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Protein

Poly [ADP-ribose] polymerase 1

Gene

PARP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 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).8 Publications

Catalytic activityi

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.PROSITE-ProRule annotation1 Publication

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
  • NAD+ ADP-ribosyltransferase activity Source: UniProtKB
  • NAD binding Source: Ensembl
  • poly(A) RNA binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • transcription factor binding Source: BHF-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS07107-MONOMER.
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:2.4.2.30)
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

HGNCiHGNC:270. PARP1.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
  • mitochondrion Source: MGI
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear envelope Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • protein complex Source: MGI
  • transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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.
DrugBankiDB02701. Nicotinamide.
DB09074. Olaparib.
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-linki203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki203Glycyl 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)Combined sources
Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei488PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei491PolyADP-ribosyl glutamic acidSequence analysis1
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 residuei520PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei600N6-acetyllysineCombined sources1
Modified residuei621N6-acetyllysineCombined sources1
Cross-linki748Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki748Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined 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.
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).By similarity13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-355676,EBI-355676
APLFQ8IW193EBI-355676,EBI-1256044
APTXQ7Z2E38EBI-355676,EBI-847814
CEBPAP497152EBI-355676,EBI-1172054
E2F1Q010942EBI-355676,EBI-448924
ERGP113087EBI-355676,EBI-79704
IL24Q130072EBI-355676,EBI-3915542
OARD1Q9Y5305EBI-355676,EBI-8502288
PIAS4Q8N2W95EBI-355676,EBI-473160
SNAI1O9586310EBI-355676,EBI-1045459
Snai1Q020853EBI-355676,EBI-6049807From a different organism.
SUMO1P631652EBI-355676,EBI-80140
TP53P046373EBI-355676,EBI-366083
UBCP0CG482EBI-355676,EBI-3390054
WRNQ141918EBI-355676,EBI-368417
XRCC1P188876EBI-355676,EBI-947466
ZNF423Q2M1K92EBI-355676,EBI-950016

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi106652. 243 interactors.
DIPiDIP-38N.
IntActiP09874. 93 interactors.
MINTiMINT-104344.
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[»]
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

Sequence similaritiesi

Contains 1 BRCT domain.PROSITE-ProRule annotation
Contains 1 PARP alpha-helical domain.PROSITE-ProRule annotation
Contains 1 PARP catalytic domain.PROSITE-ProRule annotation
Contains 2 PARP-type zinc fingers.PROSITE-ProRule annotation

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.
OMAiEIEVAYN.
OrthoDBiEOG091G13H1.
PhylomeDBiP09874.
TreeFamiTF316616.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di1.20.142.10. 1 hit.
2.20.140.10. 1 hit.
3.30.1740.10. 2 hits.
3.40.50.10190. 1 hit.
3.90.228.10. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR012982. PADR1.
IPR008288. PARP.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
IPR001510. Znf_PARP.
[Graphical view]
PfamiPF00533. 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.
[Graphical view]
PIRSFiPIRSF000489. NAD_ADPRT. 1 hit.
SMARTiSM00292. BRCT. 1 hit.
SM01335. PADR1. 1 hit.
SM00773. WGR. 1 hit.
SM01336. zf-PARP. 2 hits.
[Graphical view]
SUPFAMiSSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09874-1 [UniParc]FASTAAdd to basket

« Hide

        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 rs3738708dbSNPEnsembl.1
Natural variantiVAR_014714188A → T.1 PublicationCorresponds to variant rs1805409dbSNPEnsembl.1
Natural variantiVAR_019171334V → I.1 PublicationCorresponds to variant rs3219057dbSNPEnsembl.1
Natural variantiVAR_050461377P → S.Corresponds to variant rs2230484dbSNPEnsembl.1
Natural variantiVAR_019172383S → Y.1 PublicationCorresponds to variant rs3219062dbSNPEnsembl.1
Natural variantiVAR_035852488E → V in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_014715762V → A.2 PublicationsCorresponds to variant rs1136410dbSNPEnsembl.1
Natural variantiVAR_019173940K → R.2 PublicationsCorresponds to variant rs3219145dbSNPEnsembl.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, AL359742 Genomic DNA. Translation: CAH70215.1.
AL359742, AL359704 Genomic DNA. Translation: CAI12102.1.
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

Cross-referencesi

Web resourcesi

NIEHS-SNPs

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, AL359742 Genomic DNA. Translation: CAH70215.1.
AL359742, AL359704 Genomic DNA. Translation: CAI12102.1.
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.

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[»]
ProteinModelPortaliP09874.
SMRiP09874.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106652. 243 interactors.
DIPiDIP-38N.
IntActiP09874. 93 interactors.
MINTiMINT-104344.
STRINGi9606.ENSP00000355759.

Chemistry databases

BindingDBiP09874.
ChEMBLiCHEMBL3105.
DrugBankiDB02701. Nicotinamide.
DB09074. Olaparib.
GuidetoPHARMACOLOGYi2771.

PTM databases

iPTMnetiP09874.
PhosphoSitePlusiP09874.
SwissPalmiP09874.

Polymorphism and mutation databases

BioMutaiPARP1.
DMDMi130781.

2D gel databases

SWISS-2DPAGEP09874.

Proteomic databases

EPDiP09874.
MaxQBiP09874.
PaxDbiP09874.
PeptideAtlasiP09874.
PRIDEiP09874.

Protocols and materials databases

DNASUi142.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi142.
DisGeNETi142.
GeneCardsiPARP1.
H-InvDBHIX0023551.
HGNCiHGNC:270. PARP1.
HPAiCAB000147.
CAB003839.
CAB003840.
CAB075726.
CAB075727.
HPA045168.
MIMi173870. gene.
neXtProtiNX_P09874.
OpenTargetsiENSG00000143799.
PharmGKBiPA32.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:HS07107-MONOMER.
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.

Miscellaneous databases

ChiTaRSiPARP1. human.
EvolutionaryTraceiP09874.
GeneWikiiPARP1.
GenomeRNAii142.
PMAP-CutDBP09874.
PROiP09874.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143799.
CleanExiHS_PARP1.
ExpressionAtlasiP09874. baseline and differential.
GenevisibleiP09874. HS.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di1.20.142.10. 1 hit.
2.20.140.10. 1 hit.
3.30.1740.10. 2 hits.
3.40.50.10190. 1 hit.
3.90.228.10. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR012982. PADR1.
IPR008288. PARP.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
IPR001510. Znf_PARP.
[Graphical view]
PfamiPF00533. 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.
[Graphical view]
PIRSFiPIRSF000489. NAD_ADPRT. 1 hit.
SMARTiSM00292. BRCT. 1 hit.
SM01335. PADR1. 1 hit.
SM00773. WGR. 1 hit.
SM01336. zf-PARP. 2 hits.
[Graphical view]
SUPFAMiSSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPARP1_HUMAN
AccessioniPrimary (citable) accession number: P09874
Secondary accession number(s): B1ANJ4, Q8IUZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 213 of the entry and version 4 of the sequence. [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

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.

Keywords - Technical termi

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

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.