[1]	NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. TISSUE=Embryo; DOI=10.1074/jbc.274.25.17860; PubMed=10364231 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "PARP-2, a novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase."; J. Biol. Chem. 274:17860-17868(1999).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=129/Sv; DOI=10.1074/jbc.M007870200; PubMed=11133988 [NCBI, ExPASy, EBI, Israel, Japan] Ame J.-C., Schreiber V., Fraulob V., Dolle P., de Murcia G.M., Niedergang C.P.; "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."; J. Biol. Chem. 276:11092-11099(2001).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Embryo; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 9-559. STRAIN=C57BL/6 X 129/Sv; DOI=10.1016/S0014-5793(99)00448-2; PubMed=10338144 [NCBI, ExPASy, EBI, Israel, Japan] Berghammer H., Ebner M., Marksteiner R., Auer B.; "pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans."; FEBS Lett. 449:259-263(1999).
[5]	INTERACTION WITH PARP1; XRCC1; POLB AND LIG3, AND POLY-ADP-RIBOSYLATION. DOI=10.1074/jbc.M202390200; PubMed=11948190 [NCBI, ExPASy, EBI, Israel, Japan] Schreiber V., Ame J.-C., Dolle P., Schultz I., Rinaldi B., Fraulob V., Menissier-de Murcia J., de Murcia G.M.; "Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1."; J. Biol. Chem. 277:23028-23036(2002).
[6]	ACETYLATION AT LYS-36 AND LYS-37, ADP-RIBOSYLATION AT LYS-36 AND LYS-37, AND MUTAGENESIS OF LYS-36 AND LYS-37. DOI=10.1016/j.biocel.2008.03.008; PubMed=18436469 [NCBI, ExPASy, EBI, Israel, Japan] Haenni S.S., Hassa P.O., Altmeyer M., Fey M., Imhof R., Hottiger M.O.; "Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation."; Int. J. Biochem. Cell Biol. 40:2274-2283(2008).

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: 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.
PTM: Poly-ADP-ribosylated by PARP1.
PTM: Acetylation reduces DNA binding and enzymatic activity.
SIMILARITY: Contains 1 PARP alpha-helical domain.
SIMILARITY: Contains 1 PARP catalytic domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ007780; CAA07679.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF191547; AAK13253.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC062150; AAH62150.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF072521; AAC25415.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00131935; -.

NP_033762.1; -.

3D structure databases

PDB

1GS0; X-ray; 2.80 A; A/B=207-557.

[ExPASy / RCSB / EBI]

1GS0; -.

PTM databases

O88554; -.

Enzyme and pathway databases

BRENDA

2.4.2.30; 244.

Organism-specific databases

MGI

MGI:1341112; Parp2.

Gene expression databases

O88554; -.

O88554; -.

MM_PARP2; -.

ENSMUSG00000036023; Mus musculus.

Ontologies

GO:0005730;	Cellular component: nucleolus (inferred from direct assay from MGI).
GO:0005654;	Cellular component: nucleoplasm (inferred from direct assay from MGI).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003950;	Molecular function: NAD+ ADP-ribosyltransferase activity (inferred from direct assay from MGI).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0006284;	Biological process: base-excision repair (inferred from mutant phenotype from MGI).
GO:0006471;	Biological process: protein amino acid ADP-ribosylation (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR012317; PARP_catalytic.
IPR004102; PARP_reg.
IPR008893; WGR.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.142.10; PARP_reg; 1.

Pfam

PF00644; PARP; 1.
PF02877; PARP_reg; 1.
PF05406; WGR; 1.
Pfam graphical view of domain structure.

SMART

SM00773; WGR; 1.
SMART graphical view of domain structure.

PROSITE

PS51060; PARP_ALPHA_HD; 1.
PS51059; PARP_CATALYTIC; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

O88554; -.

Genome annotation databases

Ensembl

ENSMUSG00000036023; Mus musculus. [Contig view]

GeneID

11546; -.

KEGG

mmu:11546; -.

Phylogenomic databases

HOGENOM

O88554; -.

HOVERGEN

O88554; -.

OMA

O88554; SRLSNWV.

Other

279022; -.

O88554; -.

Parp2; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; ADP-ribosylation; DNA-binding; Glycosyltransferase; NAD; Nucleus; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 559`	`559`	`Poly [ADP-ribose] polymerase 2.`	`PRO_0000211328`
`DOMAIN`	`207 324`	`118`	`PARP alpha-helical.`
`DOMAIN`	`332 559`	`228`	`PARP catalytic.`
`DNA_BIND`	`1 65`	`65`	`Potential.`
`MOTIF`	`3 9`	`7`	`Nuclear localization signal (Potential).`
`MOTIF`	`33 39`	`7`	`Nuclear localization signal (Potential).`
`MOD_RES`	`36 36`		`N6-(ADP-ribosyl)lysine; alternate (Probable).`
`MOD_RES`	`36 36`		`N6-acetyllysine; alternate.`
`MOD_RES`	`37 37`		`N6-(ADP-ribosyl)lysine; alternate (Probable).`
`MOD_RES`	`37 37`		`N6-acetyllysine; alternate.`
`MUTAGEN`	`36 36`		`K->R: Decreases levels of mono-ADP-ribosylation without loss of enzyme activity.`
`MUTAGEN`	`37 37`		`K->R: Decreases levels of mono-ADP-ribosylation without loss of enzyme activity.`
`CONFLICT`	`82 82`		`L -> V (in Ref. 2; AAK13253).`
`CONFLICT`	`177 177`		`V -> I (in Ref. 2; AAK13253).`
`CONFLICT`	`486 486`		`R -> Q (in Ref. 2; AAK13253).`
`HELIX`	`212 222`	`11`
`HELIX`	`224 232`	`9`
`TURN`	`233 235`	`3`
`STRAND`	`238 241`	`4`
`HELIX`	`243 245`	`3`
`HELIX`	`248 266`	`19`
`HELIX`	`272 284`	`13`
`HELIX`	`300 320`	`21`
`HELIX`	`333 340`	`8`
`STRAND`	`343 347`	`5`
`HELIX`	`353 364`	`12`
`STRAND`	`372 385`	`14`
`HELIX`	`388 391`	`4`
`STRAND`	`399 406`	`8`
`HELIX`	`408 410`	`3`
`HELIX`	`411 417`	`7`
`STRAND`	`424 426`	`3`
`HELIX`	`428 430`	`3`
`STRAND`	`434 441`	`8`
`HELIX`	`443 447`	`5`
`HELIX`	`448 450`	`3`
`STRAND`	`454 456`	`3`
`STRAND`	`458 467`	`10`
`STRAND`	`470 476`	`7`
`HELIX`	`481 484`	`4`
`STRAND`	`489 493`	`5`
`STRAND`	`496 498`	`3`
`HELIX`	`501 503`	`3`
`STRAND`	`505 507`	`3`
`STRAND`	`510 512`	`3`
`STRAND`	`525 527`	`3`
`STRAND`	`534 538`	`5`
`HELIX`	`540 542`	`3`
`STRAND`	`543 555`	`13`

Sequence information

Length: 559 AA [This is the length of the unprocessed precursor]

Molecular weight: 63397 Da [This is the MW of the unprocessed precursor]

CRC64: E0AEDAEE412C1445 [This is a checksum on the sequence]

        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

O88554 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools