P09874 (PARP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Poly [ADP-ribose] polymerase 1
Short name=PARP-1
EC=2.4.2.30

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 names

Name:	PARP1
Synonyms:	ADPRT, PPOL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1014 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 recruitement 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. Ref.13 Ref.28 Ref.30 Ref.33 Ref.43
Catalytic activity	NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor. Ref.28
Subunit structure	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. Ref.13 Ref.22 Ref.24 Ref.25 Ref.26 Ref.31 Ref.33 Ref.38 Ref.39 Ref.41 Ref.43
Subcellular location	Nucleus. Nucleus › nucleolus. Note: Localizes at sites of DNA damage. Ref.13 Ref.39 Ref.42 Ref.43
Post-translational modification	Phosphorylated by PRKDC and TXK. Ref.13 Ref.23 Poly-ADP-ribosylated by PARP2. Poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites. Ref.33 S-nitrosylated, leading to inhibit transcription regulation activity By similarity.
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.
Sequence similarities	Contains 1 BRCT domain. Contains 1 PARP alpha-helical domain. Contains 1 PARP catalytic domain. Contains 2 PARP-type zinc fingers.

Ontologies

Keywords
Biological process	DNA damage DNA repair Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding NAD Zinc
Molecular function	Glycosyltransferase Transferase
PTM	ADP-ribosylation Acetylation Phosphoprotein S-nitrosylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, detection of DNA damage Inferred from electronic annotation. Source: Compara base-excision repair Inferred from electronic annotation. Source: Compara cellular response to insulin stimulus Inferred from direct assay PubMed 19303849. Source: BHF-UCL double-strand break repair Inferred from mutant phenotype Ref.43. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: Reactome protein autoprocessing Inferred from electronic annotation. Source: Compara protein poly-ADP-ribosylation Inferred from direct assay PubMed 15674325. Source: UniProtKB regulation of growth rate Inferred from electronic annotation. Source: Compara telomere maintenance Inferred from electronic annotation. Source: Compara transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome
Cellular_component	nuclear envelope Inferred from direct assay Ref.22. Source: UniProtKB nucleolus Inferred from direct assay PubMed 16107709Ref.22. Source: UniProtKB transcription factor complex Inferred from direct assay PubMed 19303849. Source: BHF-UCL
Molecular_function	DNA binding Traceable author statement Ref.4. Source: ProtInc NAD binding Inferred from electronic annotation. Source: Compara NAD+ ADP-ribosyltransferase activity Inferred from direct assay PubMed 16107709Ref.26. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APTX	Q7Z2E3	7	EBI-355676,EBI-847814
CEBPA	P49715	2	EBI-355676,EBI-1172054
E2F1	Q01094	2	EBI-355676,EBI-448924
ERG	P11308	7	EBI-355676,EBI-79704
SNAI1	O95863	10	EBI-355676,EBI-1045459
Snai1	Q02085	3	EBI-355676,EBI-6049807	From a different organism.
TP53	P04637	3	EBI-355676,EBI-366083
WRN	Q14191	6	EBI-355676,EBI-368417
ZNF423	Q2M1K9	2	EBI-355676,EBI-950016

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.12

Chain

2 – 1014

1013

Poly [ADP-ribose] polymerase 1

PRO_0000211320

Regions

Domain

385 – 476

92

BRCT

Domain

662 – 779

118

PARP alpha-helical

Domain

788 – 1014

227

PARP catalytic

DNA binding

2 – 372

371

Zinc finger

9 – 93

85

PARP-type 1

Zinc finger

113 – 203

91

PARP-type 2

Region

373 – 524

152

Automodification domain

Motif

207 – 209

3

Nuclear localization signal Ref.20

Motif

221 – 226

6

Nuclear localization signal Ref.20

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.12

Modified residue

41

1

Phosphoserine Ref.35

Modified residue

97

1

N6-acetyllysine Ref.34

Modified residue

105

1

N6-acetyllysine Ref.34

Modified residue

131

1

N6-acetyllysine Ref.34

Modified residue

179

1

Phosphoserine Ref.27

Modified residue

368

1

Phosphothreonine Ref.29

Modified residue

407

1

PolyADP-ribosyl glutamic acid Potential

Modified residue

413

1

PolyADP-ribosyl glutamic acid Potential

Modified residue

435

1

PolyADP-ribosyl glutamic acid Potential

Modified residue

437

1

PolyADP-ribosyl glutamic acid Potential

Modified residue

444

1

PolyADP-ribosyl glutamic acid Potential

Modified residue

445

1

PolyADP-ribosyl glutamic acid Potential

Modified residue

448

1

PolyADP-ribosyl glutamic acid Potential

Modified residue

456

1

PolyADP-ribosyl glutamic acid Potential

Modified residue

471

1

PolyADP-ribosyl glutamic acid Potential

Modified residue

484

1

PolyADP-ribosyl glutamic acid Potential

Modified residue

488

1

PolyADP-ribosyl glutamic acid Potential

Modified residue

491

1

PolyADP-ribosyl glutamic acid Potential

Modified residue

513

1

PolyADP-ribosyl glutamic acid Potential

Modified residue

514

1

PolyADP-ribosyl glutamic acid Potential

Modified residue

520

1

PolyADP-ribosyl glutamic acid Potential

Modified residue

600

1

N6-acetyllysine Ref.34

Modified residue

621

1

N6-acetyllysine Ref.34

Modified residue

782

1

Phosphoserine Ref.29 Ref.32 Ref.35 Ref.40

Natural variations

Natural variant

54

1

F → L.
Corresponds to variant rs3738708 [ dbSNP | Ensembl ].

VAR_050460

Natural variant

188

1

A → T. Ref.5
Corresponds to variant rs1805409 [ dbSNP | Ensembl ].

VAR_014714

Natural variant

334

1

V → I. Ref.5
Corresponds to variant rs3219057 [ dbSNP | Ensembl ].

VAR_019171

Natural variant

377

1

P → S.
Corresponds to variant rs2230484 [ dbSNP | Ensembl ].

VAR_050461

Natural variant

383

1

S → Y. Ref.5
Corresponds to variant rs3219062 [ dbSNP | Ensembl ].

VAR_019172

Natural variant

488

1

E → V in a breast cancer sample; somatic mutation. Ref.45

VAR_035852

Natural variant

762

1

V → A. Ref.5 Ref.8
Corresponds to variant rs1136410 [ dbSNP | Ensembl ].

VAR_014715

Natural variant

940

1

K → R. Ref.3 Ref.5
Corresponds to variant rs3219145 [ dbSNP | Ensembl ].

VAR_019173

Experimental info

Mutagenesis

797

1

L → P: 1.5% of wild-type activity. Ref.19 Ref.21

Mutagenesis

868

1

N → S: 4% of wild-type activity. Ref.19 Ref.21

Mutagenesis

890

1

M → V: <0.5% of wild-type activity. Ref.19 Ref.21

Mutagenesis

893

1

K → I: Abolishes enzymatic activity. Ref.19 Ref.21

Mutagenesis

897

1

F → S: 10% of wild-type activity. Ref.19 Ref.21

Mutagenesis

899

1

D → N: 0.6% of wild-type activity. Ref.19 Ref.21

Mutagenesis

908

1

C → R: <0.5% of wild-type activity. Ref.19 Ref.21

Mutagenesis

926

1

L → F: 1.5% of wild-type activity. Ref.19 Ref.21

Mutagenesis

986

1

Y → H: 14% of wild-type activity and increased branching 15-fold. Ref.19 Ref.21

Mutagenesis

988

1

E → K: 1.25% of wild-type activity; only monomers are added. Ref.19 Ref.21

Mutagenesis

1003

1

L → P: 1.5% of wild-type activity. Ref.19 Ref.21

Sequence conflict

17

1

G → E in AAB59447. Ref.2

Sequence conflict

70

1

E → Q in AAA60137. Ref.1

Sequence conflict

212

1

E → K in AAB59447. Ref.2

Sequence conflict

613

1

H → Q in AAA60155. Ref.3

Sequence conflict

827

1

N → S in AAA60155. Ref.3

Sequence conflict

908

1

C → Y in AAA60155. Ref.3

Sequence conflict

980

1

N → I in AAA60155. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1014

Helix Strand Turn

Details...

Turn

2 – 5

4

Beta strand

8 – 13

6

Beta strand

15 – 17

3

Turn

22 – 24

3

Beta strand

25 – 27

3

Beta strand

32 – 40

9

Beta strand

42 – 53

12

Helix

54 – 59

6

Helix

67 – 70

4

Helix

74 – 76

3

Helix

79 – 90

12

Beta strand

113 – 117

5

Beta strand

119 – 121

3

Turn

126 – 128

3

Beta strand

137 – 145

9

Beta strand

148 – 158

11

Helix

160 – 165

6

Helix

167 – 170

4

Turn

174 – 176

3

Helix

177 – 180

4

Helix

184 – 186

3

Helix

189 – 198

10

Turn

204 – 206

3

Helix

226 – 255

30

Helix

258 – 267

10

Turn

273 – 275

3

Helix

276 – 289

14

Turn

296 – 298

3

Beta strand

302 – 305

4

Beta strand

308 – 311

4

Beta strand

314 – 316

3

Beta strand

324 – 327

4

Helix

337 – 340

4

Helix

342 – 347

6

Beta strand

389 – 392

4

Beta strand

394 – 397

4

Helix

405 – 414

10

Beta strand

418 – 421

4

Beta strand

427 – 430

4

Helix

433 – 438

6

Helix

441 – 448

8

Helix

457 – 463

7

Helix

469 – 475

7

Turn

535 – 538

4

Turn

540 – 542

3

Beta strand

543 – 545

3

Beta strand

554 – 560

7

Beta strand

562 – 564

3

Beta strand

567 – 577

11

Turn

578 – 581

4

Beta strand

582 – 589

8

Beta strand

591 – 595

5

Beta strand

598 – 606

9

Helix

607 – 621

15

Beta strand

622 – 624

3

Beta strand

639 – 642

4

Helix

667 – 676

10

Helix

679 – 688

10

Turn

693 – 695

3

Helix

698 – 700

3

Helix

703 – 722

20

Helix

728 – 739

12

Beta strand

745 – 747

3

Beta strand

752 – 754

3

Helix

755 – 777

23

Turn

778 – 781

4

Beta strand

785 – 787

3

Helix

789 – 796

8

Beta strand

799 – 803

5

Beta strand

806 – 808

3

Helix

809 – 820

12

Beta strand

824 – 826

3

Beta strand

828 – 841

14

Turn

842 – 850

9

Helix

851 – 853

3

Beta strand

857 – 864

8

Helix

866 – 868

3

Helix

869 – 875

7

Beta strand

882 – 884

3

Helix

886 – 888

3

Beta strand

889 – 891

3

Beta strand

892 – 900

9

Helix

901 – 905

5

Helix

906 – 908

3

Beta strand

912 – 914

3

Beta strand

916 – 925

10

Beta strand

928 – 934

7

Beta strand

947 – 950

4

Beta strand

953 – 956

4

Helix

958 – 960

3

Beta strand

962 – 964

3

Beta strand

967 – 969

3

Beta strand

974 – 976

3

Beta strand

981 – 986

6

Beta strand

988 – 992

5

Helix

994 – 996

3

Beta strand

997 – 1009

13

Sequences

	Sequence		Length	Mass (Da)
	P09874 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 6A5FC01EB91C046B	FASTA	1,014	113,084
	10 20 30 40 50 60 MAESSDKLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH WYHFSCFWKV 70 80 90 100 110 120 GHSIRHPDVE VDGFSELRWD DQQKVKKTAE AGGVTGKGQD GIGSKAEKTL GDFAAEYAKS 130 140 150 160 170 180 NRSTCKGCME KIEKGQVRLS KKMVDPEKPQ LGMIDRWYHP GCFVKNREEL GFRPEYSASQ 190 200 210 220 230 240 LKGFSLLATE DKEALKKQLP GVKSEGKRKG DEVDGVDEVA KKKSKKEKDK DSKLEKALKA 250 260 270 280 290 300 QNDLIWNIKD ELKKVCSTND LKELLIFNKQ QVPSGESAIL DRVADGMVFG ALLPCEECSG 310 320 330 340 350 360 QLVFKSDAYY CTGDVTAWTK CMVKTQTPNR KEWVTPKEFR EISYLKKLKV KKQDRIFPPE 370 380 390 400 410 420 TSASVAATPP PSTASAPAAV NSSASADKPL SNMKILTLGK LSRNKDEVKA MIEKLGGKLT 430 440 450 460 470 480 GTANKASLCI STKKEVEKMN KKMEEVKEAN IRVVSEDFLQ DVSASTKSLQ ELFLAHILSP 490 500 510 520 530 540 WGAEVKAEPV EVVAPRGKSG AALSKKSKGQ VKEEGINKSE KRMKLTLKGG AAVDPDSGLE 550 560 570 580 590 600 HSAHVLEKGG KVFSATLGLV DIVKGTNSYY KLQLLEDDKE NRYWIFRSWG RVGTVIGSNK 610 620 630 640 650 660 LEQMPSKEDA IEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE AVKKLTVNPG 670 680 690 700 710 720 TKSKLPKPVQ DLIKMIFDVE SMKKAMVEYE IDLQKMPLGK LSKRQIQAAY SILSEVQQAV 730 740 750 760 770 780 SQGSSDSQIL DLSNRFYTLI PHDFGMKKPP LLNNADSVQA KVEMLDNLLD IEVAYSLLRG 790 800 810 820 830 840 GSDDSSKDPI DVNYEKLKTD IKVVDRDSEE AEIIRKYVKN THATTHNAYD LEVIDIFKIE 850 860 870 880 890 900 REGECQRYKP FKQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM 910 920 930 940 950 960 VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG LGKTTPDPSA 970 980 990 1000 1010 NISLDGVDVP LGTGISSGVN DTSLLYNEYI VYDIAQVNLK YLLKLKFNFK TSLW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"Human poly(ADP-ribose) polymerase gene. Cloning of the promoter region." Yokoyama Y., Kawamoto T., Mitsuuchi Y., Kurosaki T., Toda K., Ushiro H., Terashima M., Sumimoto H., Kuribayashi I., Yamamoto Y., Maeda T., Ikeda H., Sagara Y., Shizuta Y. Eur. J. Biochem. 194:521-526(1990) [PubMed] [Europe PMC] [Abstract] 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]	Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB 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, 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]	"Aprataxin, a novel protein that protects against genotoxic stress." Gueven N., Becherel O.J., Kijas A.W., Chen P., Howe O., Rudolph J.H., Gatti R., Date H., Onodera O., Taucher-Scholz G., Lavin M.F. Hum. Mol. Genet. 13:1081-1093(2004) [PubMed] [Europe PMC] [Abstract] 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]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, MASS SPECTROMETRY. 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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-368 AND SER-782, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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]	"Ubiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt signaling." Callow M.G., Tran H., Phu L., Lau T., Lee J., Sandoval W.N., Liu P.S., Bheddah S., Tao J., Lill J.R., Hongo J.A., Davis D., Kirkpatrick D.S., Polakis P., Costa M. PLoS ONE 6:E22595-E22595(2011) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY.
[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]	"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.
[44]	"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.
[45]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-488.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00449049.

PIR

A29725.

RefSeq

NP_001609.2. NM_001618.3.

UniGene

Hs.177766.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UK0	X-ray	3.00	A/B	662-1010	[»]
1UK1	X-ray	3.00	A/B	662-1010	[»]
1WOK	X-ray	3.00	A/B/C/D	662-1010	[»]
2COK	NMR	-	A	387-486	[»]
2CR9	NMR	-	A	518-643	[»]
2CS2	NMR	-	A	103-224	[»]
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	1-96	[»]
3ODA	X-ray	2.64	A/B/C/D/E/F/G/H	1-96	[»]
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	[»]
4HHY	X-ray	2.36	A/B/C/D	662-1011	[»]
4HHZ	X-ray	2.72	A/B/C/D	662-1011	[»]

ProteinModelPortal

P09874.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38N.

IntAct

P09874. 45 interactions.

MINT

MINT-104344.

STRING

9606.ENSP00000355759.

PTM databases

PhosphoSite

P09874.

Polymorphism databases

DMDM

130781.

2D gel databases

SWISS-2DPAGE

P09874.

Proteomic databases

PaxDb

P09874.

PeptideAtlas

P09874.

PRIDE

P09874.

Protocols and materials databases

DNASU

142.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000366794; ENSP00000355759; ENSG00000143799.

GeneID

142.

KEGG

hsa:142.

UCSC

uc001hqd.4. human.

Organism-specific databases

CTD

142.

GeneCards

GC01M224102.

H-InvDB

HIX0023551.

HGNC

HGNC:270. PARP1.

HPA

CAB000147.
CAB003839.
CAB003840.
HPA045168.

MIM

173870. gene.

neXtProt

NX_P09874.

PharmGKB

PA32.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG243963.

HOGENOM

HOG000030402.

HOVERGEN

HBG053513.

InParanoid

P09874.

KO

K10798.

OMA

SRYWIFR.

OrthoDB

EOG4PG609.

PhylomeDB

P09874.

Enzyme and pathway databases

BRENDA

2.4.2.30. 2681.

Pathway_Interaction_DB

caspase_pathway. Caspase cascade in apoptosis.
faspathway. FAS signaling pathway (CD95).

Reactome

REACT_111102. Signal Transduction.
REACT_71. Gene Expression.

SignaLink

P09874.

Gene expression databases

ArrayExpress

P09874.

Bgee

P09874.

CleanEx

HS_PARP1.

Genevestigator

P09874.

GermOnline

ENSG00000143799. Homo sapiens.

Family and domain databases

Gene3D

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.

InterPro

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]

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.
[Graphical view]

PIRSF

PIRSF000489. NAD_ADPRT. 1 hit.

SMART

SM00292. BRCT. 1 hit.
SM00773. WGR. 1 hit.
[Graphical view]

SUPFAM

SSF52113. BRCT. 1 hit.
SSF47587. PARP_reg. 1 hit.
SSF142921. SSF142921. 1 hit.

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.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P09874.

ChEMBL

CHEMBL3105.

ChiTaRS

PARP1. human.

EvolutionaryTrace

P09874.

GenomeRNAi

142.

NextBio

565.

PMAP-CutDB

P09874.

SOURCE

Search...

Entry information

Entry name

PARP1_HUMAN

Accession

Primary (citable) accession number: P09874
Secondary accession number(s): B1ANJ4, Q8IUZ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 174 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.