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O50017 (PARP2_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:PARP
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length653 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 Potential.

Sequence similarities

Contains 1 PARP alpha-helical domain.

Contains 1 PARP catalytic domain.

Contains 2 SAP domains.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 653653Poly [ADP-ribose] polymerase 2
PRO_0000260499

Regions

Domain2 – 3635SAP 1
Domain91 – 12535SAP 2
Domain301 – 419119PARP alpha-helical
Domain427 – 653227PARP catalytic
Motif69 – 724Nuclear localization signal Potential

Sequences

Sequence LengthMass (Da)Tools
O50017 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 5FD01923C4ABCD1D

FASTA65372,995
        10         20         30         40         50         60 
MSARLRVADV RAELQRRGLD VSGTKPALVR RLDAAICEAE KAVVAAAPTS VANGYDVAVD 

        70         80         90        100        110        120 
GKRNCGNNKR KRSGDGGEEG NGDTCTDVTK LEGMSYRELQ GLAKARGVAA NGGKKDVIQR 

       130        140        150        160        170        180 
LLSATAGPAA VADGGPLGAK EVIKGGDEEV EVKKEKMVTA TKKGAAVLDQ HIPDHIKVNY 

       190        200        210        220        230        240 
HVLQVGDEIY DATLNQTNVG DNNNKFYIIQ VLESDAGGSF MVYNRWGRVG VRGQDKLHGP 

       250        260        270        280        290        300 
SPTRDQAIYE FEGKFHNKTN NHWSDRKNFK CYAKKYTWLE MDYGETEKEI EKGSITDQIK 

       310        320        330        340        350        360 
ETKLETRIAQ FISLICNISM MKQRMVEIGY NAEKLPLGKL RKATILKGYH VLKRISDVIS 

       370        380        390        400        410        420 
KADRRHLEQL TGEFYTVIPH DFGFRKMREF IIDTPQKLKA KLEMVEALGE IEIATKLLED 

       430        440        450        460        470        480 
DSSDQDDPLY ARYKQLHCDF TPLEADSDEY SMIKSYLRNT HGKTHSGYTV DIVQIFKVSR 

       490        500        510        520        530        540 
HGETERFQKF ASTRNRMLLW HGSRLSNWAG ILSQGLRIAP PEAPVTGYMF GKGVYFADMF 

       550        560        570        580        590        600 
SKSANYCYAS EACRSGVLLL CEVALGDMNE LLNADYDANN LPKGKLRSKG VGQTAPNMVE 

       610        620        630        640        650 
SKVADDGVVV PLGEPKQEPS KRGGLLYNEY IVYNVDQIRM RYVLHVNFNF KRR 

« Hide

References

[1]"Higher plants possess two structurally different poly(ADP-ribose) polymerases."
Babiychuk E., Cottrill P.B., Storozhenko S., Fuangthong M., Chen Y., O'Farrell M.K., Van Montagu M., Inze D., Kushnir S.
Plant J. 15:635-645(1998) [PubMed: 9778846] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ222588 mRNA. Translation: CAA10888.1.
PIRT03656.

3D structure databases

HSSPHSSP built from PDB template 1GS0 based on UniProtKB O88554.
ProteinModelPortalO50017.
SMRO50017. Positions 3-38.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneO50017.
MaizeGDB403201.

Phylogenomic databases

GeneTreeEPGT00070000029473.

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. 1 hit.
G3DSA:2.20.140.10. G3DSA:2.20.140.10. 1 hit.
G3DSA:1.20.142.10. PARP_reg. 1 hit.
PfamPF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF02037. SAP. 1 hit.
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_MAIZE
AccessionPrimary (citable) accession number: O50017
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: June 1, 1998
Last modified: November 16, 2011
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families