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Protein

Poly [ADP-ribose] polymerase 2

Gene

PARP2

Organism
Homo sapiens (Human)
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 – 88Sequence analysisAdd BLAST88

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

DNA-binding, NAD

Enzyme and pathway databases

BioCyciZFISH:HS05285-MONOMER.
BRENDAi2.4.2.30. 2681.
ReactomeiR-HSA-110362. POLB-Dependent Long Patch Base Excision Repair.
R-HSA-5685939. HDR through MMEJ (alt-NHEJ).
R-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
SIGNORiQ9UGN5.

Names & Taxonomyi

Protein namesi
Recommended name:
Poly [ADP-ribose] polymerase 2 (EC:2.4.2.30)
Short name:
PARP-2
Short name:
hPARP-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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:272. PARP2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi10038.
OpenTargetsiENSG00000129484.
PharmGKBiPA24592.

Chemistry databases

ChEMBLiCHEMBL5366.
DrugBankiDB09074. Olaparib.
GuidetoPHARMACOLOGYi2772.

Polymorphism and mutation databases

BioMutaiPARP2.
DMDMi17380230.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002113271 – 583Poly [ADP-ribose] polymerase 2Add BLAST583

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei37N6-acetyllysineBy similarity1
Modified residuei38N6-acetyllysineBy similarity1
Modified residuei226PhosphoserineCombined sources1
Modified residuei232PhosphoserineCombined sources1

Post-translational modificationi

Poly-ADP-ribosylated by PARP1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9UGN5.
PaxDbiQ9UGN5.
PeptideAtlasiQ9UGN5.
PRIDEiQ9UGN5.

PTM databases

iPTMnetiQ9UGN5.
PhosphoSitePlusiQ9UGN5.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiENSG00000129484.
CleanExiHS_PARP2.
ExpressionAtlasiQ9UGN5. baseline and differential.
GenevisibleiQ9UGN5. HS.

Organism-specific databases

HPAiHPA052003.

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:20092359). Interacts weakly (via the PARP catalytic domain) with HPF1 (PubMed:27067600).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FKBP3Q006882EBI-2795348,EBI-1044081
STACQ994692EBI-2795348,EBI-2652799

Protein-protein interaction databases

BioGridi115350. 41 interactors.
DIPiDIP-48934N.
IntActiQ9UGN5. 57 interactors.
MINTiMINT-7914677.
STRINGi9606.ENSP00000250416.

Chemistry databases

BindingDBiQ9UGN5.

Structurei

Secondary structure

1583
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi236 – 245Combined sources10
Helixi248 – 257Combined sources10
Turni262 – 264Combined sources3
Helixi267 – 269Combined sources3
Helixi272 – 290Combined sources19
Helixi296 – 308Combined sources13
Helixi324 – 346Combined sources23
Helixi357 – 365Combined sources9
Beta strandi367 – 371Combined sources5
Helixi377 – 388Combined sources12
Beta strandi397 – 409Combined sources13
Helixi412 – 415Combined sources4
Beta strandi423 – 429Combined sources7
Helixi432 – 434Combined sources3
Helixi435 – 441Combined sources7
Helixi452 – 454Combined sources3
Beta strandi459 – 466Combined sources8
Helixi467 – 471Combined sources5
Helixi472 – 474Combined sources3
Beta strandi478 – 480Combined sources3
Beta strandi482 – 491Combined sources10
Beta strandi494 – 500Combined sources7
Helixi505 – 508Combined sources4
Beta strandi514 – 517Combined sources4
Beta strandi519 – 523Combined sources5
Helixi525 – 527Combined sources3
Beta strandi529 – 531Combined sources3
Beta strandi534 – 536Combined sources3
Beta strandi541 – 543Combined sources3
Beta strandi549 – 551Combined sources3
Beta strandi554 – 556Combined sources3
Beta strandi558 – 563Combined sources6
Helixi564 – 566Combined sources3
Beta strandi567 – 579Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KCZX-ray2.00A/B235-579[»]
3KJDX-ray1.95A/B235-579[»]
4PJVX-ray2.50A/B235-579[»]
4TVJX-ray2.10A/B235-579[»]
4ZZXX-ray1.65A/B223-583[»]
4ZZYX-ray2.20A223-583[»]
5D5KX-ray1.90B1-91[»]
5DSYX-ray2.70A/B/C/D348-583[»]
ProteinModelPortaliQ9UGN5.
SMRiQ9UGN5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UGN5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini231 – 348PARP alpha-helicalPROSITE-ProRule annotationAdd BLAST118
Domaini356 – 583PARP catalyticPROSITE-ProRule annotationAdd BLAST228

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi4 – 7Nuclear localization signalSequence analysis4
Motifi35 – 40Nuclear localization signalSequence analysis6

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.
InParanoidiQ9UGN5.
KOiK10798.
OMAiACSGDLN.
OrthoDBiEOG091G13H1.
PhylomeDBiQ9UGN5.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UGN5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAARRRRSTG GGRARALNES KRVNNGNTAP EDSSPAKKTR RCQRQESKKM
60 70 80 90 100
PVAGGKANKD RTEDKQDGMP GRSWASKRVS ESVKALLLKG KAPVDPECTA
110 120 130 140 150
KVGKAHVYCE GNDVYDVMLN QTNLQFNNNK YYLIQLLEDD AQRNFSVWMR
160 170 180 190 200
WGRVGKMGQH SLVACSGNLN KAKEIFQKKF LDKTKNNWED REKFEKVPGK
210 220 230 240 250
YDMLQMDYAT NTQDEEETKK EESLKSPLKP ESQLDLRVQE LIKLICNVQA
260 270 280 290 300
MEEMMMEMKY NTKKAPLGKL TVAQIKAGYQ SLKKIEDCIR AGQHGRALME
310 320 330 340 350
ACNEFYTRIP HDFGLRTPPL IRTQKELSEK IQLLEALGDI EIAIKLVKTE
360 370 380 390 400
LQSPEHPLDQ HYRNLHCALR PLDHESYEFK VISQYLQSTH APTHSDYTMT
410 420 430 440 450
LLDLFEVEKD GEKEAFREDL HNRMLLWHGS RMSNWVGILS HGLRIAPPEA
460 470 480 490 500
PITGYMFGKG IYFADMSSKS ANYCFASRLK NTGLLLLSEV ALGQCNELLE
510 520 530 540 550
ANPKAEGLLQ GKHSTKGLGK MAPSSAHFVT LNGSTVPLGP ASDTGILNPD
560 570 580
GYTLNYNEYI VYNPNQVRMR YLLKVQFNFL QLW
Length:583
Mass (Da):66,206
Last modified:September 26, 2001 - v2
Checksum:i5B7AE8AE531836AF
GO
Isoform 2 (identifier: Q9UGN5-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:570
Mass (Da):64,805
Checksum:i335A5B64E758FDFF
GO

Sequence cautioni

The sequence AAD29857 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAL77437 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAB41505 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti447P → H in AAD29857 (PubMed:10329013).Curated1
Sequence conflicti481N → H in BAA92017 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_019174161S → N.1 PublicationCorresponds to variant rs3093905dbSNPEnsembl.1
Natural variantiVAR_019175168N → S.1 PublicationCorresponds to variant rs3093906dbSNPEnsembl.1
Natural variantiVAR_019176235D → G.1 PublicationCorresponds to variant rs3093921dbSNPEnsembl.1
Natural variantiVAR_019177285I → V.1 PublicationCorresponds to variant rs3093925dbSNPEnsembl.1
Natural variantiVAR_019178296R → Q.1 PublicationCorresponds to variant rs3093926dbSNPEnsembl.1
Natural variantiVAR_050462331I → T.Corresponds to variant rs2275010dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00453768 – 80Missing in isoform 2. 1 PublicationAdd BLAST13

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41910.1. [Q9UGN5-1]
CCDS45077.1. [Q9UGN5-2]
RefSeqiNP_001036083.1. NM_001042618.1. [Q9UGN5-2]
NP_005475.2. NM_005484.3. [Q9UGN5-1]
UniGeneiHs.409412.

Genome annotation databases

EnsembliENST00000250416; ENSP00000250416; ENSG00000129484. [Q9UGN5-1]
ENST00000429687; ENSP00000392972; ENSG00000129484. [Q9UGN5-2]
GeneIDi10038.
KEGGihsa:10038.
UCSCiuc001vxc.4. human. [Q9UGN5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41910.1. [Q9UGN5-1]
CCDS45077.1. [Q9UGN5-2]
RefSeqiNP_001036083.1. NM_001042618.1. [Q9UGN5-2]
NP_005475.2. NM_005484.3. [Q9UGN5-1]
UniGeneiHs.409412.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KCZX-ray2.00A/B235-579[»]
3KJDX-ray1.95A/B235-579[»]
4PJVX-ray2.50A/B235-579[»]
4TVJX-ray2.10A/B235-579[»]
4ZZXX-ray1.65A/B223-583[»]
4ZZYX-ray2.20A223-583[»]
5D5KX-ray1.90B1-91[»]
5DSYX-ray2.70A/B/C/D348-583[»]
ProteinModelPortaliQ9UGN5.
SMRiQ9UGN5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115350. 41 interactors.
DIPiDIP-48934N.
IntActiQ9UGN5. 57 interactors.
MINTiMINT-7914677.
STRINGi9606.ENSP00000250416.

Chemistry databases

BindingDBiQ9UGN5.
ChEMBLiCHEMBL5366.
DrugBankiDB09074. Olaparib.
GuidetoPHARMACOLOGYi2772.

PTM databases

iPTMnetiQ9UGN5.
PhosphoSitePlusiQ9UGN5.

Polymorphism and mutation databases

BioMutaiPARP2.
DMDMi17380230.

Proteomic databases

EPDiQ9UGN5.
PaxDbiQ9UGN5.
PeptideAtlasiQ9UGN5.
PRIDEiQ9UGN5.

Protocols and materials databases

DNASUi10038.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000250416; ENSP00000250416; ENSG00000129484. [Q9UGN5-1]
ENST00000429687; ENSP00000392972; ENSG00000129484. [Q9UGN5-2]
GeneIDi10038.
KEGGihsa:10038.
UCSCiuc001vxc.4. human. [Q9UGN5-1]

Organism-specific databases

CTDi10038.
DisGeNETi10038.
GeneCardsiPARP2.
HGNCiHGNC:272. PARP2.
HPAiHPA052003.
MIMi607725. gene.
neXtProtiNX_Q9UGN5.
OpenTargetsiENSG00000129484.
PharmGKBiPA24592.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
GeneTreeiENSGT00390000017341.
HOGENOMiHOG000173055.
HOVERGENiHBG053514.
InParanoidiQ9UGN5.
KOiK10798.
OMAiACSGDLN.
OrthoDBiEOG091G13H1.
PhylomeDBiQ9UGN5.
TreeFamiTF315407.

Enzyme and pathway databases

BioCyciZFISH:HS05285-MONOMER.
BRENDAi2.4.2.30. 2681.
ReactomeiR-HSA-110362. POLB-Dependent Long Patch Base Excision Repair.
R-HSA-5685939. HDR through MMEJ (alt-NHEJ).
R-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
SIGNORiQ9UGN5.

Miscellaneous databases

ChiTaRSiPARP2. human.
EvolutionaryTraceiQ9UGN5.
GeneWikiiPARP2.
GenomeRNAii10038.
PROiQ9UGN5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000129484.
CleanExiHS_PARP2.
ExpressionAtlasiQ9UGN5. baseline and differential.
GenevisibleiQ9UGN5. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q9UGN5
Secondary accession number(s): Q8TEU4
, Q9NUV2, Q9UMR4, Q9Y6C8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: November 2, 2016
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.