PARP1 | Poly [ADP-ribose] polymerase 1
 
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Sequence Viewer
Gene
Synonyms
ADPRT PPOL
Protein Name
Poly [ADP-ribose] polymerase 1
UniProt ID
P09874 [go to UniProt ] [go to PDBe-KB ]
Ensembl Gene ID
NCBI Gene ID
Molecular Weight
113084
Protein Length
1014
Protein Domain
3D Structure
(PDB ID : 1uk0)
Target by Small Molecules
Protein-protein Interaction Database
Gene Expression
Drugs and Diseases
Enzyme Class
2.4.2.30; (BRENDA)
Catalytic Site
Catalytic Activity
NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamideL-tyrosyl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-ribosyl)-L-tyrosyl-[protein]L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + nicotinamideL-seryl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-ribosyl)-L-seryl-[protein]
Localization
Nucleus,Nucleus,Nucleolus,Chromosome;
Function
Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:17177976, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:23230272, PubMed:25043379, PubMed:26344098). Mainly mediates glutamate and aspartate ADP-ribosylation of target proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of glutamate and aspartate residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units (PubMed:7852410, PubMed:9315851, PubMed:19764761, PubMed:25043379). Mediates the poly(ADP-ribosyl)ation of a number of proteins, including itself, APLF and CHFR (PubMed:17396150, PubMed:19764761). Also mediates serine ADP-ribosylation of target proteins following interaction with HPF1; HPF1 conferring serine specificity (PubMed:28190768). Probably also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1 (PubMed:30257210). Catalyzes the poly-ADP-ribosylation of histones in a HPF1-dependent manner (PubMed:27067600). Involved in the base excision repair (BER) pathway by catalyzing the poly-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism (PubMed:17177976, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:23230272). ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks (PubMed:17177976, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:23230272). In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair: together with TIMELESS, accumulates at DNA damage sites and promotes homologous recombination repair by mediating poly-ADP-ribosylation (PubMed:26344098, PubMed:30356214). In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively (PubMed:27471034). Required for PARP9 and DTX3L recruitment to DNA damage sites (PubMed:23230272). PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (PubMed:23230272). Acts as a regulator of transcription: positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150 (PubMed:19344625). With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production (PubMed:17177976). Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257).
Gene Ontology
GO:0016020; GO:0005739; GO:0000784; GO:0005635; GO:0005730; GO:0005654; GO:0005634; GO:0032991; GO:0032993; GO:0090734; GO:0035861; GO:0005667; GO:0003677; GO:0001228; GO:0019899; GO:0030331; GO:0042826; GO:0042802; GO:0051287; GO:0140294; GO:0003950; GO:1990404; GO:0019901; GO:0047485; GO:0070412; GO:0003723; GO:0000977; GO:0008134; GO:0008270; GO:0006915; GO:1990966; GO:1904646; GO:0006974; GO:0032869; GO:0034599; GO:0034644; GO:0071294; GO:0030592; GO:0042769; GO:0006281; GO:0006302; GO:0000724; GO:0070911; GO:0030225; GO:0032042; GO:0043504; GO:0007005; GO:2001170; GO:1904357; GO:0000122; GO:0000715; GO:0033683; GO:0006296; GO:0006294; GO:0006293; GO:0018424; GO:0018312; GO:0010613; GO:1905168; GO:0033148; GO:0051901; GO:1904762; GO:1901216; GO:1900182; GO:1903518; GO:0060391; GO:0045944; GO:2000679; GO:0006471; GO:0070213; GO:0016540; GO:0036211; GO:0070212; GO:0050790; GO:1903827; GO:0044030; GO:1903376; GO:0010990; GO:1904044; GO:0010332; GO:0023019; GO:0000723; GO:0006366; GO:0007179
 
Gene Ontology