PARP1: 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. Mediates the poly(ADP- ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. 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. Component of a base excision repair (BER) complex, containing at least XRCC1, PARP2, POLB and LRIG3. Homo- and heterodimer with PARP2. Interacts with PARP3, APTX and SRY. The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with TIAM2 and ZNF423. Interacts (when poly-ADP- ribosylated) with CHD1L. Interacts with the DNA polymerase alpha catalytic subunit POLA1; this interaction functions as part of the control of replication fork progression. Interacts with EEF1A1, RNF4 and TXK.
Protein type: DNA repair, damage; EC 2.4.2.30; Nuclear envelope; Nuclear receptor co-regulator; Nucleolus; Transferase
Chromosomal Location of Human Ortholog: 1q42.12
Cellular Component: membrane; mitochondrion; nuclear chromosome, telomeric region; nuclear envelope; nucleolus; nucleoplasm; nucleus; protein complex; transcription factor complex
Molecular Function: DNA binding; DNA ligase (ATP) activity; enzyme binding; estrogen receptor binding; histone deacetylase binding; identical protein binding; NAD binding; NAD+ ADP-ribosyltransferase activity; protein ADP-ribosylase activity; protein binding; protein kinase binding; protein N-terminus binding; R-SMAD binding; RNA binding; transcription factor binding; zinc ion binding
Biological Process: apoptosis; ATP generation from poly-ADP-D-ribose; cellular response to amyloid-beta; cellular response to DNA damage stimulus; cellular response to insulin stimulus; cellular response to oxidative stress; cellular response to zinc ion; DNA damage response, detection of DNA damage; DNA ligation involved in DNA repair; DNA repair; double-strand break repair; double-strand break repair via homologous recombination; lagging strand elongation; macrophage differentiation; mitochondrial DNA metabolic process; mitochondrial DNA repair; mitochondrion organization; negative regulation of ATP biosynthetic process; negative regulation of telomere maintenance via telomere lengthening; negative regulation of transcription from RNA polymerase II promoter; nucleotide-excision repair, DNA damage recognition; nucleotide-excision repair, DNA duplex unwinding; nucleotide-excision repair, DNA incision; nucleotide-excision repair, DNA incision, 3'-to lesion; nucleotide-excision repair, DNA incision, 5'-to lesion; nucleotide-excision repair, preincision complex assembly; nucleotide-excision repair, preincision complex stabilization; peptidyl-serine ADP-ribosylation; positive regulation of cardiac muscle hypertrophy; positive regulation of intracellular estrogen receptor signaling pathway; positive regulation of mitochondrial depolarization; positive regulation of myofibroblast differentiation; positive regulation of neuron death; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription regulatory region DNA binding; protein ADP-ribosylation; protein autoprocessing; regulation of catalytic activity; regulation of SMAD protein complex assembly; response to aldosterone; response to gamma radiation; telomere maintenance; transcription from RNA polymerase II promoter; transforming growth factor beta receptor signaling pathway
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