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P09874

- PARP1_HUMAN

UniProt

P09874 - PARP1_HUMAN

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Protein

Poly [ADP-ribose] polymerase 1

Gene

PARP1

Organism
Homo sapiens (Human)
Status
Reviewed - 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. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. 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. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites.5 Publications

Catalytic activityi

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.1 PublicationPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi2 – 372371Add
BLAST
Zinc fingeri9 – 9385PARP-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri113 – 20391PARP-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. enzyme binding Source: UniProt
  3. identical protein binding Source: IntAct
  4. NAD+ ADP-ribosyltransferase activity Source: UniProtKB
  5. NAD binding Source: Ensembl
  6. poly(A) RNA binding Source: UniProtKB
  7. protein N-terminus binding Source: UniProtKB
  8. transcription factor binding Source: BHF-UCL
  9. zinc ion binding Source: InterPro

GO - Biological processi

  1. base-excision repair Source: Ensembl
  2. cellular response to insulin stimulus Source: BHF-UCL
  3. DNA damage response, detection of DNA damage Source: Ensembl
  4. DNA repair Source: UniProtKB
  5. double-strand break repair Source: UniProtKB
  6. gene expression Source: Reactome
  7. macrophage differentiation Source: UniProtKB
  8. negative regulation of transcription from RNA polymerase II promoter Source: Reactome
  9. positive regulation of SMAD protein import into nucleus Source: Ensembl
  10. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  11. positive regulation of transcription regulatory region DNA binding Source: Ensembl
  12. protein ADP-ribosylation Source: UniProtKB
  13. protein autoprocessing Source: Ensembl
  14. protein poly-ADP-ribosylation Source: UniProtKB
  15. regulation of growth rate Source: Ensembl
  16. signal transduction involved in regulation of gene expression Source: Ensembl
  17. telomere maintenance Source: Ensembl
  18. transcription, DNA-templated Source: Reactome
  19. transcription from RNA polymerase II promoter Source: ProtInc
  20. transcription initiation from RNA polymerase II promoter Source: Reactome
  21. transforming growth factor beta receptor signaling pathway Source: Reactome
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

BRENDAi2.4.2.30. 2681.
ReactomeiREACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
SignaLinkiP09874.

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
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:270. PARP1.

Subcellular locationi

Nucleus. Nucleusnucleolus
Note: Localizes at sites of DNA damage.

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. nuclear envelope Source: UniProtKB
  3. nucleolus Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. nucleus Source: HPA
  6. transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi797 – 7971L → P: 1.5% of wild-type activity.
Mutagenesisi868 – 8681N → S: 4% of wild-type activity.
Mutagenesisi890 – 8901M → V: <0.5% of wild-type activity.
Mutagenesisi893 – 8931K → I: Abolishes enzymatic activity.
Mutagenesisi897 – 8971F → S: 10% of wild-type activity.
Mutagenesisi899 – 8991D → N: 0.6% of wild-type activity.
Mutagenesisi908 – 9081C → R: <0.5% of wild-type activity.
Mutagenesisi926 – 9261L → F: 1.5% of wild-type activity.
Mutagenesisi986 – 9861Y → H: 14% of wild-type activity and increased branching 15-fold.
Mutagenesisi988 – 9881E → K: 1.25% of wild-type activity; only monomers are added.
Mutagenesisi1003 – 10031L → P: 1.5% of wild-type activity.

Organism-specific databases

PharmGKBiPA32.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 10141013Poly [ADP-ribose] polymerase 1PRO_0000211320Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei41 – 411Phosphoserine1 Publication
Modified residuei97 – 971N6-acetyllysine1 Publication
Modified residuei105 – 1051N6-acetyllysine1 Publication
Modified residuei131 – 1311N6-acetyllysine1 Publication
Modified residuei179 – 1791Phosphoserine1 Publication
Modified residuei368 – 3681Phosphothreonine1 Publication
Modified residuei407 – 4071PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei413 – 4131PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei435 – 4351PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei437 – 4371PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei444 – 4441PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei445 – 4451PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei448 – 4481PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei456 – 4561PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei471 – 4711PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei484 – 4841PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei488 – 4881PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei491 – 4911PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei513 – 5131PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei514 – 5141PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei520 – 5201PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei600 – 6001N6-acetyllysine1 Publication
Modified residuei621 – 6211N6-acetyllysine1 Publication
Modified residuei782 – 7821Phosphoserine4 Publications

Post-translational modificationi

Phosphorylated by PRKDC and TXK.7 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, Phosphoprotein

Proteomic databases

MaxQBiP09874.
PaxDbiP09874.
PeptideAtlasiP09874.
PRIDEiP09874.

2D gel databases

SWISS-2DPAGEP09874.

PTM databases

PhosphoSiteiP09874.

Miscellaneous databases

PMAP-CutDBP09874.

Expressioni

Gene expression databases

BgeeiP09874.
CleanExiHS_PARP1.
ExpressionAtlasiP09874. baseline and differential.
GenevestigatoriP09874.

Organism-specific databases

HPAiCAB000147.
CAB003839.
CAB003840.
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 PARP3, APTX and SRY. The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with TIAM2 (By similarity). Interacts (when poly-ADP-ribosylated) with CHD1L. Interacts with the DNA polymerase alpha catalytic subunit POLA1; this interaction functions as part of the control of replication fork progression. Interacts with EEF1A1, RNF4 and TXK. Interacts with RNF146. Interacts with ZNF423. Interacts with SNAI1 (via zinc fingers); the interaction requires SNAI1 to be poly-ADP-ribosylated and non-phosphorylated (active) by GSK3B. Interacts (when poly-ADP-ribosylated) with PARP9.By similarity11 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
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
XRCC1P188875EBI-355676,EBI-947466
ZNF423Q2M1K92EBI-355676,EBI-950016

Protein-protein interaction databases

BioGridi106652. 197 interactions.
DIPiDIP-38N.
IntActiP09874. 65 interactions.
MINTiMINT-104344.
STRINGi9606.ENSP00000355759.

Structurei

Secondary structure

1
1014
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni2 – 54Combined sources
Beta strandi8 – 136Combined sources
Beta strandi15 – 173Combined sources
Turni22 – 243Combined sources
Beta strandi25 – 273Combined sources
Beta strandi32 – 409Combined sources
Beta strandi42 – 5312Combined sources
Helixi54 – 596Combined sources
Helixi67 – 704Combined sources
Helixi74 – 763Combined sources
Helixi79 – 9012Combined sources
Beta strandi113 – 1175Combined sources
Beta strandi119 – 1213Combined sources
Turni126 – 1283Combined sources
Beta strandi137 – 1459Combined sources
Beta strandi148 – 15811Combined sources
Helixi160 – 1656Combined sources
Helixi167 – 1704Combined sources
Turni174 – 1763Combined sources
Helixi177 – 1804Combined sources
Helixi184 – 1863Combined sources
Helixi189 – 19810Combined sources
Helixi226 – 25530Combined sources
Helixi258 – 26710Combined sources
Turni273 – 2753Combined sources
Helixi276 – 28914Combined sources
Turni296 – 2983Combined sources
Beta strandi302 – 3054Combined sources
Beta strandi308 – 3114Combined sources
Beta strandi314 – 3163Combined sources
Beta strandi324 – 3274Combined sources
Helixi337 – 3404Combined sources
Helixi342 – 3476Combined sources
Beta strandi389 – 3924Combined sources
Beta strandi394 – 3974Combined sources
Helixi405 – 41410Combined sources
Beta strandi418 – 4214Combined sources
Beta strandi427 – 4304Combined sources
Helixi433 – 4386Combined sources
Helixi441 – 4488Combined sources
Helixi457 – 4637Combined sources
Helixi469 – 4757Combined sources
Helixi535 – 5373Combined sources
Turni540 – 5423Combined sources
Beta strandi543 – 5453Combined sources
Beta strandi551 – 56010Combined sources
Turni562 – 5643Combined sources
Beta strandi567 – 5737Combined sources
Turni578 – 5814Combined sources
Beta strandi585 – 5917Combined sources
Beta strandi597 – 6026Combined sources
Helixi608 – 62215Combined sources
Beta strandi639 – 6413Combined sources
Helixi667 – 67610Combined sources
Helixi679 – 68810Combined sources
Turni693 – 6953Combined sources
Helixi698 – 7003Combined sources
Helixi703 – 72119Combined sources
Helixi726 – 73914Combined sources
Beta strandi745 – 7473Combined sources
Beta strandi752 – 7543Combined sources
Helixi755 – 77925Combined sources
Beta strandi785 – 7873Combined sources
Helixi789 – 7968Combined sources
Beta strandi799 – 8035Combined sources
Beta strandi806 – 8083Combined sources
Helixi809 – 82012Combined sources
Helixi824 – 8263Combined sources
Beta strandi829 – 84113Combined sources
Helixi844 – 8485Combined sources
Helixi849 – 8513Combined sources
Beta strandi855 – 86410Combined sources
Helixi866 – 8683Combined sources
Helixi869 – 8757Combined sources
Beta strandi882 – 8843Combined sources
Helixi886 – 8883Combined sources
Beta strandi889 – 8913Combined sources
Beta strandi893 – 9008Combined sources
Helixi901 – 9055Combined sources
Helixi906 – 9083Combined sources
Beta strandi912 – 9143Combined sources
Beta strandi916 – 92510Combined sources
Beta strandi928 – 9347Combined sources
Beta strandi947 – 9504Combined sources
Beta strandi952 – 9565Combined sources
Helixi958 – 9603Combined sources
Beta strandi962 – 9643Combined sources
Beta strandi967 – 9693Combined sources
Beta strandi974 – 9763Combined sources
Beta strandi983 – 9864Combined sources
Beta strandi988 – 9925Combined sources
Helixi994 – 9963Combined sources
Beta strandi997 – 100913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
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[»]
ProteinModelPortaliP09874.
SMRiP09874. Positions 5-94, 105-359, 381-489, 520-1011.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09874.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini385 – 47692BRCTPROSITE-ProRule annotationAdd
BLAST
Domaini662 – 779118PARP alpha-helicalPROSITE-ProRule annotationAdd
BLAST
Domaini788 – 1014227PARP catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni373 – 524152Automodification domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi207 – 2093Nuclear localization signal1 Publication
Motifi221 – 2266Nuclear localization signal1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri9 – 9385PARP-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri113 – 20391PARP-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG243963.
GeneTreeiENSGT00390000017341.
HOGENOMiHOG000030402.
HOVERGENiHBG053513.
InParanoidiP09874.
KOiK10798.
OMAiITAWTKC.
OrthoDBiEOG7KM5S0.
PhylomeDBiP09874.
TreeFamiTF316616.

Family and domain databases

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.
IPR008288. NAD_ADPRT.
IPR012982. PADR1.
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.
SM00773. WGR. 1 hit.
[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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171G → E in AAB59447. (PubMed:2824474)Curated
Sequence conflicti70 – 701E → Q in AAA60137. (PubMed:3120710)Curated
Sequence conflicti212 – 2121E → K in AAB59447. (PubMed:2824474)Curated
Sequence conflicti613 – 6131H → Q in AAA60155. (PubMed:2891139)Curated
Sequence conflicti827 – 8271N → S in AAA60155. (PubMed:2891139)Curated
Sequence conflicti908 – 9081C → Y in AAA60155. (PubMed:2891139)Curated
Sequence conflicti980 – 9801N → I in AAA60155. (PubMed:2891139)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541F → L.
Corresponds to variant rs3738708 [ dbSNP | Ensembl ].
VAR_050460
Natural varianti188 – 1881A → T.1 Publication
Corresponds to variant rs1805409 [ dbSNP | Ensembl ].
VAR_014714
Natural varianti334 – 3341V → I.1 Publication
Corresponds to variant rs3219057 [ dbSNP | Ensembl ].
VAR_019171
Natural varianti377 – 3771P → S.
Corresponds to variant rs2230484 [ dbSNP | Ensembl ].
VAR_050461
Natural varianti383 – 3831S → Y.1 Publication
Corresponds to variant rs3219062 [ dbSNP | Ensembl ].
VAR_019172
Natural varianti488 – 4881E → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_035852
Natural varianti762 – 7621V → A.2 Publications
Corresponds to variant rs1136410 [ dbSNP | Ensembl ].
VAR_014715
Natural varianti940 – 9401K → R.2 Publications
Corresponds to variant rs3219145 [ dbSNP | Ensembl ].
VAR_019173

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.4. human.

Polymorphism databases

DMDMi130781.

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.
CCDSi CCDS1554.1.
PIRi A29725.
RefSeqi NP_001609.2. NM_001618.3.
UniGenei Hs.177766.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UK0 X-ray 3.00 A/B 662-1011 [» ]
1UK1 X-ray 3.00 A/B 662-1011 [» ]
1WOK X-ray 3.00 A/B/C/D 662-1011 [» ]
2COK NMR - A 387-486 [» ]
2CR9 NMR - A 518-643 [» ]
2CS2 NMR - A 103-223 [» ]
2DMJ NMR - A 1-93 [» ]
2JVN NMR - A 233-358 [» ]
2L30 NMR - A 1-108 [» ]
2L31 NMR - A 103-214 [» ]
2RCW X-ray 2.80 A 662-1011 [» ]
2RD6 X-ray 2.30 A 662-1011 [» ]
2RIQ X-ray 1.70 A 216-366 [» ]
3GJW X-ray 2.30 A 662-1011 [» ]
3GN7 X-ray 2.50 A 662-1011 [» ]
3L3L X-ray 2.50 A 662-1011 [» ]
3L3M X-ray 2.50 A 662-1011 [» ]
3OD8 X-ray 2.40 A/B/C/D/E/F/G/H 2-96 [» ]
3ODA X-ray 2.64 A/B/C/D/E/F/G/H 2-96 [» ]
3ODC X-ray 2.80 A/B 105-206 [» ]
3ODE X-ray 2.95 A/B 105-206 [» ]
4AV1 X-ray 3.10 A/B/C/D 5-202 [» ]
4DQY X-ray 3.25 A/D 1-96 [» ]
B/E 216-366 [» ]
C/F 518-1014 [» ]
4GV7 X-ray 2.89 A/B/C/D 662-1011 [» ]
4HHY X-ray 2.36 A/B/C/D 660-1011 [» ]
4HHZ X-ray 2.72 A/B/C/D 660-1011 [» ]
4L6S X-ray 2.20 A/B 662-1011 [» ]
4OPX X-ray 3.31 A/D 1-97 [» ]
A/D 207-366 [» ]
C/F 518-1014 [» ]
4OQA X-ray 3.65 A/D 1-97 [» ]
A/D 207-366 [» ]
C/F 518-1014 [» ]
4OQB X-ray 3.36 A/D 1-97 [» ]
A/D 207-366 [» ]
C/F 518-1014 [» ]
4PJT X-ray 2.35 A/B/C/D 662-1011 [» ]
ProteinModelPortali P09874.
SMRi P09874. Positions 5-94, 105-359, 381-489, 520-1011.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106652. 197 interactions.
DIPi DIP-38N.
IntActi P09874. 65 interactions.
MINTi MINT-104344.
STRINGi 9606.ENSP00000355759.

Chemistry

BindingDBi P09874.
ChEMBLi CHEMBL3105.
GuidetoPHARMACOLOGYi 2771.

PTM databases

PhosphoSitei P09874.

Polymorphism databases

DMDMi 130781.

2D gel databases

SWISS-2DPAGE P09874.

Proteomic databases

MaxQBi P09874.
PaxDbi P09874.
PeptideAtlasi P09874.
PRIDEi P09874.

Protocols and materials databases

DNASUi 142.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366794 ; ENSP00000355759 ; ENSG00000143799 .
GeneIDi 142.
KEGGi hsa:142.
UCSCi uc001hqd.4. human.

Organism-specific databases

CTDi 142.
GeneCardsi GC01M226548.
H-InvDB HIX0023551.
HGNCi HGNC:270. PARP1.
HPAi CAB000147.
CAB003839.
CAB003840.
HPA045168.
MIMi 173870. gene.
neXtProti NX_P09874.
PharmGKBi PA32.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG243963.
GeneTreei ENSGT00390000017341.
HOGENOMi HOG000030402.
HOVERGENi HBG053513.
InParanoidi P09874.
KOi K10798.
OMAi ITAWTKC.
OrthoDBi EOG7KM5S0.
PhylomeDBi P09874.
TreeFami TF316616.

Enzyme and pathway databases

BRENDAi 2.4.2.30. 2681.
Reactomei REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
SignaLinki P09874.

Miscellaneous databases

ChiTaRSi PARP1. human.
EvolutionaryTracei P09874.
GeneWikii PARP1.
GenomeRNAii 142.
NextBioi 565.
PMAP-CutDB P09874.
PROi P09874.
SOURCEi Search...

Gene expression databases

Bgeei P09874.
CleanExi HS_PARP1.
ExpressionAtlasi P09874. baseline and differential.
Genevestigatori P09874.

Family and domain databases

Gene3Di 1.20.142.10. 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.
InterProi IPR001357. BRCT_dom.
IPR008288. NAD_ADPRT.
IPR012982. PADR1.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
IPR001510. Znf_PARP.
[Graphical view ]
Pfami 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.
[Graphical view ]
PIRSFi PIRSF000489. NAD_ADPRT. 1 hit.
SMARTi SM00292. BRCT. 1 hit.
SM00773. WGR. 1 hit.
[Graphical view ]
SUPFAMi SSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of a full-length cDNA for human fibroblast poly(ADP-ribose) polymerase."
    Uchida K., Morita T., Sato T., Ogura T., Yamashita R., Noguchi S., Suzuki H., Nyunoya H., Miwa M., Sugimura T.
    Biochem. Biophys. Res. Commun. 148:617-622(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fibroblast.
  2. "Primary structure of human poly(ADP-ribose) synthetase as deduced from cDNA sequence."
    Kurosaki T., Ushiro H., Mitsuuchi Y., Suzuki S., Matsuda M., Matsuda Y., Katunuma N., Kangawa K., Matsuo H., Hirose T., Inayama S., Shizuta Y.
    J. Biol. Chem. 262:15990-15997(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fibroblast.
  3. "cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase."
    Cherney B.W., McBride O.W., Chen D., Alkhatib H., Bhatia K., Hensley P., Smulson M.E.
    Proc. Natl. Acad. Sci. U.S.A. 84:8370-8374(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-940.
  4. "Human nuclear NAD+ ADP-ribosyltransferase(polymerizing): organization of the gene."
    Auer B., Nagl U., Herzog H., Schneider R., Schweiger M.
    DNA 8:575-580(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. NIEHS SNPs program
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-188; ILE-334; TYR-383; ALA-762 AND ARG-940.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-762.
    Tissue: Brain.
  9. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
  10. "Characterization of a putative promoter region of the human poly(ADP-ribose) polymerase gene: structural similarity to that of the DNA polymerase beta gene."
    Ogura T., Nyunoya H., Takahashi-Masutani M., Miwa M., Sugimura T., Esumi H.
    Biochem. Biophys. Res. Commun. 167:701-710(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
  11. "Human pADPRT is involved in the regulation of its own gene."
    Herzog H., Schneider R., Hirsch-Kauffmann M., Schnitzer D., Schweiger M.
    Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
  12. Cited for: PROTEIN SEQUENCE OF 2-10; 35-47; 66-78; 109-119; 183-197; 209-221; 263-282; 453-467; 487-496; 529-548; 552-564; 572-582; 637-654; 668-695; 748-761; 780-796; 803-816 AND 859-903, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma and Ovarian carcinoma.
  13. "Txk, a member of the non-receptor tyrosine kinase of the Tec family, forms a complex with poly(ADP-ribose) polymerase 1 and elongation factor 1alpha and regulates interferon-gamma gene transcription in Th1 cells."
    Maruyama T., Nara K., Yoshikawa H., Suzuki N.
    Clin. Exp. Immunol. 147:164-175(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 166-177 AND 356-367, INTERACTION WITH EEF1A1 AND TXK, PHOSPHORYLATION BY TXK, SUBCELLULAR LOCATION, FUNCTION AS A TRANSCRIPTION FACTOR.
  14. "Isolation of a cDNA clone for human NAD+: protein ADP-ribosyltransferase."
    Schneider R., Auer B., Kuhne C., Herzog H., Klocker H., Burtscher H.J., Hirsch-Kauffmann M., Wintersberger U., Schweiger M.
    Eur. J. Cell Biol. 44:302-307(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 381-420 AND 682-710.
  15. "Molecular cloning of cDNA for human poly(ADP-ribose) polymerase and expression of its gene during HL-60 cell differentiation."
    Suzuki H., Uchida K., Shima H., Sato T., Okamoto T., Kimura T., Miwa M.
    Biochem. Biophys. Res. Commun. 146:403-409(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 441-1014.
  16. Erratum
    Suzuki H., Uchida K., Shima H., Sato T., Okamoto T., Kimura T., Miwa M.
    Biochem. Biophys. Res. Commun. 148:1549-1550(1987)
  17. "The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA."
    Gradwohl G., Menissier-de Murcia J., Molinete M., Simonin F., Koken M.H.M., Hoeijmakers J.H.J., de Murcia G.M.
    Proc. Natl. Acad. Sci. U.S.A. 87:2990-2994(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: ANALYSIS OF ZINC-FINGERS.
  18. "The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA."
    Ikelima M., Noguchi S., Yamashita R., Ogura T., Sugimura T., Gill D.M., Miwa M.
    J. Biol. Chem. 265:21907-21913(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: ANALYSIS OF ZINC-FINGERS.
  19. "Expression and site-directed mutagenesis of the catalytic domain of human poly(ADP-ribose)polymerase in Escherichia coli. Lysine 893 is critical for activity."
    Simonin F., Menissier-de Murcia J., Poch O., Muller S., Gradwohl G., Molinete M., Penning C., Keith G., de Murcia G.M.
    J. Biol. Chem. 265:19249-19256(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CATALYTIC DOMAIN.
  20. "The human poly(ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity."
    Schreiber V., Molinete M., Boeuf H., de Murcia G.M., Menissier-de Murcia J.
    EMBO J. 11:3263-3269(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEAR LOCALIZATION SIGNAL.
  21. "Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching."
    Rolli V., O'Farrell M., Menissier-de Murcia J., de Murcia G.M.
    Biochemistry 36:12147-12154(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CATALYTIC DOMAIN.
  22. "Functional association of poly(ADP-ribose) polymerase with DNA polymerase alpha-primase complex: a link between DNA strand break detection and DNA replication."
    Dantzer F., Nasheuer H.P., Vonesch J.L., de Murcia G., Menissier-de Murcia J.
    Nucleic Acids Res. 26:1891-1898(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POLA1.
  23. "Suppression of the poly(ADP-ribose) polymerase activity by DNA-dependent protein kinase in vitro."
    Ariumi Y., Masutani M., Copeland T.D., Mimori T., Sugimura T., Shimotohno K., Ueda K., Hatanaka M., Noda M.
    Oncogene 18:4616-4625(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  24. Cited for: INTERACTION WITH APTX.
  25. "The poly(ADP-ribose) polymerase 1 interacts with Sry and modulates its biological functions."
    Li Y., Oh H.J., Lau Y.-F.C.
    Mol. Cell. Endocrinol. 257:35-46(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRY.
  26. "A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses."
    Kanno S., Kuzuoka H., Sasao S., Hong Z., Lan L., Nakajima S., Yasui A.
    EMBO J. 26:2094-2103(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APLF.
  27. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  28. "Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins."
    Ahel I., Ahel D., Matsusaka T., Clark A.J., Pines J., Boulton S.J., West S.C.
    Nature 451:81-85(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  29. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-368 AND SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. "Poly(ADP-ribose) polymerase-1 (PARP-1) transcriptionally regulates angiotensin AT2 receptor (AT2R) and AT2R binding protein (ATBP) genes."
    Reinemund J., Seidel K., Steckelings U.M., Zaade D., Klare S., Rompe F., Katerbaum M., Schacherl J., Li Y., Menk M., Schefe J.H., Goldin-Lang P., Szabo C., Olah G., Unger T., Funke-Kaiser H.
    Biochem. Pharmacol. 77:1795-1805(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  31. "PARP-1 transcriptional activity is regulated by sumoylation upon heat shock."
    Martin N., Schwamborn K., Schreiber V., Werner A., Guillier C., Zhang X.D., Bischof O., Seeler J.S., Dejean A.
    EMBO J. 28:3534-3548(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF4.
  32. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  33. "Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1."
    Ahel D., Horejsi Z., Wiechens N., Polo S.E., Garcia-Wilson E., Ahel I., Flynn H., Skehel M., West S.C., Jackson S.P., Owen-Hughes T., Boulton S.J.
    Science 325:1240-1243(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, POLY-ADP-RIBOSYLATION, INTERACTION WITH CHD1L.
  34. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-97; LYS-105; LYS-131; LYS-600 AND LYS-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  36. "Toward a unified nomenclature for mammalian ADP-ribosyltransferases."
    Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.
    Trends Biochem. Sci. 35:208-219(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  37. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  38. "Poly(ADP-ribose)-dependent regulation of Snail1 protein stability."
    Rodriguez M.I., Gonzalez-Flores A., Dantzer F., Collard J., de Herreros A.G., Oliver F.J.
    Oncogene 30:4365-4372(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNAI1.
  39. Cited for: INTERACTION WITH RNF146, SUBCELLULAR LOCATION.
  40. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  41. "Exome capture reveals ZNF423 and CEP164 mutations, linking renal ciliopathies to DNA damage response signaling."
    Chaki M., Airik R., Ghosh A.K., Giles R.H., Chen R., Slaats G.G., Wang H., Hurd T.W., Zhou W., Cluckey A., Gee H.Y., Ramaswami G., Hong C.J., Hamilton B.A., Cervenka I., Ganji R.S., Bryja V., Arts H.H.
    , van Reeuwijk J., Oud M.M., Letteboer S.J., Roepman R., Husson H., Ibraghimov-Beskrovnaya O., Yasunaga T., Walz G., Eley L., Sayer J.A., Schermer B., Liebau M.C., Benzing T., Le Corre S., Drummond I., Janssen S., Allen S.J., Natarajan S., O'Toole J.F., Attanasio M., Saunier S., Antignac C., Koenekoop R.K., Ren H., Lopez I., Nayir A., Stoetzel C., Dollfus H., Massoudi R., Gleeson J.G., Andreoli S.P., Doherty D.G., Lindstrad A., Golzio C., Katsanis N., Pape L., Abboud E.B., Al-Rajhi A.A., Lewis R.A., Omran H., Lee E.Y., Wang S., Sekiguchi J.M., Saunders R., Johnson C.A., Garner E., Vanselow K., Andersen J.S., Shlomai J., Nurnberg G., Nurnberg P., Levy S., Smogorzewska A., Otto E.A., Hildebrandt F.
    Cell 150:533-548(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZNF423.
  42. "Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
    Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
    Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  43. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  44. "BAL1 and its partner E3 ligase, BBAP, link Poly(ADP-ribose) activation, ubiquitylation, and double-strand DNA repair independent of ATM, MDC1, and RNF8."
    Yan Q., Xu R., Zhu L., Cheng X., Wang Z., Manis J., Shipp M.A.
    Mol. Cell. Biol. 33:845-857(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PARP9.
  45. "Solution structure of the first ZF-PARP domain, of the BRCT domain and of the WGR domain of human poly(ADP-ribose)polymerase-1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-93 AND 385-643.
  46. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-488.

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 26, 2014
This is version 190 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

External Data

Dasty 3