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Q9UGN5 (PARP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly [ADP-ribose] polymerase 2

Short name=PARP-2
Short name=hPARP-2
EC=2.4.2.30
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 names
Name:PARP2
Synonyms:ADPRT2, ADPRTL2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length583 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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 structure

Component of a base excision repair (BER) complex, containing at least XRCC1, PARP1, POLB and LRIG3. Homo- and heterodimer with PARP1. Ref.10

Subcellular location

Nucleus.

Tissue specificity

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.

Post-translational modification

Poly-ADP-ribosylated by PARP1 By similarity.

Sequence similarities

Contains 1 PARP alpha-helical domain.

Contains 1 PARP catalytic domain.

Sequence caution

The sequence AAD29857.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAL77437.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB41505.2 differs from that shown. Reason: Erroneous initiation.

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UGN5-1)

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.
Isoform 2 (identifier: Q9UGN5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     68-80: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 583583Poly [ADP-ribose] polymerase 2
PRO_0000211327

Regions

Domain231 – 348118PARP alpha-helical
Domain356 – 583228PARP catalytic
DNA binding1 – 8888 Potential
Motif4 – 74Nuclear localization signal Potential
Motif35 – 406Nuclear localization signal Potential

Amino acid modifications

Modified residue371N6-acetyllysine By similarity
Modified residue381N6-acetyllysine By similarity
Modified residue2261Phosphoserine Ref.9
Modified residue2321Phosphoserine Ref.9

Natural variations

Alternative sequence68 – 8013Missing in isoform 2.
VSP_004537
Natural variant1611S → N. Ref.5
Corresponds to variant rs3093905 [ dbSNP | Ensembl ].
VAR_019174
Natural variant1681N → S. Ref.5
Corresponds to variant rs3093906 [ dbSNP | Ensembl ].
VAR_019175
Natural variant2351D → G. Ref.5
Corresponds to variant rs3093921 [ dbSNP | Ensembl ].
VAR_019176
Natural variant2851I → V. Ref.5
Corresponds to variant rs3093925 [ dbSNP | Ensembl ].
VAR_019177
Natural variant2961R → Q. Ref.5
Corresponds to variant rs3093926 [ dbSNP | Ensembl ].
VAR_019178
Natural variant3311I → T.
Corresponds to variant rs2275010 [ dbSNP | Ensembl ].
VAR_050462

Experimental info

Sequence conflict4471P → H in AAD29857. Ref.2
Sequence conflict4811N → H in BAA92017. Ref.4

Secondary structure

............................................................... 583
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: 5B7AE8AE531836AF

FASTA58366,206
        10         20         30         40         50         60 
MAARRRRSTG GGRARALNES KRVNNGNTAP EDSSPAKKTR RCQRQESKKM PVAGGKANKD 

        70         80         90        100        110        120 
RTEDKQDGMP GRSWASKRVS ESVKALLLKG KAPVDPECTA KVGKAHVYCE GNDVYDVMLN 

       130        140        150        160        170        180 
QTNLQFNNNK YYLIQLLEDD AQRNFSVWMR WGRVGKMGQH SLVACSGNLN KAKEIFQKKF 

       190        200        210        220        230        240 
LDKTKNNWED REKFEKVPGK YDMLQMDYAT NTQDEEETKK EESLKSPLKP ESQLDLRVQE 

       250        260        270        280        290        300 
LIKLICNVQA MEEMMMEMKY NTKKAPLGKL TVAQIKAGYQ SLKKIEDCIR AGQHGRALME 

       310        320        330        340        350        360 
ACNEFYTRIP HDFGLRTPPL IRTQKELSEK IQLLEALGDI EIAIKLVKTE LQSPEHPLDQ 

       370        380        390        400        410        420 
HYRNLHCALR PLDHESYEFK VISQYLQSTH APTHSDYTMT LLDLFEVEKD GEKEAFREDL 

       430        440        450        460        470        480 
HNRMLLWHGS RMSNWVGILS HGLRIAPPEA PITGYMFGKG IYFADMSSKS ANYCFASRLK 

       490        500        510        520        530        540 
NTGLLLLSEV ALGQCNELLE ANPKAEGLLQ GKHSTKGLGK MAPSSAHFVT LNGSTVPLGP 

       550        560        570        580 
ASDTGILNPD GYTLNYNEYI VYNPNQVRMR YLLKVQFNFL QLW 

« Hide

Isoform 2 [UniParc].

Checksum: 335A5B64E758FDFF
Show »

FASTA57064,805

References

« Hide 'large scale' references
[1]"PARP-2, a novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase."
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.
J. Biol. Chem. 274:17860-17868(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Fetal brain.
[2]"A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues."
Johansson M.
Genomics 57:442-445(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-583 (ISOFORM 1).
Tissue: Fetal brain.
[3]"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 22-583 (ISOFORM 1).
Tissue: Fibroblast.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[5]NIEHS SNPs program
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-161; SER-168; GLY-235; VAL-285 AND GLN-296.
[6]"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.
[7]"Toward a unified nomenclature for mammalian ADP-ribosyltransferases."
Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.
Trends Biochem. Sci. 35:208-219(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Crystal structure of the catalytic domain of human PARP2 in complex with PARP inhibitor ABT-888."
Karlberg T., Hammarstrom M., Schutz P., Svensson L., Schuler H.
Biochemistry 49:1056-1058(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 235-579 IN COMPLEX WITH PARP INHIBITORS, SUBUNIT.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS41910.1. [Q9UGN5-1]
CCDS45077.1. [Q9UGN5-2]
RefSeqNP_001036083.1. NM_001042618.1. [Q9UGN5-2]
NP_005475.2. NM_005484.3. [Q9UGN5-1]
UniGeneHs.409412.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KCZX-ray2.00A/B235-579[»]
3KJDX-ray1.95A/B235-579[»]
ProteinModelPortalQ9UGN5.
SMRQ9UGN5. Positions 92-579.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115350. 12 interactions.
DIPDIP-48934N.
IntActQ9UGN5. 53 interactions.
MINTMINT-7914677.
STRING9606.ENSP00000250416.

Chemistry

BindingDBQ9UGN5.
ChEMBLCHEMBL5366.

PTM databases

PhosphoSiteQ9UGN5.

Polymorphism databases

DMDM17380230.

Proteomic databases

MaxQBQ9UGN5.
PaxDbQ9UGN5.
PRIDEQ9UGN5.

Protocols and materials databases

DNASU10038.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250416; ENSP00000250416; ENSG00000129484. [Q9UGN5-1]
ENST00000429687; ENSP00000392972; ENSG00000129484. [Q9UGN5-2]
GeneID10038.
KEGGhsa:10038.
UCSCuc001vxb.1. human. [Q9UGN5-1]
uc001vxd.3. human. [Q9UGN5-2]

Organism-specific databases

CTD10038.
GeneCardsGC14P020811.
HGNCHGNC:272. PARP2.
HPAHPA052003.
MIM607725. gene.
neXtProtNX_Q9UGN5.
PharmGKBPA24592.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG243963.
HOGENOMHOG000173055.
HOVERGENHBG053514.
InParanoidQ9UGN5.
KOK10798.
OMAFTTIPHV.
OrthoDBEOG7KM5S0.
PhylomeDBQ9UGN5.
TreeFamTF315407.

Enzyme and pathway databases

BRENDA2.4.2.30. 2681.

Gene expression databases

ArrayExpressQ9UGN5.
BgeeQ9UGN5.
CleanExHS_PARP2.
GenevestigatorQ9UGN5.

Family and domain databases

Gene3D1.20.142.10. 1 hit.
2.20.140.10. 1 hit.
3.90.228.10. 1 hit.
InterProIPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
[Graphical view]
PfamPF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
[Graphical view]
SMARTSM00773. WGR. 1 hit.
[Graphical view]
SUPFAMSSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
PROSITEPS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPARP2. human.
EvolutionaryTraceQ9UGN5.
GeneWikiPARP2.
GenomeRNAi10038.
NextBio37907.
PROQ9UGN5.
SOURCESearch...

Entry information

Entry namePARP2_HUMAN
AccessionPrimary (citable) accession number: Q9UGN5
Secondary accession number(s): Q8TEU4 expand/collapse secondary AC list , Q9NUV2, Q9UMR4, Q9Y6C8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: July 9, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM