UniProt Accession

 PARP2_HUMAN; Q9UGN5; Q8TEU4; Q9NUV2; Q9UMR4; Q9Y6C8 

Genbank Protein ID

 AJ236912; AF085734; AJ236876; AK001980; AF479321 

Genbank Nucleotide ID

 CAB65088.1; AAD29857.1; CAB41505.2; BAA92017.1; AAL77437.1 

Protein Name

 Poly [ADP-ribose] polymerase 2 

Protein Synonyms/Alias

 PARP-2; hPARP-2; ADP-ribosyltransferase diphtheria toxin-like 2; ARTD2; NAD(+) ADP-ribosyltransferase 2; ADPRT-2; Poly[ADP-ribose] synthase 2; pADPRT-2 

Gene Name

 PARP2 

Gene Synonyms/Alias

 ADPRT2; ADPRTL2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
37	PEDSSPAKKTRRCQR	acetylation	[1]
38	EDSSPAKKTRRCQRQ	acetylation	[1]
276	KLTVAQIKAGYQSLK	ubiquitination	[2, 3, 4]
348	EIAIKLVKTELQSPE	ubiquitination	[2, 4]
469	YFADMSSKSANYCFA	ubiquitination	[3]
480	YCFASRLKNTGLLLL	ubiquitination	[3]

Reference

 [1] Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation.
 Haenni SS, Hassa PO, Altmeyer M, Fey M, Imhof R, Hottiger MO.
 Int J Biochem Cell Biol. 2008;40(10):2274-83. [PMID: 18436469]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 231 348 PARP alpha-helical.
 DOMAIN 356 583 PARP catalytic.
 DNA_BIND 1 88 Potential.
 MOTIF 4 7 Nuclear localization signal (Potential).
 MOTIF 35 40 Nuclear localization signal (Potential).
 MOD_RES 37 37 N6-acetyllysine (By similarity).
 MOD_RES 38 38 N6-acetyllysine (By similarity).
 MOD_RES 226 226 Phosphoserine.
 MOD_RES 232 232 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; DNA-binding; Glycosyltransferase; NAD; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 583 AA 

Protein Sequence

Gene Ontology

 GO:0005730; C:nucleolus; IDA:MGI.
 GO:0005654; C:nucleoplasm; IDA:MGI.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:EC.
 GO:0006284; P:base-excision repair; IEA:Compara.
 GO:0006281; P:DNA repair; TAS:ProtInc.
 GO:0006471; P:protein ADP-ribosylation; TAS:ProtInc. 

Interpro

 IPR012317; Poly(ADP-ribose)pol_cat_dom.
 IPR004102; Poly(ADP-ribose)pol_reg_dom.
 IPR008893; WGR_domain. 

Pfam

 PF00644; PARP
 PF02877; PARP_reg
 PF05406; WGR 

SMART

 SM00773; WGR 

PROSITE

 PS51060; PARP_ALPHA_HD
 PS51059; PARP_CATALYTIC 

PRINTS