Cell Senescence Entries for PARP1

Cell Types
Colon cancer, Embryonic kidney
Cell Lines
HCT116, HEK293T
Cancer Cell?
Yes
Method
Knockout
Type of senescence
Unclear
Senescence Effect
Inhibits
Primary Reference
Ghosh et al. (2018) PARP1 depletion induces RIG-I-dependent signaling in human cancer cells. PLoS One 13(3)e0194611 (PubMed)

PARP1 Gene Information

HGNC symbol
PARP1 
Aliases
ADPRT; ARTD1; PARP; PPOL 
Common name
poly(ADP-ribose) polymerase 1 
Entrez Id
142
Description
This gene encodes a chromatin-associated enzyme, poly(ADP-ribosyl)transferase, which modifies various nuclear proteins by poly(ADP-ribosyl)ation. The modification is dependent on DNA and is involved in the regulation of various important cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage. In addition, this enzyme may be the site of mutation in Fanconi anemia, and may participate in the pathophysiology of type I diabetes. [provided by RefSeq, Jul 2008].

PARP1 Ontologies

Gene Ontology
Process: GO:6915; apoptotic process
GO:6281; DNA repair
GO:6974; cellular response to DNA damage stimulus
GO:6471; protein ADP-ribosylation
GO:6302; double-strand break repair
GO:7179; transforming growth factor beta receptor signaling pathway
GO:10332; response to gamma radiation
GO:10613; positive regulation of cardiac muscle hypertrophy
GO:10990; regulation of SMAD protein complex assembly
GO:16540; protein autoprocessing
GO:23019; signal transduction involved in regulation of gene expression
GO:33148; positive regulation of intracellular estrogen receptor signaling pathway
GO:44030; regulation of DNA methylation
GO:45944; positive regulation of transcription by RNA polymerase II
GO:51901; positive regulation of mitochondrial depolarization
GO:60391; positive regulation of SMAD protein signal transduction
GO:70212; protein poly-ADP-ribosylation
GO:71294; cellular response to zinc ion
GO:71560; cellular response to transforming growth factor beta stimulus
GO:1900182; positive regulation of protein localization to nucleus
GO:1901216; positive regulation of neuron death
GO:1903376; regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
GO:1904044; response to aldosterone
GO:1904646; cellular response to amyloid-beta
GO:1904762; positive regulation of myofibroblast differentiation
GO:2000679; positive regulation of transcription regulatory region DNA binding
GO:1905168; positive regulation of double-strand break repair via homologous recombination
GO:6366; transcription by RNA polymerase II
GO:32869; cellular response to insulin stimulus
GO:34644; cellular response to UV
GO:7005; mitochondrion organization
GO:32880; regulation of protein localization
GO:723; telomere maintenance
GO:70213; protein auto-ADP-ribosylation
GO:1904357; negative regulation of telomere maintenance via telomere lengthening
GO:30225; macrophage differentiation
GO:32042; mitochondrial DNA metabolic process
GO:34599; cellular response to oxidative stress
GO:36211; protein modification process
GO:43504; mitochondrial DNA repair
GO:122; negative regulation of transcription by RNA polymerase II
GO:18312; peptidyl-serine ADP-ribosylation
GO:18424; peptidyl-glutamic acid poly-ADP-ribosylation
GO:30592; DNA ADP-ribosylation
GO:50790; regulation of catalytic activity
GO:1903518; positive regulation of single strand break repair
GO:1990966; ATP generation from poly-ADP-D-ribose
GO:2001170; negative regulation of ATP biosynthetic process
Cellular component: GO:781; chromosome, telomeric region
GO:5634; nucleus
GO:16020; membrane
GO:5654; nucleoplasm
GO:5730; nucleolus
GO:5635; nuclear envelope
GO:5694; chromosome
GO:16604; nuclear body
GO:43229; intracellular organelle
GO:5737; cytoplasm
GO:35861; site of double-strand break
GO:32991; protein-containing complex
GO:5667; transcription regulator complex
GO:5739; mitochondrion
GO:32993; protein-DNA complex
GO:90734; site of DNA damage
Function: GO:5515; protein binding
GO:3723; RNA binding
GO:8270; zinc ion binding
GO:46872; metal ion binding
GO:16740; transferase activity
GO:3677; DNA binding
GO:16757; glycosyltransferase activity
GO:51287; NAD binding
GO:3950; NAD+ ADP-ribosyltransferase activity
GO:19899; enzyme binding
GO:30331; estrogen receptor binding
GO:42826; histone deacetylase binding
GO:46332; SMAD binding
GO:70412; R-SMAD binding
GO:42802; identical protein binding
GO:19901; protein kinase binding
GO:47485; protein N-terminus binding
GO:61629; RNA polymerase II-specific DNA-binding transcription factor binding
GO:1990404; protein ADP-ribosylase activity
GO:140294; NAD DNA ADP-ribosyltransferase activity
Hide GO terms

Homologs of PARP1 in Model Organisms

Caenorhabditis elegans
pme-1
Danio rerio
parp1
Drosophila melanogaster
Parp
Mus musculus
Parp1
Rattus norvegicus
Parp1

In other databases

GenAge model organism genes
  • A homolog of this gene for Caenorhabditis elegans is present as pme-1
GenAge human genes
  • This gene is present as PARP1
LongevityMap
  • This gene is present as PARP1
CellAge gene expression
  • This gene is present as PARP1

External links

OMIM
173870
Ensembl
ENSG00000143799
Entrez Gene
142
UniGene
177766
1000 Genomes
1000 Genomes
HPRD
GenAtlas
PARP1
GeneCards
PARP1