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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)DescriptionActionsGraphical viewLength
DNA bindingi1 – 65Sequence analysisAdd BLAST65

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)DescriptionActionsGraphical viewLength
Mutagenesisi36K → R: Decreases levels of mono-ADP-ribosylation without loss of enzyme activity. 1 Publication1
Mutagenesisi37K → R: Decreases levels of mono-ADP-ribosylation without loss of enzyme activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2794.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002113281 – 559Poly [ADP-ribose] polymerase 2Add BLAST559

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei36N6-(ADP-ribosyl)lysine; alternate1 Publication1
Modified residuei36N6-acetyllysine; alternate1 Publication1
Modified residuei37N6-(ADP-ribosyl)lysine; alternate1 Publication1
Modified residuei37N6-acetyllysine; alternate1 Publication1
Modified residuei208PhosphoserineBy similarity1

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.
PhosphoSitePlusiO88554.

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

BgeeiENSMUSG00000036023.
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 (PubMed:11948190). Interacts weakly (via the PARP catalytic domain) with HPF1 (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi197999. 3 interactors.
IntActiO88554. 1 interactor.
MINTiMINT-8178420.
STRINGi10090.ENSMUSP00000048877.

Chemistry databases

BindingDBiO88554.

Structurei

Secondary structure

1559
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi212 – 222Combined sources11
Helixi224 – 232Combined sources9
Turni233 – 235Combined sources3
Beta strandi238 – 241Combined sources4
Helixi243 – 245Combined sources3
Helixi248 – 266Combined sources19
Helixi272 – 284Combined sources13
Helixi300 – 320Combined sources21
Helixi333 – 340Combined sources8
Beta strandi343 – 347Combined sources5
Helixi353 – 364Combined sources12
Beta strandi372 – 385Combined sources14
Helixi388 – 391Combined sources4
Beta strandi399 – 406Combined sources8
Helixi408 – 410Combined sources3
Helixi411 – 417Combined sources7
Beta strandi424 – 426Combined sources3
Helixi428 – 430Combined sources3
Beta strandi434 – 441Combined sources8
Helixi443 – 447Combined sources5
Helixi448 – 450Combined sources3
Beta strandi454 – 456Combined sources3
Beta strandi458 – 467Combined sources10
Beta strandi470 – 476Combined sources7
Helixi481 – 484Combined sources4
Beta strandi489 – 493Combined sources5
Beta strandi496 – 498Combined sources3
Helixi501 – 503Combined sources3
Beta strandi505 – 507Combined sources3
Beta strandi510 – 512Combined sources3
Beta strandi525 – 527Combined sources3
Beta strandi534 – 538Combined sources5
Helixi540 – 542Combined sources3
Beta strandi543 – 555Combined sources13

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO88554.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini207 – 324PARP alpha-helicalPROSITE-ProRule annotationAdd BLAST118
Domaini332 – 559PARP catalyticPROSITE-ProRule annotationAdd BLAST228

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi3 – 9Nuclear localization signalSequence analysis7
Motifi33 – 39Nuclear localization signalSequence analysis7

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.
OrthoDBiEOG091G13H1.
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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti82L → V in AAK13253 (PubMed:11133988).Curated1
Sequence conflicti177V → I in AAK13253 (PubMed:11133988).Curated1
Sequence conflicti486R → Q in AAK13253 (PubMed:11133988).Curated1

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_006518442.3.
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_006518442.3.
UniGeneiMm.281482.

3D structure databases

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

Protein-protein interaction databases

BioGridi197999. 3 interactors.
IntActiO88554. 1 interactor.
MINTiMINT-8178420.
STRINGi10090.ENSMUSP00000048877.

Chemistry databases

BindingDBiO88554.
ChEMBLiCHEMBL2794.

PTM databases

iPTMnetiO88554.
PhosphoSitePlusiO88554.

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.
OrthoDBiEOG091G13H1.
PhylomeDBiO88554.
TreeFamiTF315407.

Miscellaneous databases

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

Gene expression databases

BgeeiENSMUSG00000036023.
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...

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: November 2, 2016
This is version 147 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.