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Protein

Poly [ADP-ribose] polymerase 1

Gene

PARP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks (PubMed:17177976, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:23230272). Mediates the poly(ADP-ribosyl)ation of APLF and CHFR (PubMed:17396150). Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production (PubMed:17177976). Required for PARP9 and DTX3L recruitment to DNA damage sites (PubMed:23230272). PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (PubMed:23230272). Mediates serine ADP-ribosylation of target proteins following interaction with HPF1; HPF1 conferring serine specificity (PubMed:28190768). Mediates the poly(ADP-ribosyl)ation of histones in a HPF1-dependent manner (PubMed:27067600). Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257).9 Publications

Miscellaneous

The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxyl group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.

Catalytic activityi

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.PROSITE-ProRule annotation2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi2 – 372Add BLAST371
Zinc fingeri9 – 93PARP-type 1PROSITE-ProRule annotationAdd BLAST85
Zinc fingeri113 – 203PARP-type 2PROSITE-ProRule annotationAdd BLAST91

GO - Molecular functioni

  • DNA binding Source: ProtInc
  • DNA ligase (ATP) activity Source: GO_Central
  • enzyme binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • NAD+ ADP-ribosyltransferase activity Source: UniProtKB
  • NAD binding Source: Ensembl
  • protein ADP-ribosylase activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  • R-SMAD binding Source: Ensembl
  • transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding Source: NTNU_SB
  • transcription factor binding Source: BHF-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • ATP generation from poly-ADP-D-ribose Source: UniProtKB
  • cellular response to amyloid-beta Source: Ensembl
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to insulin stimulus Source: BHF-UCL
  • cellular response to oxidative stress Source: MGI
  • cellular response to UV Source: BHF-UCL
  • cellular response to zinc ion Source: Ensembl
  • DNA damage response, detection of DNA damage Source: Ensembl
  • DNA ligation involved in DNA repair Source: GO_Central
  • DNA repair Source: UniProtKB
  • double-strand break repair Source: UniProtKB
  • double-strand break repair via homologous recombination Source: Reactome
  • global genome nucleotide-excision repair Source: Reactome
  • lagging strand elongation Source: GO_Central
  • macrophage differentiation Source: UniProtKB
  • mitochondrial DNA metabolic process Source: MGI
  • mitochondrial DNA repair Source: MGI
  • mitochondrion organization Source: MGI
  • negative regulation of ATP biosynthetic process Source: ParkinsonsUK-UCL
  • negative regulation of telomere maintenance via telomere lengthening Source: BHF-UCL
  • negative regulation of transcription by RNA polymerase II Source: Reactome
  • nucleotide-excision repair, DNA damage recognition Source: Reactome
  • nucleotide-excision repair, DNA incision Source: Reactome
  • nucleotide-excision repair, DNA incision, 5'-to lesion Source: Reactome
  • nucleotide-excision repair, preincision complex assembly Source: Reactome
  • nucleotide-excision repair, preincision complex stabilization Source: Reactome
  • peptidyl-serine ADP-ribosylation Source: UniProtKB
  • positive regulation of cardiac muscle hypertrophy Source: UniProtKB
  • positive regulation of intracellular estrogen receptor signaling pathway Source: Ensembl
  • positive regulation of mitochondrial depolarization Source: Ensembl
  • positive regulation of myofibroblast differentiation Source: Ensembl
  • positive regulation of neuron death Source: Ensembl
  • positive regulation of protein localization to nucleus Source: Ensembl
  • positive regulation of single strand break repair Source: UniProtKB
  • positive regulation of SMAD protein signal transduction Source: Ensembl
  • positive regulation of transcription by RNA polymerase II Source: NTNU_SB
  • positive regulation of transcription regulatory region DNA binding Source: Ensembl
  • protein ADP-ribosylation Source: UniProtKB
  • protein autoprocessing Source: Ensembl
  • protein modification process Source: MGI
  • protein poly-ADP-ribosylation Source: UniProtKB
  • regulation of catalytic activity Source: BHF-UCL
  • regulation of cellular protein localization Source: MGI
  • regulation of DNA methylation Source: Ensembl
  • regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway Source: Ensembl
  • regulation of SMAD protein complex assembly Source: Ensembl
  • response to aldosterone Source: Ensembl
  • response to gamma radiation Source: Ensembl
  • signal transduction involved in regulation of gene expression Source: Ensembl
  • telomere maintenance Source: BHF-UCL
  • transcription by RNA polymerase II Source: ProtInc
  • transforming growth factor beta receptor signaling pathway Source: Ensembl

Keywordsi

Molecular functionDNA-binding, Glycosyltransferase, Transferase
Biological processDNA damage, DNA repair, Transcription, Transcription regulation
LigandMetal-binding, NAD, Zinc

Enzyme and pathway databases

BRENDAi2.4.2.30 2681
ReactomeiR-HSA-110362 POLB-Dependent Long Patch Base Excision Repair
R-HSA-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-5685939 HDR through MMEJ (alt-NHEJ)
R-HSA-5696394 DNA Damage Recognition in GG-NER
R-HSA-5696395 Formation of Incision Complex in GG-NER
R-HSA-5696400 Dual Incision in GG-NER
SignaLinkiP09874
SIGNORiP09874

Names & Taxonomyi

Protein namesi
Recommended name:
Poly [ADP-ribose] polymerase 1 (EC:2.4.2.302 Publications)
Short name:
PARP-1
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 1
Short name:
ARTD1
NAD(+) ADP-ribosyltransferase 1
Short name:
ADPRT 1
Poly[ADP-ribose] synthase 1
Gene namesi
Name:PARP1
Synonyms:ADPRT, PPOL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000143799.12
HGNCiHGNC:270 PARP1
MIMi173870 gene
neXtProtiNX_P09874

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi499S → A: Abolishes automodification on serine following interaction with HPF1; when associated with A-507 and A-519. 1 Publication1
Mutagenesisi507S → A: Abolishes automodification on serine following interaction with HPF1; when associated with A-499 and A-519. 1 Publication1
Mutagenesisi519S → A: Abolishes automodification on serine following interaction with HPF1; when associated with A-499 and A-507. 1 Publication1
Mutagenesisi797L → P: 1.5% of wild-type activity. 1
Mutagenesisi868N → S: 4% of wild-type activity. 1
Mutagenesisi890M → V: <0.5% of wild-type activity. 1
Mutagenesisi893K → I: Abolishes enzymatic activity. 1
Mutagenesisi897F → S: 10% of wild-type activity. 1
Mutagenesisi899D → N: 0.6% of wild-type activity. 1
Mutagenesisi908C → R: <0.5% of wild-type activity. 1
Mutagenesisi926L → F: 1.5% of wild-type activity. 1
Mutagenesisi986Y → H: 14% of wild-type activity and increased branching 15-fold. 1
Mutagenesisi988E → K: 1.25% of wild-type activity; only monomers are added. 1
Mutagenesisi1003L → P: 1.5% of wild-type activity. 1

Organism-specific databases

DisGeNETi142
OpenTargetsiENSG00000143799
PharmGKBiPA32

Chemistry databases

ChEMBLiCHEMBL3105
DrugBankiDB04010 2-(3'-Methoxyphenyl) Benzimidazole-4-Carboxamide
DB03509 2-(4-Chlorophenyl)-5-Quinoxalinecarboxamide
DB03073 3-Methoxybenzamide
DB02498 Carba-Nicotinamide-Adenine-Dinucleotide
DB02701 Nicotinamide
DB02690 NU1025
DB09074 Olaparib
DB12332 Rucaparib
DB07330 trans-4-(7-carbamoyl-1H-benzimidazol-2-yl)-1-propylpiperidinium
DB07232 Veliparib
GuidetoPHARMACOLOGYi2771

Polymorphism and mutation databases

BioMutaiPARP1
DMDMi130781

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00002113202 – 1014Poly [ADP-ribose] polymerase 1Add BLAST1013

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei41PhosphoserineCombined sources1
Modified residuei97N6-acetyllysineCombined sources1
Modified residuei105N6-acetyllysineCombined sources1
Modified residuei131N6-acetyllysineCombined sources1
Modified residuei177PhosphoserineCombined sources1
Modified residuei179PhosphoserineCombined sources1
Modified residuei185PhosphoserineCombined sources1
Cross-linki192Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei274PhosphoserineCombined sources1
Modified residuei277PhosphoserineCombined sources1
Modified residuei364PhosphoserineCombined sources1
Modified residuei368PhosphothreonineCombined sources1
Modified residuei407PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei413PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei435PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei437PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei444PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei445PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei448PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei456PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki467Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei471PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei484PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei488PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei491PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei499ADP-ribosylserine1 Publication1
Modified residuei507ADP-ribosylserine1 Publication1
Cross-linki512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei513PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei514PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei519ADP-ribosylserine1 Publication1
Modified residuei520PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki528Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei600N6-acetyllysineCombined sources1
Modified residuei621N6-acetyllysineCombined sources1
Cross-linki748Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki748Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei782PhosphoserineCombined sources1
Modified residuei786PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by PRKDC and TXK.2 Publications
Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites (PubMed:19661379). ADP-ribosylated on serine by autocatalysis; serine ADP-ribosylation takes place following interaction with HPF1 (PubMed:28190768).2 Publications
S-nitrosylated, leading to inhibit transcription regulation activity.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP09874
MaxQBiP09874
PaxDbiP09874
PeptideAtlasiP09874
PRIDEiP09874

2D gel databases

SWISS-2DPAGEP09874

PTM databases

iPTMnetiP09874
PhosphoSitePlusiP09874
SwissPalmiP09874

Miscellaneous databases

PMAP-CutDBP09874

Expressioni

Gene expression databases

BgeeiENSG00000143799
CleanExiHS_PARP1
ExpressionAtlasiP09874 baseline and differential
GenevisibleiP09874 HS

Organism-specific databases

HPAiCAB000147
CAB003839
CAB003840
CAB075726
CAB075727
HPA045168

Interactioni

Subunit structurei

Component of a base excision repair (BER) complex, containing at least XRCC1, PARP2, POLB and LRIG3. Homo- and heterodimer with PARP2. Interacts with APTX (PubMed:15044383). Interacts with PARP3. Interacts with SRY (PubMed:16904257). The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with TIAM2 (By similarity). Interacts (when poly-ADP-ribosylated) with CHD1L (PubMed:19661379). Interacts with the DNA polymerase alpha catalytic subunit POLA1; this interaction functions as part of the control of replication fork progression (PubMed:9518481). Interacts with EEF1A1 and TXK (PubMed:17177976). Interacts with RNF4 (PubMed:19779455). Interacts with RNF146 (PubMed:21799911). Interacts with ZNF423 (PubMed:22863007). Interacts with SNAI1 (via zinc fingers); the interaction requires SNAI1 to be poly-ADP-ribosylated and non-phosphorylated (active) by GSK3B (PubMed:21577210). Interacts (when poly-ADP-ribosylated) with PARP9 (PubMed:23230272). Interacts with NR4A3; activates PARP1 by improving acetylation of PARP1 and suppressing the interaction between PARP1 and SIRT1 (By similarity). Interacts (via catalytic domain) with PUM3; the interaction inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress (PubMed:21266351). Interacts (via the PARP catalytic domain) with HPF1 (PubMed:27067600, PubMed:28190768). Interacts with ZNF365 (PubMed:23966166). Interacts with RRP1B (PubMed:19710015).By similarity16 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein kinase binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • R-SMAD binding Source: Ensembl
  • transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi106652, 277 interactors
CORUMiP09874
DIPiDIP-38N
ELMiP09874
IntActiP09874, 108 interactors
MINTiP09874
STRINGi9606.ENSP00000355759

Chemistry databases

BindingDBiP09874

Structurei

Secondary structure

11014
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni2 – 5Combined sources4
Beta strandi8 – 13Combined sources6
Beta strandi15 – 17Combined sources3
Turni22 – 24Combined sources3
Beta strandi25 – 27Combined sources3
Beta strandi32 – 40Combined sources9
Beta strandi42 – 53Combined sources12
Helixi54 – 59Combined sources6
Helixi67 – 70Combined sources4
Helixi74 – 76Combined sources3
Helixi79 – 90Combined sources12
Beta strandi102 – 105Combined sources4
Beta strandi113 – 117Combined sources5
Beta strandi119 – 121Combined sources3
Turni126 – 128Combined sources3
Beta strandi137 – 145Combined sources9
Beta strandi148 – 158Combined sources11
Helixi160 – 165Combined sources6
Helixi167 – 170Combined sources4
Turni174 – 176Combined sources3
Helixi177 – 180Combined sources4
Helixi184 – 186Combined sources3
Helixi189 – 198Combined sources10
Turni204 – 206Combined sources3
Beta strandi209 – 211Combined sources3
Helixi226 – 255Combined sources30
Helixi258 – 267Combined sources10
Turni273 – 275Combined sources3
Helixi276 – 289Combined sources14
Turni296 – 298Combined sources3
Beta strandi302 – 305Combined sources4
Beta strandi308 – 311Combined sources4
Beta strandi314 – 316Combined sources3
Beta strandi324 – 327Combined sources4
Helixi337 – 340Combined sources4
Helixi342 – 347Combined sources6
Beta strandi389 – 392Combined sources4
Beta strandi394 – 397Combined sources4
Helixi405 – 414Combined sources10
Beta strandi418 – 421Combined sources4
Beta strandi427 – 430Combined sources4
Helixi433 – 438Combined sources6
Helixi441 – 448Combined sources8
Helixi457 – 463Combined sources7
Helixi469 – 475Combined sources7
Helixi535 – 537Combined sources3
Turni540 – 542Combined sources3
Beta strandi543 – 545Combined sources3
Beta strandi551 – 560Combined sources10
Turni562 – 564Combined sources3
Beta strandi567 – 573Combined sources7
Turni578 – 581Combined sources4
Beta strandi585 – 591Combined sources7
Beta strandi597 – 602Combined sources6
Helixi608 – 622Combined sources15
Beta strandi639 – 641Combined sources3
Helixi667 – 676Combined sources10
Helixi679 – 688Combined sources10
Turni693 – 695Combined sources3
Helixi698 – 700Combined sources3
Helixi703 – 721Combined sources19
Helixi726 – 739Combined sources14
Beta strandi745 – 747Combined sources3
Beta strandi752 – 754Combined sources3
Helixi755 – 779Combined sources25
Beta strandi785 – 787Combined sources3
Helixi789 – 795Combined sources7
Turni796 – 798Combined sources3
Beta strandi799 – 803Combined sources5
Beta strandi806 – 808Combined sources3
Helixi809 – 820Combined sources12
Helixi824 – 826Combined sources3
Beta strandi829 – 841Combined sources13
Helixi844 – 848Combined sources5
Helixi849 – 853Combined sources5
Beta strandi857 – 864Combined sources8
Helixi866 – 868Combined sources3
Helixi869 – 875Combined sources7
Beta strandi882 – 884Combined sources3
Helixi886 – 888Combined sources3
Beta strandi889 – 891Combined sources3
Beta strandi893 – 900Combined sources8
Helixi901 – 905Combined sources5
Helixi906 – 908Combined sources3
Beta strandi912 – 914Combined sources3
Beta strandi916 – 925Combined sources10
Beta strandi928 – 934Combined sources7
Beta strandi947 – 950Combined sources4
Beta strandi952 – 956Combined sources5
Helixi958 – 960Combined sources3
Beta strandi962 – 964Combined sources3
Beta strandi967 – 969Combined sources3
Beta strandi974 – 976Combined sources3
Beta strandi983 – 986Combined sources4
Beta strandi988 – 993Combined sources6
Helixi994 – 996Combined sources3
Beta strandi997 – 1009Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UK0X-ray3.00A/B662-1011[»]
1UK1X-ray3.00A/B662-1011[»]
1WOKX-ray3.00A/B/C/D662-1011[»]
2COKNMR-A387-486[»]
2CR9NMR-A518-643[»]
2CS2NMR-A103-223[»]
2DMJNMR-A1-93[»]
2JVNNMR-A233-358[»]
2L30NMR-A1-108[»]
2L31NMR-A103-214[»]
2N8ANMR-A1-214[»]
2RCWX-ray2.80A662-1011[»]
2RD6X-ray2.30A662-1011[»]
2RIQX-ray1.70A216-366[»]
3GJWX-ray2.30A662-1011[»]
3GN7X-ray2.50A662-1011[»]
3L3LX-ray2.50A662-1011[»]
3L3MX-ray2.50A662-1011[»]
3OD8X-ray2.40A/B/C/D/E/F/G/H2-96[»]
3ODAX-ray2.64A/B/C/D/E/F/G/H2-96[»]
3ODCX-ray2.80A/B105-206[»]
3ODEX-ray2.95A/B105-206[»]
4AV1X-ray3.10A/B/C/D5-202[»]
4DQYX-ray3.25A/D1-96[»]
B/E216-366[»]
C/F518-1014[»]
4GV7X-ray2.89A/B/C/D662-1011[»]
4HHYX-ray2.36A/B/C/D660-1011[»]
4HHZX-ray2.72A/B/C/D660-1011[»]
4L6SX-ray2.20A/B662-1011[»]
4OPXX-ray3.31A/D1-97[»]
A/D207-366[»]
C/F518-1014[»]
4OQAX-ray3.65A/D1-97[»]
A/D207-366[»]
C/F518-1014[»]
4OQBX-ray3.36A/D1-97[»]
A/D207-366[»]
C/F518-1014[»]
4PJTX-ray2.35A/B/C/D662-1011[»]
4R5WX-ray2.84A/B662-1011[»]
4R6EX-ray2.20A/B/C/D662-1011[»]
4RV6X-ray3.19A/B/C/D662-1011[»]
4UNDX-ray2.20A/B662-1011[»]
4UXBX-ray3.22A/B662-1011[»]
4XHUX-ray2.09A/C661-1014[»]
4ZZZX-ray1.90A/B655-1014[»]
5A00X-ray2.75A655-1014[»]
5DS3X-ray2.60A788-1012[»]
5HA9X-ray4.01A/B662-1011[»]
5KPNX-ray2.30A/B662-1011[»]
5KPOX-ray2.65A/B662-1011[»]
5KPPX-ray2.33A/B662-1011[»]
5KPQX-ray2.55A/B662-1011[»]
5WRQX-ray2.65A/B662-1011[»]
5WRYX-ray2.30A/B662-1011[»]
5WRZX-ray2.20A/B662-1011[»]
5WS0X-ray2.60A/B662-1011[»]
5WS1X-ray1.90A/B662-1011[»]
5WTCX-ray2.20A/B662-1011[»]
6BHVX-ray2.30A/B/C/D788-1012[»]
ProteinModelPortaliP09874
SMRiP09874
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09874

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini385 – 476BRCTPROSITE-ProRule annotationAdd BLAST92
Domaini662 – 779PARP alpha-helicalPROSITE-ProRule annotationAdd BLAST118
Domaini788 – 1014PARP catalyticPROSITE-ProRule annotationAdd BLAST227

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni373 – 524Automodification domainAdd BLAST152

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi207 – 209Nuclear localization signal1 Publication3
Motifi221 – 226Nuclear localization signal1 Publication6

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri9 – 93PARP-type 1PROSITE-ProRule annotationAdd BLAST85
Zinc fingeri113 – 203PARP-type 2PROSITE-ProRule annotationAdd BLAST91

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1037 Eukaryota
ENOG410XP18 LUCA
GeneTreeiENSGT00390000017341
HOGENOMiHOG000030402
HOVERGENiHBG053513
InParanoidiP09874
KOiK10798
OMAiWNHASCI
OrthoDBiEOG091G13H1
PhylomeDBiP09874
TreeFamiTF316616

Family and domain databases

CDDicd00027 BRCT, 1 hit
Gene3Di1.20.142.10, 1 hit
2.20.140.10, 1 hit
2.20.25.630, 1 hit
3.30.1740.10, 2 hits
3.40.50.10190, 1 hit
InterProiView protein in InterPro
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR012982 PADR1
IPR038650 PADR1_dom_sf
IPR008288 PARP
IPR012317 Poly(ADP-ribose)pol_cat_dom
IPR004102 Poly(ADP-ribose)pol_reg_dom
IPR036616 Poly(ADP-ribose)pol_reg_dom_sf
IPR036930 WGR_dom_sf
IPR008893 WGR_domain
IPR001510 Znf_PARP
IPR036957 Znf_PARP_sf
PfamiView protein in Pfam
PF00533 BRCT, 1 hit
PF08063 PADR1, 1 hit
PF00644 PARP, 1 hit
PF02877 PARP_reg, 1 hit
PF05406 WGR, 1 hit
PF00645 zf-PARP, 2 hits
PIRSFiPIRSF000489 NAD_ADPRT, 1 hit
SMARTiView protein in SMART
SM00292 BRCT, 1 hit
SM01335 PADR1, 1 hit
SM00773 WGR, 1 hit
SM01336 zf-PARP, 2 hits
SUPFAMiSSF142921 SSF142921, 1 hit
SSF47587 SSF47587, 1 hit
SSF52113 SSF52113, 1 hit
PROSITEiView protein in PROSITE
PS50172 BRCT, 1 hit
PS51060 PARP_ALPHA_HD, 1 hit
PS51059 PARP_CATALYTIC, 1 hit
PS00347 PARP_ZN_FINGER_1, 2 hits
PS50064 PARP_ZN_FINGER_2, 2 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09874-1 [UniParc]FASTAAdd to basket

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        10         20         30         40         50
MAESSDKLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH
60 70 80 90 100
WYHFSCFWKV GHSIRHPDVE VDGFSELRWD DQQKVKKTAE AGGVTGKGQD
110 120 130 140 150
GIGSKAEKTL GDFAAEYAKS NRSTCKGCME KIEKGQVRLS KKMVDPEKPQ
160 170 180 190 200
LGMIDRWYHP GCFVKNREEL GFRPEYSASQ LKGFSLLATE DKEALKKQLP
210 220 230 240 250
GVKSEGKRKG DEVDGVDEVA KKKSKKEKDK DSKLEKALKA QNDLIWNIKD
260 270 280 290 300
ELKKVCSTND LKELLIFNKQ QVPSGESAIL DRVADGMVFG ALLPCEECSG
310 320 330 340 350
QLVFKSDAYY CTGDVTAWTK CMVKTQTPNR KEWVTPKEFR EISYLKKLKV
360 370 380 390 400
KKQDRIFPPE TSASVAATPP PSTASAPAAV NSSASADKPL SNMKILTLGK
410 420 430 440 450
LSRNKDEVKA MIEKLGGKLT GTANKASLCI STKKEVEKMN KKMEEVKEAN
460 470 480 490 500
IRVVSEDFLQ DVSASTKSLQ ELFLAHILSP WGAEVKAEPV EVVAPRGKSG
510 520 530 540 550
AALSKKSKGQ VKEEGINKSE KRMKLTLKGG AAVDPDSGLE HSAHVLEKGG
560 570 580 590 600
KVFSATLGLV DIVKGTNSYY KLQLLEDDKE NRYWIFRSWG RVGTVIGSNK
610 620 630 640 650
LEQMPSKEDA IEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE
660 670 680 690 700
AVKKLTVNPG TKSKLPKPVQ DLIKMIFDVE SMKKAMVEYE IDLQKMPLGK
710 720 730 740 750
LSKRQIQAAY SILSEVQQAV SQGSSDSQIL DLSNRFYTLI PHDFGMKKPP
760 770 780 790 800
LLNNADSVQA KVEMLDNLLD IEVAYSLLRG GSDDSSKDPI DVNYEKLKTD
810 820 830 840 850
IKVVDRDSEE AEIIRKYVKN THATTHNAYD LEVIDIFKIE REGECQRYKP
860 870 880 890 900
FKQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM
910 920 930 940 950
VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG
960 970 980 990 1000
LGKTTPDPSA NISLDGVDVP LGTGISSGVN DTSLLYNEYI VYDIAQVNLK
1010
YLLKLKFNFK TSLW
Length:1,014
Mass (Da):113,084
Last modified:January 23, 2007 - v4
Checksum:i6A5FC01EB91C046B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti17G → E in AAB59447 (PubMed:2824474).Curated1
Sequence conflicti70E → Q in AAA60137 (PubMed:3120710).Curated1
Sequence conflicti212E → K in AAB59447 (PubMed:2824474).Curated1
Sequence conflicti613H → Q in AAA60155 (PubMed:2891139).Curated1
Sequence conflicti827N → S in AAA60155 (PubMed:2891139).Curated1
Sequence conflicti908C → Y in AAA60155 (PubMed:2891139).Curated1
Sequence conflicti980N → I in AAA60155 (PubMed:2891139).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05046054F → L. Corresponds to variant dbSNP:rs3738708Ensembl.1
Natural variantiVAR_014714188A → T1 PublicationCorresponds to variant dbSNP:rs1805409Ensembl.1
Natural variantiVAR_019171334V → I1 PublicationCorresponds to variant dbSNP:rs3219057Ensembl.1
Natural variantiVAR_050461377P → S. Corresponds to variant dbSNP:rs2230484Ensembl.1
Natural variantiVAR_019172383S → Y1 PublicationCorresponds to variant dbSNP:rs3219062Ensembl.1
Natural variantiVAR_035852488E → V in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_014715762V → A2 PublicationsCorresponds to variant dbSNP:rs1136410Ensembl.1
Natural variantiVAR_019173940K → R2 PublicationsCorresponds to variant dbSNP:rs3219145Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18112 mRNA Translation: AAA60137.1
J03473 mRNA Translation: AAB59447.1
M32721 mRNA Translation: AAA60155.1
M29786
, M29545, M29766, M29767, M29768, M29769, M29770, M29771, M29772, M29773, M29774, M29775, M29776, M29777, M29778, M29779, M29780, M29781, M29783, M29784, M29785, M29544, M29782 Genomic DNA Translation: AAA51663.1
AF524947 Genomic DNA Translation: AAM75364.1
AL359704 Genomic DNA No translation available.
AL359742 Genomic DNA No translation available.
CH471098 Genomic DNA Translation: EAW69783.1
BC037545 mRNA Translation: AAH37545.1
X56140, X56141 Genomic DNA Translation: CAA39606.1
X16674 Genomic DNA Translation: CAA34663.1
M60436 Genomic DNA Translation: AAA60000.1
M17081 mRNA Translation: AAA51599.1 Sequence problems.
CCDSiCCDS1554.1
PIRiA29725
RefSeqiNP_001609.2, NM_001618.3
UniGeneiHs.177766

Genome annotation databases

EnsembliENST00000366794; ENSP00000355759; ENSG00000143799
GeneIDi142
KEGGihsa:142
UCSCiuc001hqd.5 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPARP1_HUMAN
AccessioniPrimary (citable) accession number: P09874
Secondary accession number(s): B1ANJ4, Q8IUZ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 230 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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