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Protein

Poly [ADP-ribose] polymerase 2

Gene

PARP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 (PubMed:10364231, PubMed:28190768). This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks (PubMed:10364231). Mediates serine ADP-ribosylation of target proteins following interaction with HPF1; HPF1 conferring serine specificity (PubMed:28190768).2 Publications

Caution

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
  • peptidyl-serine ADP-ribosylation Source: UniProtKB
  • protein ADP-ribosylation Source: ProtInc

Keywordsi

Molecular functionDNA-binding, Glycosyltransferase, Transferase
LigandNAD

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000129484.13
HGNCiHGNC:272 PARP2
MIMi607725 gene
neXtProtiNX_Q9UGN5

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi10038
OpenTargetsiENSG00000129484
PharmGKBiPA24592

Chemistry databases

ChEMBLiCHEMBL5366
DrugBankiDB09074 Olaparib
DB12332 Rucaparib
DB07232 Veliparib
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
Acetylation reduces DNA binding and enzymatic activity.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 (By similarity). Homo- and heterodimer with PARP1 (PubMed:20092359). Interacts weakly (via the PARP catalytic domain) with HPF1 (PubMed:27067600, PubMed:28190768).By similarity3 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi11535058 interactors.
DIPiDIP-48934N
IntActiQ9UGN5 59 interactors.
MINTiQ9UGN5
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

Phylogenomic databases

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

Family and domain databases

Gene3Di1.20.142.101 hit
2.20.140.101 hit
InterProiView protein in InterPro
IPR012317 Poly(ADP-ribose)pol_cat_dom
IPR004102 Poly(ADP-ribose)pol_reg_dom
IPR036616 Poly(ADP-ribose)pol_reg_dom_sf
IPR036930 WGR_dom_sf
IPR008893 WGR_domain
PfamiView protein in Pfam
PF00644 PARP, 1 hit
PF02877 PARP_reg, 1 hit
PF05406 WGR, 1 hit
SMARTiView protein in SMART
SM00773 WGR, 1 hit
SUPFAMiSSF142921 SSF142921, 1 hit
SSF47587 SSF47587, 1 hit
PROSITEiView protein in PROSITE
PS51060 PARP_ALPHA_HD, 1 hit
PS51059 PARP_CATALYTIC, 1 hit

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 → N1 PublicationCorresponds to variant dbSNP:rs3093905Ensembl.1
Natural variantiVAR_019175168N → S1 PublicationCorresponds to variant dbSNP:rs3093906Ensembl.1
Natural variantiVAR_019176235D → G1 PublicationCorresponds to variant dbSNP:rs3093921Ensembl.1
Natural variantiVAR_019177285I → V1 PublicationCorresponds to variant dbSNP:rs3093925Ensembl.1
Natural variantiVAR_019178296R → Q1 PublicationCorresponds to variant dbSNP:rs3093926Ensembl.1
Natural variantiVAR_050462331I → T. Corresponds to variant dbSNP:rs2275010Ensembl.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

Similar proteinsi

Entry informationi

Entry nameiPARP2_HUMAN
AccessioniPrimary (citable) accession number: Q9UGN5
Secondary accession number(s): Q8TEU4
, Q9NUV2, Q9UMR4, Q9Y6C8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: April 25, 2018
This is version 175 of the entry and version 2 of the sequence. See 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