PARP1_RAT
ID PARP1_RAT Reviewed; 1014 AA.
AC P27008; O35937;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Poly [ADP-ribose] polymerase 1;
DE Short=PARP-1;
DE EC=2.4.2.30 {ECO:0000250|UniProtKB:P09874};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 1;
DE Short=ARTD1;
DE AltName: Full=DNA ADP-ribosyltransferase PARP1 {ECO:0000250|UniProtKB:P09874};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
DE AltName: Full=NAD(+) ADP-ribosyltransferase 1;
DE Short=ADPRT 1;
DE AltName: Full=Poly[ADP-ribose] synthase 1;
DE AltName: Full=Protein poly-ADP-ribosyltransferase PARP1 {ECO:0000250|UniProtKB:P09874};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
GN Name=Parp1; Synonyms=Adprt;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Monocyte;
RX PubMed=9385436; DOI=10.1080/15216549700204571;
RA Beneke S., Meyer R., Buerkle A.;
RT "Isolation of cDNA encoding full-length rat (Rattus norvegicus) poly (ADP-
RT ribose) polymerase.";
RL Biochem. Mol. Biol. Int. 43:755-761(1997).
RN [2]
RP SEQUENCE REVISION TO 812.
RA Beneke S., Meyer R., Buerkle A.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
RC STRAIN=Sprague-Dawley; TISSUE=Prostate;
RX PubMed=1601134; DOI=10.1016/0014-5793(92)80457-r;
RA Potvin F., Thibodeau J., Kirkland J.B., Dandenault B., Duchaine C.,
RA Poirier G.G.;
RT "Structural analysis of the putative regulatory region of the rat gene
RT encoding poly(ADP-ribose) polymerase.";
RL FEBS Lett. 302:269-273(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 515-1014.
RC STRAIN=Sprague-Dawley; TISSUE=Prostate;
RX PubMed=2508731; DOI=10.1139/o89-097;
RA Thibodeau J., Gradwohl G., Dumas C., Clairoux-Moreau S., Brunet G.;
RT "Cloning of rodent cDNA coding the poly(ADP-ribose) polymerase catalytic
RT domain and analysis of mRNA levels during the cell cycle.";
RL Biochem. Cell Biol. 67:653-660(1989).
RN [6]
RP INTERACTION WITH NR4A3.
RX PubMed=25625556; DOI=10.1111/bph.13091;
RA Feng X.J., Gao H., Gao S., Li Z., Li H., Lu J., Wang J.J., Huang X.Y.,
RA Liu M., Zou J., Ye J.T., Liu P.Q.;
RT "The orphan receptor NOR1 participates in isoprenaline-induced cardiac
RT hypertrophy by regulating PARP-1.";
RL Br. J. Pharmacol. 172:2852-2863(2015).
CC -!- FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP-
CC ribosylation of proteins and plays a key role in DNA repair. Mediates
CC glutamate, aspartate, serine or tyrosine ADP-ribosylation of proteins:
CC the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor
CC carboxyl group of target residues and further ADP-ribosyl groups are
CC transferred to the 2'-position of the terminal adenosine moiety,
CC building up a polymer with an average chain length of 20-30 units.
CC Serine ADP-ribosylation of proteins constitutes the primary form of
CC ADP-ribosylation of proteins in response to DNA damage. Mainly mediates
CC glutamate and aspartate ADP-ribosylation of target proteins in absence
CC of HPF1. Following interaction with HPF1, catalyzes serine ADP-
CC ribosylation of target proteins; HPF1 conferring serine specificity by
CC completing the PARP1 active site. Also catalyzes tyrosine ADP-
CC ribosylation of target proteins following interaction with HPF1. PARP1
CC initiates the repair of DNA breaks: recognizes and binds DNA breaks
CC within chromatin and recruits HPF1, licensing serine ADP-ribosylation
CC of target proteins, such as histones, thereby promoting decompaction of
CC chromatin and the recruitment of repair factors leading to the
CC reparation of DNA strand breaks. In addition to base excision repair
CC (BER) pathway, also involved in double-strand breaks (DSBs) repair:
CC together with TIMELESS, accumulates at DNA damage sites and promotes
CC homologous recombination repair by mediating poly-ADP-ribosylation.
CC Mediates the poly(ADP-ribosyl)ation of a number of proteins, including
CC itself, APLF and CHFR. In addition to proteins, also able to ADP-
CC ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini
CC containing terminal phosphates and a 2'-OH group in single- and double-
CC stranded DNA, respectively. Required for PARP9 and DTX3L recruitment to
CC DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination
CC promotes the rapid and specific recruitment of 53BP1/TP53BP1,
CC UIMC1/RAP80, and BRCA1 to DNA damage sites. Acts as a regulator of
CC transcription: positively regulates the transcription of MTUS1 and
CC negatively regulates the transcription of MTUS2/TIP150. Plays a role in
CC the positive regulation of IFNG transcription in T-helper 1 cells as
CC part of an IFNG promoter-binding complex with TXK and EEF1A1. Involved
CC in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and
CC NUDT5. Nuclear ATP generation is required for extensive chromatin
CC remodeling events that are energy-consuming.
CC {ECO:0000250|UniProtKB:P09874}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-
CC ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-
CC ribosyl)-L-seryl-[protein]; Xref=Rhea:RHEA:58232, Rhea:RHEA-
CC COMP:9863, Rhea:RHEA-COMP:15091, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29999, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142556; Evidence={ECO:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58233;
CC Evidence={ECO:0000250|UniProtKB:P09874};
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:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425;
CC Evidence={ECO:0000250|UniProtKB:P09874};
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:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-
CC ribosyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:58236, Rhea:RHEA-
CC COMP:10136, Rhea:RHEA-COMP:15092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:46858, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142557; Evidence={ECO:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58237;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- SUBUNIT: Homo- and heterodimer with PARP2. Interacts with APTX (By
CC similarity). Component of a base excision repair (BER) complex,
CC containing at least XRCC1, PARP1, PARP2, POLB and LRIG3 (By
CC similarity). Interacts with SRY (By similarity). The SWAP complex
CC consists of NPM1, NCL, PARP1 and SWAP70. Interacts with TIAM2 (By
CC similarity). Interacts with PARP3; leading to activate PARP1 in absence
CC of DNA (By similarity). Interacts (when poly-ADP-ribosylated) with
CC CHD1L (via macro domain). Interacts with the DNA polymerase alpha
CC catalytic subunit POLA1; this interaction functions as part of the
CC control of replication fork progression. Interacts with EEF1A1 and TXK.
CC Interacts with RNF4. Interacts with RNF146. Interacts with ZNF423.
CC Interacts with APLF. Interacts with SNAI1 (via zinc fingers); the
CC interaction requires SNAI1 to be poly-ADP-ribosylated and non-
CC phosphorylated (active) by GSK3B. Interacts (when poly-ADP-ribosylated)
CC with PARP9 (By similarity). Interacts with NR4A3; activates PARP1 by
CC improving acetylation of PARP1 and suppressing the interaction between
CC PARP1 and SIRT1 (PubMed:25625556). Interacts (via catalytic domain)
CC with PUM3; the interaction inhibits the poly-ADP-ribosylation activity
CC of PARP1 and the degradation of PARP1 by CASP3 following genotoxic
CC stress. Interacts (via the PARP catalytic domain) with HPF1. Interacts
CC with ZNF365. Interacts with RRP1B. Interacts with TIMELESS; the
CC interaction is direct. Interacts with CGAS; leading to impede the
CC formation of the PARP1-TIMELESS complex (By similarity). Interacts with
CC KHDC3, the interaction is increased following the formation of DNA
CC double-strand breaks (By similarity). {ECO:0000250|UniProtKB:P09874,
CC ECO:0000250|UniProtKB:P11103, ECO:0000269|PubMed:25625556}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09874}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:P09874}. Chromosome
CC {ECO:0000250|UniProtKB:P09874}. Note=Localizes to sites of DNA damage.
CC {ECO:0000250|UniProtKB:P09874}.
CC -!- DOMAIN: The N-terminal disordered region does not act as a key DNA-
CC binding domain. The WGR and PARP catalytic domains function together to
CC recruit PARP1 to sites of DNA breaks. The N-terminal disordered region
CC is only required for activation on specific types of DNA damage.
CC {ECO:0000250|UniProtKB:Q9UGN5}.
CC -!- DOMAIN: The WGR domain bridges two nucleosomes, with the broken DNA
CC aligned in a position suitable for ligation. The bridging induces
CC structural changes in PARP1 that signal the recognition of a DNA break
CC to the catalytic domain of PARP1, promoting HPF1 recruitment and
CC subsequent activation of PARP1, licensing serine ADP-ribosylation of
CC target proteins. {ECO:0000250|UniProtKB:Q9UGN5}.
CC -!- PTM: Poly-ADP-ribosylated on glutamate and aspartate residues by
CC autocatalysis. Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation
CC mediates the recruitment of CHD1L to DNA damage sites. ADP-ribosylated
CC on serine by autocatalysis; serine ADP-ribosylation takes place
CC following interaction with HPF1 (By similarity). Auto poly-ADP-
CC ribosylated on serine residues, leading to dissociation of the PARP1-
CC HPF1 complex from chromatin (By similarity). Mono-ADP-ribosylated at
CC Lys-521 by SIRT6 in response to oxidative stress, promoting recruitment
CC to double-strand breaks (DSBs) sites (By similarity).
CC {ECO:0000250|UniProtKB:P09874, ECO:0000250|UniProtKB:Q9UGN5}.
CC -!- PTM: S-nitrosylated, leading to inhibit transcription regulation
CC activity. {ECO:0000250|UniProtKB:P11103}.
CC -!- PTM: Phosphorylated by PRKDC and TXK. {ECO:0000250|UniProtKB:P09874}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA46478.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U94340; AAC53544.1; -; mRNA.
DR EMBL; BC085765; AAH85765.1; -; mRNA.
DR EMBL; X65496; CAA46477.1; -; Genomic_DNA.
DR EMBL; X65497; CAA46478.1; ALT_INIT; Genomic_DNA.
DR PIR; S21163; S21163.
DR PIR; S26057; S26057.
DR RefSeq; NP_037195.1; NM_013063.2.
DR PDB; 2LE0; NMR; -; A=389-487.
DR PDBsum; 2LE0; -.
DR AlphaFoldDB; P27008; -.
DR SMR; P27008; -.
DR BioGRID; 247621; 19.
DR IntAct; P27008; 1.
DR MINT; P27008; -.
DR STRING; 10116.ENSRNOP00000004232; -.
DR BindingDB; P27008; -.
DR ChEMBL; CHEMBL4664; -.
DR CarbonylDB; P27008; -.
DR iPTMnet; P27008; -.
DR PhosphoSitePlus; P27008; -.
DR jPOST; P27008; -.
DR PaxDb; P27008; -.
DR PRIDE; P27008; -.
DR Ensembl; ENSRNOT00000004232; ENSRNOP00000004232; ENSRNOG00000003084.
DR GeneID; 25591; -.
DR KEGG; rno:25591; -.
DR UCSC; RGD:2053; rat.
DR CTD; 142; -.
DR RGD; 2053; Parp1.
DR eggNOG; KOG1037; Eukaryota.
DR GeneTree; ENSGT00940000156058; -.
DR HOGENOM; CLU_004841_0_0_1; -.
DR InParanoid; P27008; -.
DR OMA; RSAMMEF; -.
DR OrthoDB; 909382at2759; -.
DR PhylomeDB; P27008; -.
DR TreeFam; TF316616; -.
DR Reactome; R-RNO-110362; POLB-Dependent Long Patch Base Excision Repair.
DR Reactome; R-RNO-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-RNO-5685939; HDR through MMEJ (alt-NHEJ).
DR Reactome; R-RNO-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-RNO-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-RNO-5696400; Dual Incision in GG-NER.
DR PRO; PR:P27008; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003084; Expressed in heart and 19 other tissues.
DR Genevisible; P27008; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0032993; C:protein-DNA complex; ISO:RGD.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0051287; F:NAD binding; IDA:RGD.
DR GO; GO:0140294; F:NAD DNA ADP-ribosyltransferase activity; ISO:RGD.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:RGD.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:RGD.
DR GO; GO:0016763; F:pentosyltransferase activity; NAS:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0046332; F:SMAD binding; IPI:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISS:UniProtKB.
DR GO; GO:0006284; P:base-excision repair; ISO:RGD.
DR GO; GO:0048148; P:behavioral response to cocaine; ISO:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IMP:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0071451; P:cellular response to superoxide; ISO:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IMP:RGD.
DR GO; GO:0034644; P:cellular response to UV; ISO:RGD.
DR GO; GO:0071294; P:cellular response to zinc ion; IEP:RGD.
DR GO; GO:0030592; P:DNA ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0006259; P:DNA metabolic process; ISO:RGD.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0032042; P:mitochondrial DNA metabolic process; ISO:RGD.
DR GO; GO:0043504; P:mitochondrial DNA repair; ISO:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:2001170; P:negative regulation of ATP biosynthetic process; ISO:RGD.
DR GO; GO:0032700; P:negative regulation of interleukin-17 production; ISO:RGD.
DR GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; ISO:RGD.
DR GO; GO:0018424; P:peptidyl-glutamic acid poly-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0018312; P:peptidyl-serine ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IMP:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IMP:RGD.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IMP:RGD.
DR GO; GO:1904762; P:positive regulation of myofibroblast differentiation; IMP:RGD.
DR GO; GO:1901216; P:positive regulation of neuron death; IMP:RGD.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:RGD.
DR GO; GO:1903518; P:positive regulation of single strand break repair; ISO:RGD.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IMP:BHF-UCL.
DR GO; GO:0006471; P:protein ADP-ribosylation; IDA:RGD.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; IDA:RGD.
DR GO; GO:0036211; P:protein modification process; ISO:RGD.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IMP:BHF-UCL.
DR GO; GO:0050790; P:regulation of catalytic activity; ISO:RGD.
DR GO; GO:0044030; P:regulation of DNA methylation; IMP:RGD.
DR GO; GO:0040009; P:regulation of growth rate; ISO:RGD.
DR GO; GO:1903376; P:regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IMP:RGD.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:1903516; P:regulation of single strand break repair; ISO:RGD.
DR GO; GO:0010990; P:regulation of SMAD protein complex assembly; IMP:RGD.
DR GO; GO:1904044; P:response to aldosterone; IEP:RGD.
DR GO; GO:0010332; P:response to gamma radiation; IEP:RGD.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0000723; P:telomere maintenance; ISO:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0050882; P:voluntary musculoskeletal movement; ISO:RGD.
DR Gene3D; 1.20.142.10; -; 1.
DR Gene3D; 2.20.25.630; -; 1.
DR Gene3D; 3.30.1740.10; -; 2.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR012982; PADR1.
DR InterPro; IPR038650; PADR1_dom_sf.
DR InterPro; IPR008288; PARP.
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 InterPro; IPR001510; Znf_PARP.
DR InterPro; IPR036957; Znf_PARP_sf.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08063; PADR1; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR Pfam; PF00645; zf-PARP; 2.
DR PIRSF; PIRSF000489; NAD_ADPRT; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM01335; PADR1; 1.
DR SMART; SM00773; WGR; 1.
DR SMART; SM01336; zf-PARP; 2.
DR SUPFAM; SSF142921; SSF142921; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS00347; PARP_ZN_FINGER_1; 2.
DR PROSITE; PS50064; PARP_ZN_FINGER_2; 2.
DR PROSITE; PS51977; WGR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Chromosome; DNA damage;
KW DNA repair; DNA-binding; Glycosyltransferase; Isopeptide bond;
KW Metal-binding; NAD; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CHAIN 2..1014
FT /note="Poly [ADP-ribose] polymerase 1"
FT /id="PRO_0000211321"
FT DOMAIN 386..477
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 542..638
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 662..779
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 788..1014
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT ZN_FING 9..93
FT /note="PARP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT ZN_FING 113..203
FT /note="PARP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT REGION 357..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..524
FT /note="Automodification domain"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT REGION 496..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 207..209
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOTIF 221..226
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT ACT_SITE 988
FT /note="For poly [ADP-ribose] polymerase activity"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT BINDING 862..864
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 871
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 878
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 904
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 388
FT /note="PolyADP-ribosyl aspartic acid"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 408
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 414
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 436
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 438
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 445
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 446
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 457
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 485
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 489
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 492
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 500
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 504
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 507
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 513
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 514
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 519
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 520
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 521
FT /note="N6-(ADP-ribosyl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 600
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 621
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 192
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 468
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 487
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 487
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 512
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 528
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 748
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 748
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CONFLICT 639
FT /note="Y -> H (in Ref. 5; CAA46478)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="E -> A (in Ref. 5; CAA46478)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="N -> D (in Ref. 5; CAA46478)"
FT /evidence="ECO:0000305"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:2LE0"
FT HELIX 406..416
FT /evidence="ECO:0007829|PDB:2LE0"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:2LE0"
FT STRAND 427..431
FT /evidence="ECO:0007829|PDB:2LE0"
FT HELIX 434..439
FT /evidence="ECO:0007829|PDB:2LE0"
FT HELIX 442..449
FT /evidence="ECO:0007829|PDB:2LE0"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:2LE0"
FT HELIX 458..465
FT /evidence="ECO:0007829|PDB:2LE0"
FT HELIX 470..476
FT /evidence="ECO:0007829|PDB:2LE0"
SQ SEQUENCE 1014 AA; 112660 MW; BE1B6F2B29B887ED CRC64;
MAEATERLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH WYHFSCFWKV
GHSIRQPDTE VDGFSELRWD DQQKVKKTAE AGGVAGKGQH GGGGKAEKTL GDFAAEYAKS
NRSTCKGCME KIEKGQMRLS KKMLDPEKPQ LGMIDRWYHP TCFVKNRDEL GFRPEYSASQ
LKGFSLLSAE DKEALKKQLP AVKSEGKRKC DEVDGIDEVA KKKSKKGKDK ESSKLEKALK
AQNELVWNIK DELKKACSTN DLKELLIFNQ QQVPSGESAI LDRVADGMAF GALLPCKECS
GQLVFKSDAY YCTGDVTAWT KCMVKTQNPS RKEWVTPKEF REISYLKKLK IKKQDRLFPP
ESSAPAPPAP PVSITSAPTA VNSSAPADKP LSNMKILTLG KLSQNKDEAK AMIEKLGGKL
TGSANKASLC ISTKKEVEKM SKKMEEVKAA NVRVVCEDFL QDVSASAKSL QELLSAHSLS
SWGAEVKVEP GEVVVPKGKS AAPSKKSKGA VKEEGVNKSE KRMKLTLKGG AAVDPDSGLE
HSAHVLEKGG KVFSATLGLV DIVKGTNSYY KLQLLESDKE SRYWIFRSWG RVGTVIGSNK
LEQMPSKEDA VEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE AVKKLAVKPG
TKSKLPKPVQ ELVGMIFDVE SMKKALVEYE IDLQKMPLGK LSRRQIQAAY SILSEVQQAV
SQGSSESQIL DLSNRFYTLI PHDFGMKKPP LLNNTDSVQA KVEMLDNLLD IEVAYSLLRG
GSDDSSKDPI DVNYEKLKTD IKVVDRDSEE AEVIRKYVKN THATTHNAYD LEVIDIFKIE
REGESQRYKP FRQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM
VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG LGKTAPDPSA
SITLDGVEVP LGTGIPSGVN DTCLLYNEYI VYDIAQVNLK YLLKLKFNFK TSLW
