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Reviewed, UniProtKB/Swiss-Prot Q9UGN5 (PARP2_HUMAN)

Last modified February 9, 2010. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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):
    NAD(+) ADP-ribosyltransferase 2
      Short name=ADPRT-2
    Poly[ADP-ribose] synthetase 2
      Short name=pADPRT-2
Gene names
Name: PARP2
Synonyms: ADPRT2, ADPRTL2
OrganismHomo sapiens (Human) [Complete 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 LIG3. Homo- and heterodimer with PARP1.

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

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandDNA-binding
NAD
   Molecular functionGlycosyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processprotein amino acid ADP-ribosylation

Traceable author statement. Source: ProtInc

   Cellular componentnucleolus

Inferred from direct assay. Source: MGI

nucleoplasm

Inferred from direct assay. Source: MGI

   Molecular functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

NAD+ ADP-ribosyltransferase activity

Inferred from electronic annotation. Source: EC

protein binding

Inferred from physical interaction. Source: MGI

Complete GO annotation...

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

Natural variations

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

Experimental info

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

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.

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: 10364231] [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: 10329013] [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: 10338144] [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: 14702039] [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: 11948190] [Abstract]
Cited for: INTERACTION WITH PARP1; XRCC1; POLB AND LIG3.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+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.
IPIIPI00026497.
IPI00220995.
RefSeqNP_001036083.1.
NP_005475.2.
UniGeneHs.409412

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KCZX-ray2.00A/B235-579[»]
3KJDX-ray1.95A/B235-579[»]
SMRQ9UGN5. Positions 79-209.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9UGN5.

PTM databases

PhosphoSiteQ9UGN5.

Proteomic databases

PRIDEQ9UGN5.

Genome annotation databases

EnsemblENST00000250416; ENSP00000250416; ENSG00000129484; Homo sapiens. [Genome view]
GeneID10038.
KEGGhsa:10038.
UCSCuc001vxb.1. human.
uc001vxd.1. human.

Organism-specific databases

CTD10038.
GeneCardsGC14P019881.
HGNCHGNC:272. PARP2.
MIM607725. gene.
PharmGKBPA24592.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG05958.
HOGENOMHBG713287.
HOVERGENQ9UGN5.
InParanoidQ9UGN5.
OMACALHPLD.
OrthoDBEOG9K3PG4.
PhylomeDBQ9UGN5.

Enzyme and pathway databases

BRENDA2.4.2.30. 247.
Pathway_Interaction_DBtelomerasepathway. Regulation of Telomerase.

Gene expression databases

ArrayExpressQ9UGN5.
BgeeQ9UGN5.
CleanExHS_PARP2.
GenevestigatorQ9UGN5.
GermOnlineENSG00000129484. Homo sapiens.

Family and domain databases

InterProIPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR.
[Graphical view]
Gene3DG3DSA:1.20.142.10. PARP_reg. 1 hit.
PfamPF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
[Graphical view]
SMARTSM00773. WGR. 1 hit.
[Graphical view]
PROSITEPS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio37907.
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: February 9, 2010
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents