PARP1
UniProt ID: P09874
Entrez ID: 142
Protein name: Poly [ADP-ribose] polymerase 1 (PARP-1) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 1) (ARTD1) (DNA ADP-ribosyltransferase PARP1) (EC 2.4.2.-) (NAD(+) ADP-ribosyltransferase 1) (ADPRT 1) (Poly[ADP-ribose] synthase 1) (Protein poly-ADP-ribosyltransferase PARP1) (EC 2.4.2.-)
External links: UniprotKB HGNC RefSeq COSMIC
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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:21680843, PubMed:23230272, PubMed:25043379, PubMed:33186521, PubMed:32028527, PubMed:26344098). Mediate...
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:21680843, PubMed:23230272, PubMed:25043379, PubMed:33186521, PubMed:32028527, PubMed:26344098). Mediates glutamate, aspartate, serine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target 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, PubMed:28190768, PubMed:29954836). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:33186521). Mainly mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1 (PubMed:19764761, PubMed:25043379). Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP1 active site (PubMed:28190768, PubMed:29954836, PubMed:33186521, PubMed:32028527). Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1 (PubMed:30257210, PubMed:29954836). PARP1 initiates the repair of DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (PubMed:17177976, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:23230272, PubMed:27067600). 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). Mediates the poly(ADP-ribosyl)ation of a number of proteins, including itself, APLF and CHFR (PubMed:17396150, PubMed:19764761). 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). Plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and EEF1A1 (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). {ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:17396150, ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:19344625, ECO:0000269|PubMed:19661379, ECO:0000269|PubMed:19764761, ECO:0000269|PubMed:21680843, ECO:0000269|PubMed:23230272, ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:26344098, ECO:0000269|PubMed:27067600, ECO:0000269|PubMed:27257257, ECO:0000269|PubMed:27471034, ECO:0000269|PubMed:28190768, ECO:0000269|PubMed:29954836, ECO:0000269|PubMed:30257210, ECO:0000269|PubMed:30356214, ECO:0000269|PubMed:32028527, ECO:0000269|PubMed:33186521, ECO:0000269|PubMed:7852410, ECO:0000269|PubMed:9315851}.
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GO - Biological processes (BP):
apoptotic process [GO:0006915]; ATP generation from poly-ADP-D-ribose [GO:1990966]; cellular response to amyloid-beta [GO:1904646]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to insulin stimulus [GO:0032869]; cellular response to oxidative stress [GO:0034599]; cellular ...
apoptotic process [GO:0006915]; ATP generation from poly-ADP-D-ribose [GO:1990966]; cellular response to amyloid-beta [GO:1904646]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to insulin stimulus [GO:0032869]; cellular response to oxidative stress [GO:0034599]; cellular response to UV [GO:0034644]; cellular response to zinc ion [GO:0071294]; DNA ADP-ribosylation [GO:0030592]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; macrophage differentiation [GO:0030225]; mitochondrial DNA metabolic process [GO:0032042]; mitochondrial DNA repair [GO:0043504]; mitochondrion organization [GO:0007005]; negative regulation of ATP biosynthetic process [GO:2001170]; negative regulation of telomere maintenance via telomere lengthening [GO:1904357]; negative regulation of transcription by RNA polymerase II [GO:0000122]; peptidyl-glutamic acid poly-ADP-ribosylation [GO:0018424]; peptidyl-serine ADP-ribosylation [GO:0018312]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of intracellular estrogen receptor signaling pathway [GO:0033148]; positive regulation of mitochondrial depolarization [GO:0051901]; positive regulation of myofibroblast differentiation [GO:1904762]; positive regulation of neuron death [GO:1901216]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of single strand break repair [GO:1903518]; positive regulation of SMAD protein signal transduction [GO:0060391]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription regulatory region DNA binding [GO:2000679]; protein ADP-ribosylation [GO:0006471]; protein auto-ADP-ribosylation [GO:0070213]; protein autoprocessing [GO:0016540]; protein modification process [GO:0036211]; protein poly-ADP-ribosylation [GO:0070212]; regulation of catalytic activity [GO:0050790]; regulation of DNA methylation [GO:0044030]; regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway [GO:1903376]; regulation of protein localization [GO:0032880]; regulation of SMAD protein complex assembly [GO:0010990]; response to aldosterone [GO:1904044]; response to gamma radiation [GO:0010332]; signal transduction involved in regulation of gene expression [GO:0023019]; telomere maintenance [GO:0000723]; transcription by RNA polymerase II [GO:0006366]; transforming growth factor beta receptor signaling pathway [GO:0007179]
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GO - Molecular function (MF):
DNA binding [GO:0003677]; enzyme binding [GO:0019899]; estrogen receptor binding [GO:0030331]; histone deacetylase binding [GO:0042826]; identical protein binding [GO:0042802]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD binding [GO:0051287]; NAD DNA ADP-ribosyltransferase activity [GO:01...
DNA binding [GO:0003677]; enzyme binding [GO:0019899]; estrogen receptor binding [GO:0030331]; histone deacetylase binding [GO:0042826]; identical protein binding [GO:0042802]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD binding [GO:0051287]; NAD DNA ADP-ribosyltransferase activity [GO:0140294]; protein ADP-ribosylase activity [GO:1990404]; protein kinase binding [GO:0019901]; protein N-terminus binding [GO:0047485]; RNA binding [GO:0003723]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; R-SMAD binding [GO:0070412]; zinc ion binding [GO:0008270]
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GO - Cellular component (CC):
chromosome, telomeric region [GO:0000781]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear body [GO:0016604]; nuclear envelope [GO:0005635]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; protein-DNA complex [GO:0032993]; s...
chromosome, telomeric region [GO:0000781]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear body [GO:0016604]; nuclear envelope [GO:0005635]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; protein-DNA complex [GO:0032993]; site of DNA damage [GO:0090734]; site of double-strand break [GO:0035861]; transcription regulator complex [GO:0005667]
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PARP1
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*NOTE: the Kaplan plots were collected from OncoLnc