Q9UGN5 (PARP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Poly [ADP-ribose] polymerase 2
Short name=PARP-2
Short name=hPARP-2
EC=2.4.2.30

Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 2
Short name=ARTD2
NAD(+) ADP-ribosyltransferase 2
Short name=ADPRT-2
Poly[ADP-ribose] synthase 2
Short name=pADPRT-2

Gene names

Name:	PARP2
Synonyms:	ADPRT2, ADPRTL2

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	583 AA.
Sequence status	Complete.
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.
Catalytic activity	NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
Subunit structure	Component of a base excision repair (BER) complex, containing at least XRCC1, PARP1, POLB and LRIG3. Homo- and heterodimer with PARP1. Ref.10
Subcellular location	Nucleus.
Tissue specificity	Widely expressed, mainly in actively dividing tissues. The highest levels are in the brain, heart, pancreas, skeletal muscle and testis; also detected in kidney, liver, lung, placenta, ovary and spleen; levels are low in leukocytes, colon, small intestine, prostate and thymus.
Post-translational modification	Poly-ADP-ribosylated by PARP1 By similarity.
Sequence similarities	Contains 1 PARP alpha-helical domain. Contains 1 PARP catalytic domain.
Sequence caution	The sequence AAD29857.1 differs from that shown. Reason: Erroneous initiation. The sequence AAL77437.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB41505.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding NAD
Molecular function	Glycosyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Traceable author statement PubMed 7260241. Source: ProtInc base-excision repair Inferred from electronic annotation. Source: Compara protein ADP-ribosylation Traceable author statement PubMed 7260241. Source: ProtInc
Cellular_component	nucleolus Inferred from direct assay PubMed 15615785. Source: MGI nucleoplasm Inferred from direct assay PubMed 15615785. Source: MGI
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW NAD+ ADP-ribosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UGN5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UGN5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     68-80: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 583

583

Poly [ADP-ribose] polymerase 2

PRO_0000211327

Regions

Domain

231 – 348

118

PARP alpha-helical

Domain

356 – 583

228

PARP catalytic

DNA binding

1 – 88

88

Potential

Motif

4 – 7

4

Nuclear localization signal Potential

Motif

35 – 40

6

Nuclear localization signal Potential

Amino acid modifications

Modified residue

37

1

N6-acetyllysine; alternate By similarity

Modified residue

38

1

N6-acetyllysine; alternate By similarity

Modified residue

226

1

Phosphoserine Ref.9

Modified residue

232

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

68 – 80

13

Missing in isoform 2.

VSP_004537

Natural variant

161

1

S → N. Ref.5
Corresponds to variant rs3093905 [ dbSNP | Ensembl ].

VAR_019174

Natural variant

168

1

N → S. Ref.5
Corresponds to variant rs3093906 [ dbSNP | Ensembl ].

VAR_019175

Natural variant

235

1

D → G. Ref.5
Corresponds to variant rs3093921 [ dbSNP | Ensembl ].

VAR_019176

Natural variant

285

1

I → V. Ref.5
Corresponds to variant rs3093925 [ dbSNP | Ensembl ].

VAR_019177

Natural variant

296

1

R → Q. Ref.5
Corresponds to variant rs3093926 [ dbSNP | Ensembl ].

VAR_019178

Natural variant

331

1

I → T.
Corresponds to variant rs2275010 [ dbSNP | Ensembl ].

VAR_050462

Experimental info

Sequence conflict

447

1

P → H in AAD29857. Ref.2

Sequence conflict

481

1

N → H in BAA92017. Ref.4

Secondary structure

1

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583

Helix Strand Turn

Details...

Helix

236 – 245

10

Helix

248 – 257

10

Turn

262 – 264

3

Helix

267 – 269

3

Helix

272 – 290

19

Helix

296 – 308

13

Helix

324 – 347

24

Helix

357 – 364

8

Beta strand

367 – 371

5

Helix

377 – 388

12

Beta strand

398 – 409

12

Helix

412 – 415

4

Beta strand

423 – 429

7

Helix

432 – 434

3

Helix

435 – 441

7

Helix

452 – 454

3

Beta strand

459 – 466

8

Helix

467 – 472

6

Beta strand

478 – 480

3

Beta strand

482 – 491

10

Beta strand

494 – 500

7

Helix

505 – 508

4

Beta strand

514 – 517

4

Beta strand

519 – 523

5

Helix

525 – 527

3

Beta strand

529 – 531

3

Beta strand

534 – 536

3

Beta strand

541 – 543

3

Beta strand

549 – 551

3

Beta strand

554 – 556

3

Beta strand

558 – 563

6

Helix

564 – 566

3

Beta strand

567 – 578

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 26, 2001. Version 2. Checksum: 5B7AE8AE531836AF	FASTA	583	66,206
	10 20 30 40 50 60 MAARRRRSTG GGRARALNES KRVNNGNTAP EDSSPAKKTR RCQRQESKKM PVAGGKANKD 70 80 90 100 110 120 RTEDKQDGMP GRSWASKRVS ESVKALLLKG KAPVDPECTA KVGKAHVYCE GNDVYDVMLN 130 140 150 160 170 180 QTNLQFNNNK YYLIQLLEDD AQRNFSVWMR WGRVGKMGQH SLVACSGNLN KAKEIFQKKF 190 200 210 220 230 240 LDKTKNNWED REKFEKVPGK YDMLQMDYAT NTQDEEETKK EESLKSPLKP ESQLDLRVQE 250 260 270 280 290 300 LIKLICNVQA MEEMMMEMKY NTKKAPLGKL TVAQIKAGYQ SLKKIEDCIR AGQHGRALME 310 320 330 340 350 360 ACNEFYTRIP HDFGLRTPPL IRTQKELSEK IQLLEALGDI EIAIKLVKTE LQSPEHPLDQ 370 380 390 400 410 420 HYRNLHCALR PLDHESYEFK VISQYLQSTH APTHSDYTMT LLDLFEVEKD GEKEAFREDL 430 440 450 460 470 480 HNRMLLWHGS RMSNWVGILS HGLRIAPPEA PITGYMFGKG IYFADMSSKS ANYCFASRLK 490 500 510 520 530 540 NTGLLLLSEV ALGQCNELLE ANPKAEGLLQ GKHSTKGLGK MAPSSAHFVT LNGSTVPLGP 550 560 570 580 ASDTGILNPD GYTLNYNEYI VYNPNQVRMR YLLKVQFNFL QLW
	Isoform 2 [UniParc]. Checksum: 335A5B64E758FDFF	FASTA	570	64,805
	10 20 30 40 50 60 MAARRRRSTG GGRARALNES KRVNNGNTAP EDSSPAKKTR RCQRQESKKM PVAGGKANKD 70 80 90 100 110 120 RTEDKQDESV KALLLKGKAP VDPECTAKVG KAHVYCEGND VYDVMLNQTN LQFNNNKYYL 130 140 150 160 170 180 IQLLEDDAQR NFSVWMRWGR VGKMGQHSLV ACSGNLNKAK EIFQKKFLDK TKNNWEDREK 190 200 210 220 230 240 FEKVPGKYDM LQMDYATNTQ DEEETKKEES LKSPLKPESQ LDLRVQELIK LICNVQAMEE 250 260 270 280 290 300 MMMEMKYNTK KAPLGKLTVA QIKAGYQSLK KIEDCIRAGQ HGRALMEACN EFYTRIPHDF 310 320 330 340 350 360 GLRTPPLIRT QKELSEKIQL LEALGDIEIA IKLVKTELQS PEHPLDQHYR NLHCALRPLD 370 380 390 400 410 420 HESYEFKVIS QYLQSTHAPT HSDYTMTLLD LFEVEKDGEK EAFREDLHNR MLLWHGSRMS 430 440 450 460 470 480 NWVGILSHGL RIAPPEAPIT GYMFGKGIYF ADMSSKSANY CFASRLKNTG LLLLSEVALG 490 500 510 520 530 540 QCNELLEANP KAEGLLQGKH STKGLGKMAP SSAHFVTLNG STVPLGPASD TGILNPDGYT 550 560 570 LNYNEYIVYN PNQVRMRYLL KVQFNFLQLW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PARP-2, a novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase." Ame J.-C., Rolli V., Schreiber V., Niedergang C., Apiou F., Decker P., Muller S., Hoeger T., Menissier-de Murcia J., de Murcia G.M. J. Biol. Chem. 274:17860-17868(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Fetal brain.
[2]	"A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues." Johansson M. Genomics 57:442-445(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-583 (ISOFORM 1). Tissue: Fetal brain.
[3]	"pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans." Berghammer H., Ebner M., Marksteiner R., Auer B. FEBS Lett. 449:259-263(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-583 (ISOFORM 1). Tissue: Fibroblast.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta.
[5]	NIEHS SNPs program Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-161; SER-168; GLY-235; VAL-285 AND GLN-296.
[6]	"Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1." Schreiber V., Ame J.-C., Dolle P., Schultz I., Rinaldi B., Fraulob V., Menissier-de Murcia J., de Murcia G.M. J. Biol. Chem. 277:23028-23036(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PARP1; XRCC1; POLB AND LRIG3.
[7]	"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.
[8]	"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].
[9]	"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-226 AND SER-232, MASS SPECTROMETRY.
[10]	"Crystal structure of the catalytic domain of human PARP2 in complex with PARP inhibitor ABT-888." Karlberg T., Hammarstrom M., Schutz P., Svensson L., Schuler H. Biochemistry 49:1056-1058(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 235-579 IN COMPLEX WITH PARP INHIBITORS, SUBUNIT.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ236912 mRNA. Translation: CAB65088.1.
AF085734 mRNA. Translation: AAD29857.1. Different initiation.
AJ236876 mRNA. Translation: CAB41505.2. Different initiation.
AK001980 mRNA. Translation: BAA92017.1. Different termination.
AF479321 Genomic DNA. Translation: AAL77437.1. Sequence problems.

IPI

IPI00026497.
IPI00220995.

RefSeq

NP_001036083.1. NM_001042618.1.
NP_005475.2. NM_005484.3.

UniGene

Hs.409412.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3KCZ	X-ray	2.00	A/B	235-579	[»]
3KJD	X-ray	1.95	A/B	235-579	[»]

ProteinModelPortal

Q9UGN5.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48934N.

STRING

9606.ENSP00000250416.

PTM databases

PhosphoSite

Q9UGN5.

Polymorphism databases

DMDM

17380230.

Proteomic databases

PaxDb

Q9UGN5.

PRIDE

Q9UGN5.

Protocols and materials databases

DNASU

10038.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000250416; ENSP00000250416; ENSG00000129484.
ENST00000429687; ENSP00000392972; ENSG00000129484.

GeneID

10038.

KEGG

hsa:10038.

UCSC

uc001vxb.1. human.
uc001vxd.3. human.

Organism-specific databases

CTD

10038.

GeneCards

GC14P020811.

HGNC

HGNC:272. PARP2.

HPA

HPA052003.

MIM

607725. gene.

neXtProt

NX_Q9UGN5.

PharmGKB

PA24592.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG243963.

HOGENOM

HOG000173055.

HOVERGEN

HBG053514.

InParanoid

Q9UGN5.

KO

K10798.

OMA

MVEMKYD.

OrthoDB

EOG4Z62N8.

PhylomeDB

Q9UGN5.

Enzyme and pathway databases

BRENDA

2.4.2.30. 2681.

Pathway_Interaction_DB

telomerasepathway. Regulation of Telomerase.

Gene expression databases

ArrayExpress

Q9UGN5.

Bgee

Q9UGN5.

CleanEx

HS_PARP2.

Genevestigator

Q9UGN5.

GermOnline

ENSG00000129484. Homo sapiens.

Family and domain databases

Gene3D

1.20.142.10. 1 hit.
2.20.140.10. 1 hit.

InterPro

IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
[Graphical view]

Pfam

PF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
[Graphical view]

SMART

SM00773. WGR. 1 hit.
[Graphical view]

SUPFAM

SSF47587. PARP_reg. 1 hit.
SSF142921. SSF142921. 1 hit.

PROSITE

PS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9UGN5.

ChEMBL

CHEMBL5366.

ChiTaRS

PARP2. human.

EvolutionaryTrace

Q9UGN5.

GenomeRNAi

10038.

NextBio

37907.

SOURCE

Search...

Entry information

Entry name

PARP2_HUMAN

Accession

Primary (citable) accession number: Q9UGN5
Secondary accession number(s): Q8TEU4 , Q9NUV2, Q9UMR4, Q9Y6C8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	September 26, 2001
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 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.