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Protein

Poly [ADP-ribose] polymerase 2

Gene

Parp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.

Catalytic activityi

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi1 – 6565Sequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • base-excision repair Source: MGI
  • DNA ligation involved in DNA repair Source: GO_Central
  • DNA repair Source: MGI
  • extrinsic apoptotic signaling pathway Source: MGI
  • lagging strand elongation Source: GO_Central
  • protein ADP-ribosylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

DNA-binding, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Poly [ADP-ribose] polymerase 2 (EC:2.4.2.30)
Short name:
PARP-2
Short name:
mPARP-2
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 namesi
Name:Parp2
Synonyms:Adprt2, Adprtl2, Aspartl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1341112. Parp2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • nucleolus Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi36 – 361K → R: Decreases levels of mono-ADP-ribosylation without loss of enzyme activity. 1 Publication
Mutagenesisi37 – 371K → R: Decreases levels of mono-ADP-ribosylation without loss of enzyme activity. 1 Publication

Chemistry

ChEMBLiCHEMBL2794.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 559559Poly [ADP-ribose] polymerase 2PRO_0000211328Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361N6-(ADP-ribosyl)lysine; alternate1 Publication
Modified residuei36 – 361N6-acetyllysine; alternate1 Publication
Modified residuei37 – 371N6-(ADP-ribosyl)lysine; alternate1 Publication
Modified residuei37 – 371N6-acetyllysine; alternate1 Publication
Modified residuei208 – 2081PhosphoserineBy similarity

Post-translational modificationi

Poly-ADP-ribosylated by PARP1.
Acetylation reduces DNA binding and enzymatic activity.1 Publication

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

EPDiO88554.
MaxQBiO88554.
PaxDbiO88554.
PeptideAtlasiO88554.
PRIDEiO88554.

PTM databases

iPTMnetiO88554.
PhosphoSiteiO88554.

Miscellaneous databases

PMAP-CutDBO88554.

Expressioni

Tissue specificityi

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 stagei

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.

Inductioni

By high levels of DNA-damaging agents.

Gene expression databases

BgeeiO88554.
CleanExiMM_PARP2.
GenevisibleiO88554. MM.

Interactioni

Subunit structurei

Component of a base excision repair (BER) complex, containing at least XRCC1, PARP1, POLB and LRIG3. Homo- and heterodimer with PARP1.

Protein-protein interaction databases

BioGridi197999. 3 interactions.
IntActiO88554. 1 interaction.
MINTiMINT-8178420.
STRINGi10090.ENSMUSP00000048877.

Chemistry

BindingDBiO88554.

Structurei

Secondary structure

1
559
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi212 – 22211Combined sources
Helixi224 – 2329Combined sources
Turni233 – 2353Combined sources
Beta strandi238 – 2414Combined sources
Helixi243 – 2453Combined sources
Helixi248 – 26619Combined sources
Helixi272 – 28413Combined sources
Helixi300 – 32021Combined sources
Helixi333 – 3408Combined sources
Beta strandi343 – 3475Combined sources
Helixi353 – 36412Combined sources
Beta strandi372 – 38514Combined sources
Helixi388 – 3914Combined sources
Beta strandi399 – 4068Combined sources
Helixi408 – 4103Combined sources
Helixi411 – 4177Combined sources
Beta strandi424 – 4263Combined sources
Helixi428 – 4303Combined sources
Beta strandi434 – 4418Combined sources
Helixi443 – 4475Combined sources
Helixi448 – 4503Combined sources
Beta strandi454 – 4563Combined sources
Beta strandi458 – 46710Combined sources
Beta strandi470 – 4767Combined sources
Helixi481 – 4844Combined sources
Beta strandi489 – 4935Combined sources
Beta strandi496 – 4983Combined sources
Helixi501 – 5033Combined sources
Beta strandi505 – 5073Combined sources
Beta strandi510 – 5123Combined sources
Beta strandi525 – 5273Combined sources
Beta strandi534 – 5385Combined sources
Helixi540 – 5423Combined sources
Beta strandi543 – 55513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GS0X-ray2.80A/B207-557[»]
ProteinModelPortaliO88554.
SMRiO88554. Positions 72-557.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88554.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini207 – 324118PARP alpha-helicalPROSITE-ProRule annotationAdd
BLAST
Domaini332 – 559228PARP catalyticPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi3 – 97Nuclear localization signalSequence analysis
Motifi33 – 397Nuclear localization signalSequence analysis

Sequence similaritiesi

Contains 1 PARP alpha-helical domain.PROSITE-ProRule annotation
Contains 1 PARP catalytic domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
GeneTreeiENSGT00390000017341.
HOGENOMiHOG000173055.
HOVERGENiHBG053514.
InParanoidiO88554.
KOiK10798.
OMAiACSGDLN.
OrthoDBiEOG7KM5S0.
PhylomeDBiO88554.
TreeFamiTF315407.

Family and domain databases

Gene3Di1.20.142.10. 1 hit.
2.20.140.10. 1 hit.
3.90.228.10. 1 hit.
InterProiIPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
[Graphical view]
PfamiPF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
[Graphical view]
SMARTiSM00773. WGR. 1 hit.
[Graphical view]
SUPFAMiSSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
PROSITEiPS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88554-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPRRQRSGS GRRVLNEAKK VDNGNKATED DSPPGKKMRT CQRKGPMAGG
60 70 80 90 100
KDADRTKDNR DSVKTLLLKG KAPVDPECAA KLGKAHVYCE GDDVYDVMLN
110 120 130 140 150
QTNLQFNNNK YYLIQLLEDD AQRNFSVWMR WGRVGKTGQH SLVTCSGDLN
160 170 180 190 200
KAKEIFQKKF LDKTKNNWED RENFEKVPGK YDMLQMDYAA STQDESKTKE
210 220 230 240 250
EETLKPESQL DLRVQELLKL ICNVQTMEEM MIEMKYDTKR APLGKLTVAQ
260 270 280 290 300
IKAGYQSLKK IEDCIRAGQH GRALVEACNE FYTRIPHDFG LSIPPVIRTE
310 320 330 340 350
KELSDKVKLL EALGDIEIAL KLVKSERQGL EHPLDQHYRN LHCALRPLDH
360 370 380 390 400
ESNEFKVISQ YLQSTHAPTH KDYTMTLLDV FEVEKEGEKE AFREDLPNRM
410 420 430 440 450
LLWHGSRLSN WVGILSHGLR VAPPEAPITG YMFGKGIYFA DMSSKSANYC
460 470 480 490 500
FASRLKNTGL LLLSEVALGQ CNELLEANPK AQGLLRGKHS TKGMGKMAPS
510 520 530 540 550
PAHFITLNGS TVPLGPASDT GILNPEGYTL NYNEFIVYSP NQVRMRYLLK

IQFNFLQLW
Length:559
Mass (Da):63,397
Last modified:September 26, 2001 - v3
Checksum:iE0AEDAEE412C1445
GO

Sequence cautioni

The sequence AAC25415.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821L → V in AAK13253 (PubMed:11133988).Curated
Sequence conflicti177 – 1771V → I in AAK13253 (PubMed:11133988).Curated
Sequence conflicti486 – 4861R → Q in AAK13253 (PubMed:11133988).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007780 mRNA. Translation: CAA07679.1.
AF191547 Genomic DNA. Translation: AAK13253.1.
BC062150 mRNA. Translation: AAH62150.1.
AF072521 mRNA. Translation: AAC25415.1. Different initiation.
CCDSiCCDS27025.1.
RefSeqiNP_033762.1. NM_009632.2.
XP_006518505.1. XM_006518442.2.
UniGeneiMm.281482.

Genome annotation databases

EnsembliENSMUST00000036126; ENSMUSP00000048877; ENSMUSG00000036023.
GeneIDi11546.
KEGGimmu:11546.
UCSCiuc007tlq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007780 mRNA. Translation: CAA07679.1.
AF191547 Genomic DNA. Translation: AAK13253.1.
BC062150 mRNA. Translation: AAH62150.1.
AF072521 mRNA. Translation: AAC25415.1. Different initiation.
CCDSiCCDS27025.1.
RefSeqiNP_033762.1. NM_009632.2.
XP_006518505.1. XM_006518442.2.
UniGeneiMm.281482.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GS0X-ray2.80A/B207-557[»]
ProteinModelPortaliO88554.
SMRiO88554. Positions 72-557.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi197999. 3 interactions.
IntActiO88554. 1 interaction.
MINTiMINT-8178420.
STRINGi10090.ENSMUSP00000048877.

Chemistry

BindingDBiO88554.
ChEMBLiCHEMBL2794.

PTM databases

iPTMnetiO88554.
PhosphoSiteiO88554.

Proteomic databases

EPDiO88554.
MaxQBiO88554.
PaxDbiO88554.
PeptideAtlasiO88554.
PRIDEiO88554.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036126; ENSMUSP00000048877; ENSMUSG00000036023.
GeneIDi11546.
KEGGimmu:11546.
UCSCiuc007tlq.1. mouse.

Organism-specific databases

CTDi10038.
MGIiMGI:1341112. Parp2.

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
GeneTreeiENSGT00390000017341.
HOGENOMiHOG000173055.
HOVERGENiHBG053514.
InParanoidiO88554.
KOiK10798.
OMAiACSGDLN.
OrthoDBiEOG7KM5S0.
PhylomeDBiO88554.
TreeFamiTF315407.

Miscellaneous databases

EvolutionaryTraceiO88554.
PMAP-CutDBO88554.
PROiO88554.
SOURCEiSearch...

Gene expression databases

BgeeiO88554.
CleanExiMM_PARP2.
GenevisibleiO88554. MM.

Family and domain databases

Gene3Di1.20.142.10. 1 hit.
2.20.140.10. 1 hit.
3.90.228.10. 1 hit.
InterProiIPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
[Graphical view]
PfamiPF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
[Graphical view]
SMARTiSM00773. WGR. 1 hit.
[Graphical view]
SUPFAMiSSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
PROSITEiPS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PARP1; XRCC1; POLB AND LRIG3, 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] [Europe PMC] [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.

Entry informationi

Entry nameiPARP2_MOUSE
AccessioniPrimary (citable) accession number: O88554
Secondary accession number(s): Q99N29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: July 6, 2016
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.