Reviewed, UniProtKB/Swiss-Prot O88554 (PARP2_MOUSE)

Names and origin

Protein names

Recommended name:
    Poly [ADP-ribose] polymerase 2
      Short name=PARP-2
      Short name=mPARP-2
    EC=2.4.2.30
Alternative name(s):
    NAD(+) ADP-ribosyltransferase 2
      Short name=ADPRT-2
    Poly[ADP-ribose] synthetase 2
      Short name=pADPRT-2

Gene names

Name:	Parp2
Synonyms:	Adprt2, Adprtl2, Aspartl2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	559 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 LIG3. Homo- and heterodimer with PARP1.
Subcellular location	Nucleus.
Tissue specificity	Widely expressed; the highest levels were in testis followed by ovary. Expression is correlated with proliferation, with higher levels occurring during early fetal development and organogenesis and in the highly proliferative cell compartments of adult.
Developmental stage	At stage E12.5, expressed at high level in the developing liver and kidneys. At E18.5, preferentially expressed in the thymus and in regions of the nervous system. Within the developing trunk, preferential expression persisted in the liver and became restricted to the cortical region of the kidney, spleen, adrenal gland, and to stomach and intestinal epithelia. From E14.5 to E18.5, as well as in the adult, expressed at the highest level in thymus. Expression is particularly high in the subcapsular zone of the thymus where immature lymphocytes proliferate.
Induction	By high levels of DNA-damaging agents.
Post-translational modification	Poly-ADP-ribosylated by PARP1. Ref.5 Acetylation reduces DNA binding and enzymatic activity.
Sequence similarities	Contains 1 PARP alpha-helical domain. Contains 1 PARP catalytic domain.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	DNA-binding NAD
Molecular function	Glycosyltransferase Transferase
PTM	ADP-ribosylation Acetylation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	base-excision repair Ref.5 Inferred from mutant phenotype. Source: MGI protein amino acid ADP-ribosylation Inferred from electronic annotation. Source: InterPro
Cellular component	nucleolus Inferred from direct assay. Source: MGI nucleoplasm Inferred from direct assay. Source: MGI
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW NAD+ ADP-ribosyltransferase activity Ref.1 Inferred from direct assay. Source: MGI protein binding Ref.5 Inferred from physical interaction. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 559

559

Poly [ADP-ribose] polymerase 2

PRO_0000211328

Regions

Domain

207 – 324

118

PARP alpha-helical

Domain

332 – 559

228

PARP catalytic

DNA binding

1 – 65

65

Potential

Motif

3 – 9

7

Nuclear localization signal Potential

Motif

33 – 39

7

Nuclear localization signal Potential

Amino acid modifications

Modified residue

36

1

N6-(ADP-ribosyl)lysine; alternate Probable

Modified residue

36

1

N6-acetyllysine; alternate Ref.6

Modified residue

37

1

N6-(ADP-ribosyl)lysine; alternate Probable

Modified residue

37

1

N6-acetyllysine; alternate Ref.6

Experimental info

Mutagenesis

36

1

K → R: Decreases levels of mono-ADP-ribosylation without loss of enzyme activity. Ref.6

Mutagenesis

37

1

K → R: Decreases levels of mono-ADP-ribosylation without loss of enzyme activity. Ref.6

Sequence conflict

82

1

L → V in AAK13253. Ref.2

Sequence conflict

177

1

V → I in AAK13253. Ref.2

Sequence conflict

486

1

R → Q in AAK13253. Ref.2

Secondary structure

1

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559

Helix Strand Turn

Details...

Helix

212 – 222

11

Helix

224 – 232

9

Turn

233 – 235

3

Beta strand

238 – 241

4

Helix

243 – 245

3

Helix

248 – 266

19

Helix

272 – 284

13

Helix

300 – 320

21

Helix

333 – 340

8

Beta strand

343 – 347

5

Helix

353 – 364

12

Beta strand

372 – 385

14

Helix

388 – 391

4

Beta strand

399 – 406

8

Helix

408 – 410

3

Helix

411 – 417

7

Beta strand

424 – 426

3

Helix

428 – 430

3

Beta strand

434 – 441

8

Helix

443 – 447

5

Helix

448 – 450

3

Beta strand

454 – 456

3

Beta strand

458 – 467

10

Beta strand

470 – 476

7

Helix

481 – 484

4

Beta strand

489 – 493

5

Beta strand

496 – 498

3

Helix

501 – 503

3

Beta strand

505 – 507

3

Beta strand

510 – 512

3

Beta strand

525 – 527

3

Beta strand

534 – 538

5

Helix

540 – 542

3

Beta strand

543 – 555

13

Sequences

	Sequence		Length	Mass (Da)
	O88554-1 [UniParc]. Last modified September 26, 2001. Version 3. Checksum: E0AEDAEE412C1445	FASTA	559	63,397
	10 20 30 40 50 60 MAPRRQRSGS GRRVLNEAKK VDNGNKATED DSPPGKKMRT CQRKGPMAGG KDADRTKDNR 70 80 90 100 110 120 DSVKTLLLKG KAPVDPECAA KLGKAHVYCE GDDVYDVMLN QTNLQFNNNK YYLIQLLEDD 130 140 150 160 170 180 AQRNFSVWMR WGRVGKTGQH SLVTCSGDLN KAKEIFQKKF LDKTKNNWED RENFEKVPGK 190 200 210 220 230 240 YDMLQMDYAA STQDESKTKE EETLKPESQL DLRVQELLKL ICNVQTMEEM MIEMKYDTKR 250 260 270 280 290 300 APLGKLTVAQ IKAGYQSLKK IEDCIRAGQH GRALVEACNE FYTRIPHDFG LSIPPVIRTE 310 320 330 340 350 360 KELSDKVKLL EALGDIEIAL KLVKSERQGL EHPLDQHYRN LHCALRPLDH ESNEFKVISQ 370 380 390 400 410 420 YLQSTHAPTH KDYTMTLLDV FEVEKEGEKE AFREDLPNRM LLWHGSRLSN WVGILSHGLR 430 440 450 460 470 480 VAPPEAPITG YMFGKGIYFA DMSSKSANYC FASRLKNTGL LLLSEVALGQ CNELLEANPK 490 500 510 520 530 540 AQGLLRGKHS TKGMGKMAPS PAHFITLNGS TVPLGPASDT GILNPEGYTL NYNEFIVYSP 550 NQVRMRYLLK IQFNFLQLW

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: 10364231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Embryo.
[2]	"A bidirectional promoter connects the poly(ADP-ribose) polymerase 2 (PARP-2) gene to the gene for RNase P RNA. Structure and expression of the mouse PARP-2 gene." Ame J.-C., Schreiber V., Fraulob V., Dolle P., de Murcia G.M., Niedergang C.P. J. Biol. Chem. 276:11092-11099(2001) [PubMed: 11133988] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/Sv.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryo.
[4]	"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: 10338144] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-559. Strain: C57BL/6 X 129/Sv.
[5]	"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: 11948190] [Abstract] Cited for: INTERACTION WITH PARP1; XRCC1; POLB AND LIG3, POLY-ADP-RIBOSYLATION.
[6]	"Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation." Haenni S.S., Hassa P.O., Altmeyer M., Fey M., Imhof R., Hottiger M.O. Int. J. Biochem. Cell Biol. 40:2274-2283(2008) [PubMed: 18436469] [Abstract] Cited for: ACETYLATION AT LYS-36 AND LYS-37, ADP-RIBOSYLATION AT LYS-36 AND LYS-37, MUTAGENESIS OF LYS-36 AND LYS-37.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ007780 mRNA. Translation: CAA07679.1.
AF191547 Genomic DNA. Translation: AAK13253.1.
BC062150 mRNA. Translation: AAH62150.1.
AF072521 mRNA. Translation: AAC25415.1. Different initiation.

IPI

IPI00131935.

RefSeq

NP_033762.1.

UniGene

Mm.281482

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GS0	X-ray	2.80	A/B	207-557	[»]

SMR

O88554. Positions 56-191.

ModBase

Search...

Protein-protein interaction databases

STRING

O88554.

PTM databases

PhosphoSite

O88554.

Proteomic databases

PRIDE

O88554.

Genome annotation databases

Ensembl

ENSMUST00000036126; ENSMUSP00000048877; ENSMUSG00000036023; Mus musculus. [Genome view]

GeneID

11546.

KEGG

mmu:11546.

UCSC

uc007tlq.1. mouse.

Organism-specific databases

CTD

11546.

MGI

MGI:1341112. Parp2.

Phylogenomic databases

eggNOG

maNOG15116.

HOGENOM

HBG713287.

HOVERGEN

O88554.

InParanoid

O88554.

OMA

CALHPLD.

OrthoDB

EOG9K3PG4.

PhylomeDB

O88554.

Enzyme and pathway databases

BRENDA

2.4.2.30. 244.

Gene expression databases

ArrayExpress

O88554.

Bgee

O88554.

CleanEx

MM_PARP2.

Genevestigator

O88554.

GermOnline

ENSMUSG00000036023. Mus musculus.

Family and domain databases

InterPro

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

Gene3D

G3DSA:1.20.142.10. PARP_reg. 1 hit.

Pfam

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

SMART

SM00773. WGR. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

279022.

PMAP-CutDB

O88554.

SOURCE

Search...

Entry information

Entry name

PARP2_MOUSE

Accession

Primary (citable) accession number: O88554
Secondary accession number(s): Q99N29

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	September 26, 2001
Last modified:	February 9, 2010
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)