Version 5.4
Homo sapiens Protein: PARP2
Summary
InnateDB Protein IDBP-2171.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol PARP2
Protein Name poly (ADP-ribose) polymerase 2
Synonyms ADPRT2; ADPRTL2; ADPRTL3; ARTD2; pADPRT-2; PARP-2;
Species Homo sapiens
Ensembl Protein ENSP00000250416
InnateDB Gene IDBG-2169 (PARP2)
Protein Structure
UniProt Annotation
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.
Subcellular Localization Nucleus.
Disease Associations
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.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 123 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Experimentally validated
Total 123 [view]
Protein-Protein 120 [view]
Protein-DNA 3 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003677 DNA binding
GO:0003950 NAD+ ADP-ribosyltransferase activity
GO:0005515 protein binding
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair
GO:0006471 protein ADP-ribosylation
GO:0097191 extrinsic apoptotic signaling pathway
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005730 nucleolus
Protein Structure and Domains
PDB ID
InterPro IPR004102 Poly(ADP-ribose) polymerase, regulatory domain
IPR008893 WGR domain
IPR012317 Poly(ADP-ribose) polymerase, catalytic domain
PFAM PF02877
PF05406
PF00644
PRINTS
PIRSF
SMART SM00773
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9UGN5
PhosphoSite PhosphoSite-Q9UGN5
TrEMBL G3V167
UniProt Splice Variant
Entrez Gene 10038
UniGene Hs.409412
RefSeq NP_005475
HUGO HGNC:272
OMIM 607725
CCDS CCDS41910
HPRD
IMGT
EMBL AF085734 AF479321 AJ236876 AJ236912 AK001980 AL355075 CH471078
GenPept AAD29857 AAL77437 BAA92017 CAB41505 CAB65088 EAW66476

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca