembl; ENST00000398755.8; ENSP00000381740.4; ENSG00000041880.15. [Q9Y6F1-1]
DR Ensembl; ENST00000417220.6; ENSP00000395951.2; ENSG00000041880.15. [Q9Y6F1-1]
DR Ensembl; ENST00000431474.6; ENSP00000401511.1; ENSG00000041880.15. [Q9Y6F1-1]
DR Ensembl; ENST00000471971.6; ENSP00000417396.2; ENSG00000041880.15. [Q9Y6F1-1]
DR Ensembl; ENST00000498510.2; ENSP00000417625.2; ENSG00000041880.15. [Q9Y6F1-1]
DR GeneID; 10039; -.
DR KEGG; hsa:10039; -.
DR MANE-Select; ENST00000398755.8; ENSP00000381740.4; NM_001003931.4; NP_001003931.4.
DR UCSC; uc003dbz.4; human. [Q9Y6F1-1]
DR CTD; 10039; -.
DR DisGeNET; 10039; -.
DR GeneCards; PARP3; -.
DR HGNC; HGNC:273; PARP3.
DR HPA; ENSG00000041880; Low tissue specificity.
DR MIM; 607726; gene.
DR neXtProt; NX_Q9Y6F1; -.
DR OpenTargets; ENSG00000041880; -.
DR PharmGKB; PA24593; -.
DR VEuPathDB; HostDB:ENSG00000041880; -.
DR eggNOG; KOG1037; Eukaryota.
DR GeneTree; ENSGT00940000158855; -.
DR InParanoid; Q9Y6F1; -.
DR OMA; AKRVQPC; -.
DR OrthoDB; 909382at2759; -.
DR PhylomeDB; Q9Y6F1; -.
DR TreeFam; TF315407; -.
DR BRENDA; 2.4.2.30; 2681.
DR PathwayCommons; Q9Y6F1; -.
DR SignaLink; Q9Y6F1; -.
DR SIGNOR; Q9Y6F1; -.
DR BioGRID-ORCS; 10039; 13 hits in 1081 CRISPR screens.
DR ChiTaRS; PARP3; human.
DR EvolutionaryTrace; Q9Y6F1; -.
DR GeneWiki; PARP3; -.
DR GenomeRNAi; 10039; -.
DR Pharos; Q9Y6F1; Tclin.
DR PRO; PR:Q9Y6F1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y6F1; protein.
DR Bgee; ENSG00000041880; Expressed in right adrenal gland cortex and 133 other tissues.
DR ExpressionAtlas; Q9Y6F1; baseline and differential.
DR Genevisible; Q9Y6F1; HS.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0035861; C:site of double-strand break; IDA:MGI.
DR GO; GO:0003824; F:catalytic activity; TAS:ProtInc.
DR GO; GO:0140294; F:NAD DNA ADP-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:MGI.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030592; P:DNA ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0006302; P:double-strand break repair; IDA:MGI.
DR GO; GO:0045829; P:negative regulation of isotype switching; ISS:UniProtKB.
DR GO; GO:1905662; P:negative regulation of telomerase RNA reverse transcriptase activity; IMP:BHF-UCL.
DR GO; GO:0051106; P:positive regulation of DNA ligation; IGI:MGI.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
DR GO; GO:0006471; P:protein ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:1990166; P:protein localization to site of double-strand break; IMP:MGI.
DR GO; GO:0140289; P:protein mono-ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IBA:GO_Central.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:MGI.
DR GO; GO:0000723; P:telomere maintenance; IMP:MGI.
DR Gene3D; 1.20.142.10; -; 1.
DR InterPro; IPR031275; PARP3.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
DR InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
DR InterPro; IPR036930; WGR_dom_sf.
DR InterPro; IPR008893; WGR_domain.
DR PANTHER; PTHR10459:SF66; PTHR10459:SF66; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF142921; SSF142921; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51977; WGR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Alternative splicing; Chromosome;
KW Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Glycosyltransferase; NAD;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..533
FT /note="Protein mono-ADP-ribosyltransferase PARP3"
FT /id="PRO_0000211329"
FT DOMAIN 59..150
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 182..300
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 313..533
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 14..20
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 10..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="N6-(ADP-ribosyl)lysine"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 12
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 15
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 26
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 34
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 37
FT /note="N6-(ADP-ribosyl)lysine"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 141
FT /note="ADP-ribosyl aspartic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 163
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 210
FT /note="ADP-ribosyl aspartic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 231
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 309
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 310
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 344
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 449
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT VAR_SEQ 1
FT /note="M -> MSLLFLAM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12640039, ECO:0000303|Ref.3"
FT /id="VSP_007863"
FT VARIANT 91
FT /note="S -> N (in dbSNP:rs34224216)"
FT /id="VAR_056643"
FT VARIANT 100
FT /note="R -> H (in dbSNP:rs28547534)"
FT /id="VAR_054622"
FT VARIANT 269
FT /note="Q -> R (in dbSNP:rs323870)"
FT /id="VAR_056644"
FT CONFLICT 80
FT /note="N -> K (in Ref. 1; AAD29855)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="G -> A (in Ref. 1; AAD29855)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="K -> E (in Ref. 6; CAB43246)"
FT /evidence="ECO:0000305"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2EOC"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:2EOC"
FT STRAND 61..74
FT /evidence="ECO:0007829|PDB:2EOC"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:2EOC"
FT STRAND 79..89
FT /evidence="ECO:0007829|PDB:2EOC"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:2EOC"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:2EOC"
FT HELIX 118..133
FT /evidence="ECO:0007829|PDB:2EOC"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2EOC"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:2EOC"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2EOC"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:4GV2"
FT HELIX 199..208
FT /evidence="ECO:0007829|PDB:4GV2"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:4GV2"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:4GV2"
FT HELIX 223..240
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:3C49"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:3C49"
FT HELIX 276..298
FT /evidence="ECO:0007829|PDB:4GV2"
FT HELIX 303..307
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:4GV2"
FT HELIX 314..321
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:4GV2"
FT HELIX 336..346
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 354..362
FT /evidence="ECO:0007829|PDB:4GV2"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:3C49"
FT HELIX 367..371
FT /evidence="ECO:0007829|PDB:4GV2"
FT TURN 372..375
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:4GV2"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:4GV2"
FT HELIX 391..397
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 411..418
FT /evidence="ECO:0007829|PDB:4GV2"
FT HELIX 419..423
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 434..445
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 448..454
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 473..477
FT /evidence="ECO:0007829|PDB:4GV2"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 483..487
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 490..494
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:4GV2"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 514..519
FT /evidence="ECO:0007829|PDB:4GV2"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:4GV2"
FT STRAND 523..532
FT /evidence="ECO:0007829|PDB:4GV2"
SQ SEQUENCE 533 AA; 60089 MW; 6296A0E439CC7767 CRC64;
MAPKPKPWVQ TEGPEKKKGR QAGREEDPFR STAEALKAIP AEKRIIRVDP TCPLSSNPGT
QVYEDYNCTL NQTNIENNNN KFYIIQLLQD SNRFFTCWNR WGRVGEVGQS KINHFTRLED
AKKDFEKKFR EKTKNNWAER DHFVSHPGKY TLIEVQAEDE AQEAVVKVDR GPVRTVTKRV
QPCSLDPATQ KLITNIFSKE MFKNTMALMD LDVKKMPLGK LSKQQIARGF EALEALEEAL
KGPTDGGQSL EELSSHFYTV IPHNFGHSQP PPINSPELLQ AKKDMLLVLA DIELAQALQA
VSEQEKTVEE VPHPLDRDYQ LLKCQLQLLD SGAPEYKVIQ TYLEQTGSNH RCPTLQHIWK
VNQEGEEDRF QAHSKLGNRK LLWHGTNMAV VAAILTSGLR IMPHSGGRVG KGIYFASENS
KSAGYVIGMK CGAHHVGYMF LGEVALGREH HINTDNPSLK SPPPGFDSVI ARGHTEPDPT
QDTELELDGQ QVVVPQGQPV PCPEFSSSTF SQSEYLIYQE SQCRLRYLLE VHL
