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Q11207 (PARP2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=PARP-2
EC=2.4.2.30
Alternative name(s):
NAD(+) ADP-ribosyltransferase 2
Short name=ADPRT-2
Poly[ADP-ribose] synthase 2
Gene names
Name:PARP2
Synonyms:APP
Ordered Locus Names:At4g02390
ORF Names:T14P8.19
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length637 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.

Subcellular location

Nucleus.

Induction

By ionising radiation (IR)-induced DNA damage, by dehydration and after cadmium exposure. Ref.4

Sequence similarities

Contains 1 PARP alpha-helical domain.

Contains 1 PARP catalytic domain.

Contains 2 SAP domains.

Sequence caution

The sequence AAC19283.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB80732.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentNucleus
   DomainRepeat
   LigandDNA-binding
NAD
   Molecular functionGlycosyltransferase
Transferase
   PTMADP-ribosylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processprotein ADP-ribosylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentnucleus

Inferred from direct assay. Source: TAIR

   Molecular functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

NAD+ ADP-ribosyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 637637Poly [ADP-ribose] polymerase 2
PRO_0000211332

Regions

Domain2 – 3635SAP 1
Domain69 – 10335SAP 2
Domain286 – 404119PARP alpha-helical
Domain412 – 637226PARP catalytic
DNA binding1 – 140140 Potential
Motif41 – 6222Nuclear localization signal Potential

Sequences

Sequence LengthMass (Da)Tools
Q11207 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 527A8F464605D127

FASTA63772,176
        10         20         30         40         50         60 
MANKLKVDEL RLKLAERGLS TTGVKAVLVE RLEEAIAEDT KKEESKSKRK RNSSNDTYES 

        70         80         90        100        110        120 
NKLIAIGEFR GMIVKELREE AIKRGLDTTG TKKDLLERLC NDANNVSNAP VKSSNGTDEA 

       130        140        150        160        170        180 
EDDNNGFEEE KKEEKIVTAT KKGAAVLDQW IPDEIKSQYH VLQRGDDVYD AILNQTNVRD 

       190        200        210        220        230        240 
NNNKFFVLQV LESDSKKTYM VYTRWGRVGV KGQSKLDGPY DSWDRAIEIF TNKFNDKTKN 

       250        260        270        280        290        300 
YWSDRKEFIP HPKSYTWLEM DYGKEENDSP VNNDIPSSSS EVKPEQSKLD TRVAKFISLI 

       310        320        330        340        350        360 
CNVSMMAQHM MEIGYNANKL PLGKISKSTI SKGYEVLKRI SEVIDRYDRT RLEELSGEFY 

       370        380        390        400        410        420 
TVIPHDFGFK KMSQFVIDTP QKLKQKIEMV EALGEIELAT KLLSVDPGLQ DDPLYYHYQQ 

       430        440        450        460        470        480 
LNCGLTPVGN DSEEFSMVAN YMENTHAKTH SGYTVEIAQL FRASRAVEAD RFQQFSSSKN 

       490        500        510        520        530        540 
RMLLWHGSRL TNWAGILSQG LRIAPPEAPV TGYMFGKGVY FADMFSKSAN YCYANTGAND 

       550        560        570        580        590        600 
GVLLLCEVAL GDMNELLYSD YNADNLPPGK LSTKGVGKTA PNPSEAQTLE DGVVVPLGKP 

       610        620        630 
VERSCSKGML LYNEYIVYNV EQIKMRYVIQ VKFNYKH 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of an Arabidopsis thaliana cDNA homologue to animal poly(ADP-ribose) polymerase."
Lepiniec L., Babiychuk E., Kushnir S., van Montagu M., Inze D.
FEBS Lett. 364:103-108(1995) [PubMed: 7750552] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Ionising radiation induces the expression of PARP-1 and PARP-2 genes in Arabidopsis."
Doucet-Chabeaud G., Godon C., Brutesco C., de Murcia G., Kazmaier M.
Mol. Genet. Genomics 265:954-963(2001) [PubMed: 11523787] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z48243 mRNA. Translation: CAA88288.1.
AF069298 Genomic DNA. Translation: AAC19283.1. Sequence problems.
AL161494 Genomic DNA. Translation: CAB80732.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE82163.1.
IPIIPI00525298.
PIRT01311.
RefSeqNP_192148.2. NM_116472.3.
UniGeneAt.92.

3D structure databases

ProteinModelPortalQ11207.
SMRQ11207. Positions 3-38, 141-261, 283-635.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ11207.

Proteomic databases

PRIDEQ11207.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G02390.1; AT4G02390.1; AT4G02390.
GeneID828049.
GenomeReviewsGene locus AT4G02390 in contig CT486007_GR.
KEGGath:AT4G02390.
NMPDRfig|3702.1.peg.18049.

Organism-specific databases

GeneFarm4817. 467.
TAIRAt4g02390.

Phylogenomic databases

eggNOGKOG1037.
GeneTreeEPGT00070000029473.
HOGENOMHBG713287.
InParanoidQ11207.
OMACICDEDV.
PhylomeDBQ11207.
ProtClustDBPLN03124.

Gene expression databases

ArrayExpressQ11207.
GenevestigatorQ11207.
GermOnlineAT4G02390. Arabidopsis thaliana.

Family and domain databases

InterProIPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR003034. SAP_DNA-bd.
IPR008893. WGR_domain.
[Graphical view]
Gene3DG3DSA:1.10.720.30. G3DSA:1.10.720.30. 2 hits.
G3DSA:2.20.140.10. G3DSA:2.20.140.10. 1 hit.
G3DSA:1.20.142.10. PARP_reg. 1 hit.
KOK10798.
PfamPF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF02037. SAP. 2 hits.
PF05406. WGR. 1 hit.
[Graphical view]
SMARTSM00513. SAP. 2 hits.
SM00773. WGR. 1 hit.
[Graphical view]
SUPFAMSSF47587. PARP_reg. 1 hit.
SSF142921. SSF142921. 1 hit.
PROSITEPS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
PS50800. SAP. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePARP2_ARATH
AccessionPrimary (citable) accession number: Q11207
Secondary accession number(s): O81294
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 16, 2011
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families