Details for: PARP1

Gene ID: 142

Symbol: PARP1

Ensembl ID: ENSG00000143799

Description: poly(ADP-ribose) polymerase 1

Associated with

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: polychromatophilic erythroblast (CL0000550)
    Fold Change: 284.8046
    Cell Significance Index: -44.3000
  • Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
    Fold Change: 121.7063
    Cell Significance Index: -30.8700
  • Cell Name: mucosal type mast cell (CL0000485)
    Fold Change: 119.7764
    Cell Significance Index: -48.6600
  • Cell Name: embryonic stem cell (CL0002322)
    Fold Change: 119.1899
    Cell Significance Index: -49.1000
  • Cell Name: smooth muscle fiber of ileum (CL1000278)
    Fold Change: 117.3636
    Cell Significance Index: -55.4100
  • Cell Name: peripheral blood mononuclear cell (CL2000001)
    Fold Change: 106.6710
    Cell Significance Index: -54.8700
  • Cell Name: ileal goblet cell (CL1000326)
    Fold Change: 82.7842
    Cell Significance Index: -55.5500
  • Cell Name: ciliated cell of the bronchus (CL0002332)
    Fold Change: 51.3646
    Cell Significance Index: -49.0400
  • Cell Name: orthochromatic erythroblast (CL0000552)
    Fold Change: 42.0696
    Cell Significance Index: -51.8700
  • Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
    Fold Change: 16.7310
    Cell Significance Index: -44.8200
  • Cell Name: stromal cell of bone marrow (CL0010001)
    Fold Change: 13.6086
    Cell Significance Index: -53.7000
  • Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
    Fold Change: 12.9255
    Cell Significance Index: -39.7000
  • Cell Name: epidermal Langerhans cell (CL0002457)
    Fold Change: 8.6586
    Cell Significance Index: -18.9500
  • Cell Name: centroblast (CL0009112)
    Fold Change: 7.0551
    Cell Significance Index: 16.4600
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: 4.4580
    Cell Significance Index: 525.7300
  • Cell Name: germ cell (CL0000586)
    Fold Change: 3.2878
    Cell Significance Index: 24.8300
  • Cell Name: microfold cell of epithelium of small intestine (CL1000353)
    Fold Change: 3.2763
    Cell Significance Index: 226.5700
  • Cell Name: early pro-B cell (CL0002046)
    Fold Change: 3.0793
    Cell Significance Index: 198.6600
  • Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
    Fold Change: 2.4550
    Cell Significance Index: 85.3100
  • Cell Name: skeletal muscle myoblast (CL0000515)
    Fold Change: 2.3272
    Cell Significance Index: 25.3000
  • Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
    Fold Change: 1.9068
    Cell Significance Index: 56.0000
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: 1.8455
    Cell Significance Index: 200.7400
  • Cell Name: tuft cell of colon (CL0009041)
    Fold Change: 1.4538
    Cell Significance Index: 1312.6700
  • Cell Name: granulosa cell (CL0000501)
    Fold Change: 1.4204
    Cell Significance Index: 37.3500
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 1.2594
    Cell Significance Index: 249.9300
  • Cell Name: basal cell of urothelium (CL1000486)
    Fold Change: 1.1598
    Cell Significance Index: 142.6100
  • Cell Name: intermediate cell of urothelium (CL4030055)
    Fold Change: 0.9774
    Cell Significance Index: 176.2000
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: 0.9350
    Cell Significance Index: 510.6500
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: 0.8557
    Cell Significance Index: 171.6500
  • Cell Name: eye photoreceptor cell (CL0000287)
    Fold Change: 0.7546
    Cell Significance Index: 47.5600
  • Cell Name: retinal progenitor cell (CL0002672)
    Fold Change: 0.7255
    Cell Significance Index: 40.7100
  • Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
    Fold Change: 0.6879
    Cell Significance Index: 51.2700
  • Cell Name: stromal cell of ovary (CL0002132)
    Fold Change: 0.6181
    Cell Significance Index: 84.8800
  • Cell Name: conjunctival epithelial cell (CL1000432)
    Fold Change: 0.6149
    Cell Significance Index: 8.3900
  • Cell Name: glycinergic neuron (CL1001509)
    Fold Change: 0.6029
    Cell Significance Index: 31.6600
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: 0.5701
    Cell Significance Index: 26.5800
  • Cell Name: basal cell of prostate epithelium (CL0002341)
    Fold Change: 0.5371
    Cell Significance Index: 14.6200
  • Cell Name: placental villous trophoblast (CL2000060)
    Fold Change: 0.5026
    Cell Significance Index: 13.4200
  • Cell Name: neutrophil progenitor cell (CL0000834)
    Fold Change: 0.4675
    Cell Significance Index: 12.5100
  • Cell Name: hair follicular keratinocyte (CL2000092)
    Fold Change: 0.4592
    Cell Significance Index: 203.0200
  • Cell Name: enteroendocrine cell of colon (CL0009042)
    Fold Change: 0.4246
    Cell Significance Index: 80.8100
  • Cell Name: fibroblast of dermis (CL0002551)
    Fold Change: 0.4240
    Cell Significance Index: 8.8800
  • Cell Name: odontoblast (CL0000060)
    Fold Change: 0.3722
    Cell Significance Index: 47.7100
  • Cell Name: pancreatic acinar cell (CL0002064)
    Fold Change: 0.3719
    Cell Significance Index: 63.5000
  • Cell Name: peg cell (CL4033014)
    Fold Change: 0.3718
    Cell Significance Index: 8.5900
  • Cell Name: colon goblet cell (CL0009039)
    Fold Change: 0.2799
    Cell Significance Index: 27.6900
  • Cell Name: GABAergic interneuron (CL0011005)
    Fold Change: 0.2766
    Cell Significance Index: 191.3000
  • Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: 0.2677
    Cell Significance Index: 96.0100
  • Cell Name: paneth cell of epithelium of small intestine (CL1000343)
    Fold Change: 0.2313
    Cell Significance Index: 5.0100
  • Cell Name: lactocyte (CL0002325)
    Fold Change: 0.2251
    Cell Significance Index: 29.0800
  • Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
    Fold Change: 0.1620
    Cell Significance Index: 7.6200
  • Cell Name: forebrain neuroblast (CL1000042)
    Fold Change: 0.1575
    Cell Significance Index: 9.6800
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: 0.1565
    Cell Significance Index: 8.1300
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: 0.1185
    Cell Significance Index: 6.1700
  • Cell Name: epithelial cell of small intestine (CL0002254)
    Fold Change: 0.0762
    Cell Significance Index: 12.4000
  • Cell Name: sebum secreting cell (CL0000317)
    Fold Change: 0.0677
    Cell Significance Index: 4.7900
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: 0.0283
    Cell Significance Index: 2.1800
  • Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
    Fold Change: 0.0224
    Cell Significance Index: 16.4600
  • Cell Name: pulmonary alveolar epithelial cell (CL0000322)
    Fold Change: 0.0205
    Cell Significance Index: 15.5000
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: -0.0010
    Cell Significance Index: -1.8400
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: -0.0018
    Cell Significance Index: -3.4700
  • Cell Name: pancreatic PP cell (CL0002275)
    Fold Change: -0.0148
    Cell Significance Index: -9.2500
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: -0.0160
    Cell Significance Index: -24.5700
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: -0.0178
    Cell Significance Index: -8.0800
  • Cell Name: pancreatic A cell (CL0000171)
    Fold Change: -0.0256
    Cell Significance Index: -18.9700
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: -0.0303
    Cell Significance Index: -41.2600
  • Cell Name: cone retinal bipolar cell (CL0000752)
    Fold Change: -0.0350
    Cell Significance Index: -0.2700
  • Cell Name: small intestine goblet cell (CL1000495)
    Fold Change: -0.0441
    Cell Significance Index: -1.5500
  • Cell Name: mesenchymal cell (CL0008019)
    Fold Change: -0.0535
    Cell Significance Index: -0.9000
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: -0.0570
    Cell Significance Index: -36.1900
  • Cell Name: type B pancreatic cell (CL0000169)
    Fold Change: -0.0593
    Cell Significance Index: -33.4400
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: -0.0625
    Cell Significance Index: -6.3800
  • Cell Name: pancreatic D cell (CL0000173)
    Fold Change: -0.1221
    Cell Significance Index: -25.7100
  • Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
    Fold Change: -0.1310
    Cell Significance Index: -2.7900
  • Cell Name: dopaminergic neuron (CL0000700)
    Fold Change: -0.1482
    Cell Significance Index: -42.6300
  • Cell Name: kidney cell (CL1000497)
    Fold Change: -0.1653
    Cell Significance Index: -1.3200
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: -0.1691
    Cell Significance Index: -19.3700
  • Cell Name: pro-T cell (CL0000827)
    Fold Change: -0.2059
    Cell Significance Index: -5.2600
  • Cell Name: epithelial cell of stomach (CL0002178)
    Fold Change: -0.2721
    Cell Significance Index: -31.7100
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: -0.2770
    Cell Significance Index: -40.2600
  • Cell Name: hippocampal granule cell (CL0001033)
    Fold Change: -0.3154
    Cell Significance Index: -21.2100
  • Cell Name: transit amplifying cell of colon (CL0009011)
    Fold Change: -0.3338
    Cell Significance Index: -10.6900
  • Cell Name: indirect pathway medium spiny neuron (CL4023029)
    Fold Change: -0.3398
    Cell Significance Index: -15.0300
  • Cell Name: enterocyte of epithelium of small intestine (CL1000334)
    Fold Change: -0.3662
    Cell Significance Index: -10.5500
  • Cell Name: pancreatic endocrine cell (CL0008024)
    Fold Change: -0.3703
    Cell Significance Index: -42.2700
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: -0.3922
    Cell Significance Index: -10.9600
  • Cell Name: umbrella cell of urothelium (CL4030056)
    Fold Change: -0.4317
    Cell Significance Index: -3.9800
  • Cell Name: direct pathway medium spiny neuron (CL4023026)
    Fold Change: -0.4320
    Cell Significance Index: -16.3600
  • Cell Name: retinal rod cell (CL0000604)
    Fold Change: -0.4396
    Cell Significance Index: -5.2400
  • Cell Name: endothelial cell of venule (CL1000414)
    Fold Change: -0.4657
    Cell Significance Index: -5.2900
  • Cell Name: cerebellar granule cell (CL0001031)
    Fold Change: -0.4665
    Cell Significance Index: -8.0000
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: -0.4849
    Cell Significance Index: -50.4900
  • Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
    Fold Change: -0.4973
    Cell Significance Index: -39.3900
  • Cell Name: intestinal tuft cell (CL0019032)
    Fold Change: -0.6811
    Cell Significance Index: -41.7600
  • Cell Name: enteroendocrine cell of small intestine (CL0009006)
    Fold Change: -0.8669
    Cell Significance Index: -21.6700
  • Cell Name: cortical interneuron (CL0008031)
    Fold Change: -0.8819
    Cell Significance Index: -21.1500
  • Cell Name: skeletal muscle fiber (CL0008002)
    Fold Change: -1.0453
    Cell Significance Index: -26.8700
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: -1.0583
    Cell Significance Index: -47.9700
  • Cell Name: fibro/adipogenic progenitor cell (CL0009099)
    Fold Change: -1.1323
    Cell Significance Index: -57.2200
  • Cell Name: kidney epithelial cell (CL0002518)
    Fold Change: -1.1849
    Cell Significance Index: -34.9000

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Other Information

**Key Characteristics:** 1. **DNA Repair:** PARP1 is a crucial enzyme in the repair of DNA damage, particularly single-strand breaks and base modifications. 2. **Poly(ADP-ribosylation):** PARP1 catalyzes the transfer of ADP-ribose units from NAD+ to target proteins, leading to the formation of poly(ADP-ribose) chains. 3. **Metabolic Functions:** PARP1 is involved in the regulation of metabolism, including the synthesis of fatty acids and the degradation of reactive oxygen species (ROS). 4. **Immune Response:** PARP1 plays a role in the regulation of immune responses, including the activation of T cells and the production of cytokines. 5. **Cell Cycle Regulation:** PARP1 is involved in the regulation of cell cycle progression, particularly during the G2/M phase. **Pathways and Functions:** 1. **Apoptotic Process:** PARP1 is involved in the regulation of apoptosis, particularly in response to DNA damage. 2. **Base Excision Repair (BER):** PARP1 is a key enzyme in the BER pathway, which corrects damage to individual DNA bases. 3. **Chromatin Binding:** PARP1 binds to chromatin, regulating the expression of target genes. 4. **DNA Damage Response:** PARP1 is involved in the regulation of DNA damage response, including the activation of DNA repair pathways. 5. **Innate Immune Response:** PARP1 plays a role in the regulation of innate immune responses, including the activation of pattern recognition receptors. **Clinical Significance:** 1. **Cancer:** PARP1 dysregulation has been linked to several types of cancer, including breast, ovarian, and prostate cancer. 2. **Autoimmune Disorders:** PARP1 dysregulation has been implicated in autoimmune disorders, including systemic lupus erythematosus and rheumatoid arthritis. 3. **Neurodegenerative Diseases:** PARP1 dysregulation has been linked to neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease. 4. **Infectious Diseases:** PARP1 plays a role in the regulation of immune responses to infectious diseases, including viral and bacterial infections. In conclusion, PARP1 is a multifunctional enzyme that plays a crucial role in various cellular processes, including DNA repair, metabolism, and immune response. Its dysregulation has been linked to several diseases, highlighting the importance of PARP1 in maintaining cellular homeostasis. Further research is needed to fully understand the complex role of PARP1 in human disease.

Genular Protein ID: 1577874424

Symbol: PARP1_HUMAN

Name: Poly[ADP-ribose] synthase 1

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 3120710

Title: Nucleotide sequence of a full-length cDNA for human fibroblast poly(ADP-ribose) polymerase.

PubMed ID: 3120710

DOI: 10.1016/0006-291x(87)90921-1

PubMed ID: 2824474

Title: Primary structure of human poly(ADP-ribose) synthetase as deduced from cDNA sequence.

PubMed ID: 2824474

DOI: 10.1016/s0021-9258(18)47687-9

PubMed ID: 2891139

Title: cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase.

PubMed ID: 2891139

DOI: 10.1073/pnas.84.23.8370

PubMed ID: 2513174

Title: Human nuclear NAD+ ADP-ribosyltransferase(polymerizing): organization of the gene.

PubMed ID: 2513174

DOI: 10.1089/dna.1989.8.575

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 2125269

Title: Human poly(ADP-ribose) polymerase gene. Cloning of the promoter region.

PubMed ID: 2125269

DOI: 10.1111/j.1432-1033.1990.tb15647.x

PubMed ID: 2108670

Title: Characterization of a putative promoter region of the human poly(ADP-ribose) polymerase gene: structural similarity to that of the DNA polymerase beta gene.

PubMed ID: 2108670

DOI: 10.1016/0006-291x(90)92082-b

PubMed ID: 17177976

Title: Txk, a member of the non-receptor tyrosine kinase of the Tec family, forms a complex with poly(ADP-ribose) polymerase 1 and elongation factor 1alpha and regulates interferon-gamma gene transcription in Th1 cells.

PubMed ID: 17177976

DOI: 10.1111/j.1365-2249.2006.03249.x

PubMed ID: 3121332

Title: Isolation of a cDNA clone for human NAD+: protein ADP-ribosyltransferase.

PubMed ID: 3121332

PubMed ID: 3113420

Title: Molecular cloning of cDNA for human poly(ADP-ribose) polymerase and expression of its gene during HL-60 cell differentiation.

PubMed ID: 3113420

DOI: 10.1016/0006-291x(87)90543-2

PubMed ID: 2109322

Title: The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA.

PubMed ID: 2109322

DOI: 10.1073/pnas.87.8.2990

PubMed ID: 2123876

Title: The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA.

PubMed ID: 2123876

DOI: 10.1016/s0021-9258(18)45824-3

PubMed ID: 2121735

Title: Expression and site-directed mutagenesis of the catalytic domain of human poly(ADP-ribose)polymerase in Escherichia coli. Lysine 893 is critical for activity.

PubMed ID: 2121735

DOI: 10.1016/s0021-9258(17)30651-8

PubMed ID: 1505517

Title: The human poly(ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity.

PubMed ID: 1505517

DOI: 10.1002/j.1460-2075.1992.tb05404.x

PubMed ID: 7852410

Title: Role of glutamic acid 988 of human poly-ADP-ribose polymerase in polymer formation. Evidence for active site similarities to the ADP-ribosylating toxins.

PubMed ID: 7852410

DOI: 10.1074/jbc.270.7.3247

PubMed ID: 7596430

Title: Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis.

PubMed ID: 7596430

DOI: 10.1038/376037a0

PubMed ID: 9315851

Title: Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching.

PubMed ID: 9315851

DOI: 10.1021/bi971055p

PubMed ID: 9721847

Title: Irreversible binding of poly(ADP)ribose polymerase cleavage product to DNA ends revealed by atomic force microscopy: possible role in apoptosis.

PubMed ID: 9721847

PubMed ID: 9518481

Title: Functional association of poly(ADP-ribose) polymerase with DNA polymerase alpha-primase complex: a link between DNA strand break detection and DNA replication.

PubMed ID: 9518481

DOI: 10.1093/nar/26.8.1891

PubMed ID: 10497198

Title: Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7.

PubMed ID: 10497198

DOI: 10.1074/jbc.274.40.28379

PubMed ID: 10467406

Title: Suppression of the poly(ADP-ribose) polymerase activity by DNA-dependent protein kinase in vitro.

PubMed ID: 10467406

DOI: 10.1038/sj.onc.1202823

PubMed ID: 15607977

Title: NAD+-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1.

PubMed ID: 15607977

DOI: 10.1016/j.cell.2004.11.002

PubMed ID: 15044383

Title: Aprataxin, a novel protein that protects against genotoxic stress.

PubMed ID: 15044383

DOI: 10.1093/hmg/ddh122

PubMed ID: 16374543

Title: Nuclear caspase-3 and caspase-7 activation, and poly(ADP-ribose) polymerase cleavage are early events in camptothecin-induced apoptosis.

PubMed ID: 16374543

DOI: 10.1007/s10495-005-3276-y

PubMed ID: 16904257

Title: The poly(ADP-ribose) polymerase 1 interacts with Sry and modulates its biological functions.

PubMed ID: 16904257

DOI: 10.1016/j.mce.2006.06.008

PubMed ID: 17396150

Title: A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses.

PubMed ID: 17396150

DOI: 10.1038/sj.emboj.7601663

PubMed ID: 17525332

Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.

PubMed ID: 17525332

DOI: 10.1126/science.1140321

PubMed ID: 18172500

Title: Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins.

PubMed ID: 18172500

DOI: 10.1038/nature06420

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19344625

Title: Poly(ADP-ribose) polymerase-1 (PARP-1) transcriptionally regulates angiotensin AT2 receptor (AT2R) and AT2R binding protein (ATBP) genes.

PubMed ID: 19344625

DOI: 10.1016/j.bcp.2009.02.025

PubMed ID: 19779455

Title: PARP-1 transcriptional activity is regulated by sumoylation upon heat shock.

PubMed ID: 19779455

DOI: 10.1038/emboj.2009.279

PubMed ID: 19764761

Title: Identification of the ADP-ribosylation sites in the PARP-1 automodification domain: analysis and implications.

PubMed ID: 19764761

DOI: 10.1021/ja906135d

PubMed ID: 19710015

Title: The metastasis efficiency modifier ribosomal RNA processing 1 homolog B (RRP1B) is a chromatin-associated factor.

PubMed ID: 19710015

DOI: 10.1074/jbc.m109.023457

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19661379

Title: Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1.

PubMed ID: 19661379

DOI: 10.1126/science.1177321

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20064938

Title: PARP-3 is a mono-ADP-ribosylase that activates PARP-1 in the absence of DNA.

PubMed ID: 20064938

DOI: 10.1074/jbc.m109.077834

PubMed ID: 20388712

Title: The Zn3 domain of human poly(ADP-ribose) polymerase-1 (PARP-1) functions in both DNA-dependent poly(ADP-ribose) synthesis activity and chromatin compaction.

PubMed ID: 20388712

DOI: 10.1074/jbc.m110.105668

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 20106667

Title: Toward a unified nomenclature for mammalian ADP-ribosyltransferases.

PubMed ID: 20106667

DOI: 10.1016/j.tibs.2009.12.003

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21266351

Title: hPuf-A/KIAA0020 modulates PARP-1 cleavage upon genotoxic stress.

PubMed ID: 21266351

DOI: 10.1158/0008-5472.can-10-1831

PubMed ID: 21577210

Title: Poly(ADP-ribose)-dependent regulation of Snail1 protein stability.

PubMed ID: 21577210

DOI: 10.1038/onc.2011.153

PubMed ID: 21799911

Title: Ubiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt signaling.

PubMed ID: 21799911

DOI: 10.1371/journal.pone.0022595

PubMed ID: 21680843

Title: SIRT6 promotes DNA repair under stress by activating PARP1.

PubMed ID: 21680843

DOI: 10.1126/science.1202723

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23213405

Title: Taperin (c9orf75), a mutated gene in nonsyndromic deafness, encodes a vertebrate specific, nuclear localized protein phosphatase one alpha (PP1alpha) docking protein.

PubMed ID: 23213405

DOI: 10.1242/bio.2011049

PubMed ID: 22863007

Title: Exome capture reveals ZNF423 and CEP164 mutations, linking renal ciliopathies to DNA damage response signaling.

PubMed ID: 22863007

DOI: 10.1016/j.cell.2012.06.028

PubMed ID: 22300411

Title: Suppressive regulation of KSHV RTA with O-GlcNAcylation.

PubMed ID: 22300411

DOI: 10.1186/1423-0127-19-12

PubMed ID: 22464733

Title: Inflammasome-activated caspase 7 cleaves PARP1 to enhance the expression of a subset of NF-kappaB target genes.

PubMed ID: 22464733

DOI: 10.1016/j.molcel.2012.02.016

PubMed ID: 22002106

Title: Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization.

PubMed ID: 22002106

DOI: 10.1074/mcp.m111.013680

PubMed ID: 22451931

Title: Caspase-7 uses an exosite to promote poly(ADP ribose) polymerase 1 proteolysis.

PubMed ID: 22451931

DOI: 10.1073/pnas.1200934109

PubMed ID: 22753495

Title: Sirtuin 6 (SIRT6) rescues the decline of homologous recombination repair during replicative senescence.

PubMed ID: 22753495

DOI: 10.1073/pnas.1200583109

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23966166

Title: ZNF365 promotes stalled replication forks recovery to maintain genome stability.

PubMed ID: 23966166

DOI: 10.4161/cc.25882

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23230272

Title: BAL1 and its partner E3 ligase, BBAP, link Poly(ADP-ribose) activation, ubiquitylation, and double-strand DNA repair independent of ATM, MDC1, and RNF8.

PubMed ID: 23230272

DOI: 10.1128/mcb.00990-12

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25043379

Title: Family-wide analysis of poly(ADP-ribose) polymerase activity.

PubMed ID: 25043379

DOI: 10.1038/ncomms5426

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 24906880

Title: PARG is dispensable for recovery from transient replicative stress but required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress.

PubMed ID: 24906880

DOI: 10.1093/nar/gku505

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

PubMed ID: 25533949

Title: A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol.

PubMed ID: 25533949

DOI: 10.1038/nature14028

PubMed ID: 27067600

Title: HPF1/C4orf27 is a PARP-1-interacting protein that regulates PARP-1 ADP-ribosylation activity.

PubMed ID: 27067600

DOI: 10.1016/j.molcel.2016.03.008

PubMed ID: 27471034

Title: Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro.

PubMed ID: 27471034

DOI: 10.1093/nar/gkw675

PubMed ID: 27257257

Title: ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for chromatin remodeling.

PubMed ID: 27257257

DOI: 10.1126/science.aad9335

PubMed ID: 28190768

Title: Serine ADP-ribosylation depends on HPF1.

PubMed ID: 28190768

DOI: 10.1016/j.molcel.2017.01.003

PubMed ID: 29220653

Title: A Poly-ADP-Ribose trigger releases the auto-inhibition of a chromatin remodeling oncogene.

PubMed ID: 29220653

DOI: 10.1016/j.molcel.2017.11.019

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 30257210

Title: Interplay of histone marks with serine ADP-ribosylation.

PubMed ID: 30257210

DOI: 10.1016/j.celrep.2018.08.092

PubMed ID: 29954836

Title: Comprehensive ADP-ribosylome analysis identifies tyrosine as an ADP-ribose acceptor site.

PubMed ID: 29954836

DOI: 10.15252/embr.201745310

PubMed ID: 30356214

Title: Nuclear cGAS suppresses DNA repair and promotes tumorigenesis.

PubMed ID: 30356214

DOI: 10.1038/s41586-018-0629-6

PubMed ID: 30104678

Title: PARP2 mediates branched poly ADP-ribosylation in response to DNA damage.

PubMed ID: 30104678

DOI: 10.1038/s41467-018-05588-5

PubMed ID: 31609975

Title: KHDC3L mutation causes recurrent pregnancy loss by inducing genomic instability of human early embryonic cells.

PubMed ID: 31609975

DOI: 10.1371/journal.pbio.3000468

PubMed ID: 33186521

Title: An HPF1/PARP1-based chemical biology strategy for exploring ADP-ribosylation.

PubMed ID: 33186521

DOI: 10.1016/j.cell.2020.09.055

PubMed ID: 27568560

Title: JNK phosphorylates SIRT6 to stimulate DNA double-strand break repair in response to oxidative stress by recruiting PARP1 to DNA Breaks.

PubMed ID: 27568560

DOI: 10.1016/j.celrep.2016.08.006

PubMed ID: 27256882

Title: Chemical genetic discovery of PARP targets reveals a role for PARP-1 in transcription elongation.

PubMed ID: 27256882

DOI: 10.1126/science.aaf7865

PubMed ID: 30675909

Title: Increased PARP1-DNA binding due to autoPARylation inhibition of PARP1 on DNA rather than PARP1-DNA trapping is correlated with PARP1 inhibitor's cytotoxicity.

PubMed ID: 30675909

DOI: 10.1002/ijc.32131

PubMed ID: 31848352

Title: PARP1 exhibits enhanced association and catalytic efficiency with gammaH2A.X-nucleosome.

PubMed ID: 31848352

DOI: 10.1038/s41467-019-13641-0

PubMed ID: 31796734

Title: Barrier-to-autointegration factor 1 (Banf1) regulates poly [ADP-ribose] polymerase 1 (PARP1) activity following oxidative DNA damage.

PubMed ID: 31796734

DOI: 10.1038/s41467-019-13167-5

PubMed ID: 32844745

Title: PARP1 inhibitors trigger innate immunity via PARP1 trapping-induced DNA damage response.

PubMed ID: 32844745

DOI: 10.7554/elife.60637

PubMed ID: 32028527

Title: HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation.

PubMed ID: 32028527

DOI: 10.1038/s41586-020-2013-6

PubMed ID: 32358582

Title: Real-time monitoring of PARP1-dependent PARylation by ATR-FTIR spectroscopy.

PubMed ID: 32358582

DOI: 10.1038/s41467-020-15858-w

PubMed ID: 32315358

Title: PARP1-cGAS-NF-kappaB pathway of proinflammatory macrophage activation by extracellular vesicles released during Trypanosoma cruzi infection and Chagas disease.

PubMed ID: 32315358

DOI: 10.1371/journal.ppat.1008474

PubMed ID: 34732825

Title: Dual function of HPF1 in the modulation of PARP1 and PARP2 activities.

PubMed ID: 34732825

DOI: 10.1038/s42003-021-02780-0

PubMed ID: 34049076

Title: PARP1-mediated PARylation of TonEBP prevents R-loop-associated DNA damage.

PubMed ID: 34049076

DOI: 10.1016/j.dnarep.2021.103132

PubMed ID: 33683197

Title: HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase.

PubMed ID: 33683197

DOI: 10.7554/elife.65773

PubMed ID: 34874266

Title: Serine ADP-ribosylation marks nucleosomes for ALC1-dependent chromatin remodeling.

PubMed ID: 34874266

DOI: 10.7554/elife.71502

PubMed ID: 33168626

Title: The 89-kDa PARP1 cleavage fragment serves as a cytoplasmic PAR carrier to induce AIF-mediated apoptosis.

PubMed ID: 33168626

DOI: 10.1074/jbc.ra120.014479

PubMed ID: 33412112

Title: CARM1 regulates replication fork speed and stress response by stimulating PARP1.

PubMed ID: 33412112

DOI: 10.1016/j.molcel.2020.12.010

PubMed ID: 34102106

Title: XRCC1 prevents toxic PARP1 trapping during DNA base excision repair.

PubMed ID: 34102106

DOI: 10.1016/j.molcel.2021.05.009

PubMed ID: 34811483

Title: XRCC1 protects transcription from toxic PARP1 activity during DNA base excision repair.

PubMed ID: 34811483

DOI: 10.1038/s41556-021-00792-w

PubMed ID: 34210965

Title: Serine-linked PARP1 auto-modification controls PARP inhibitor response.

PubMed ID: 34210965

DOI: 10.1038/s41467-021-24361-9

PubMed ID: 34625544

Title: The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome.

PubMed ID: 34625544

DOI: 10.1038/s41467-021-26172-4

PubMed ID: 34737271

Title: SPINDOC binds PARP1 to facilitate PARylation.

PubMed ID: 34737271

DOI: 10.1038/s41467-021-26588-y

PubMed ID: 34795260

Title: HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications.

PubMed ID: 34795260

DOI: 10.1038/s41467-021-27043-8

PubMed ID: 34465625

Title: Multiple roles for PARP1 in ALC1-dependent nucleosome remodeling.

PubMed ID: 34465625

DOI: 10.1073/pnas.2107277118

Sequence Information:

  • Length: 1014
  • Mass: 113084
  • Checksum: 6A5FC01EB91C046B
  • Sequence:
  • MAESSDKLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH WYHFSCFWKV 
    GHSIRHPDVE VDGFSELRWD DQQKVKKTAE AGGVTGKGQD GIGSKAEKTL GDFAAEYAKS 
    NRSTCKGCME KIEKGQVRLS KKMVDPEKPQ LGMIDRWYHP GCFVKNREEL GFRPEYSASQ 
    LKGFSLLATE DKEALKKQLP GVKSEGKRKG DEVDGVDEVA KKKSKKEKDK DSKLEKALKA 
    QNDLIWNIKD ELKKVCSTND LKELLIFNKQ QVPSGESAIL DRVADGMVFG ALLPCEECSG 
    QLVFKSDAYY CTGDVTAWTK CMVKTQTPNR KEWVTPKEFR EISYLKKLKV KKQDRIFPPE 
    TSASVAATPP PSTASAPAAV NSSASADKPL SNMKILTLGK LSRNKDEVKA MIEKLGGKLT 
    GTANKASLCI STKKEVEKMN KKMEEVKEAN IRVVSEDFLQ DVSASTKSLQ ELFLAHILSP 
    WGAEVKAEPV EVVAPRGKSG AALSKKSKGQ VKEEGINKSE KRMKLTLKGG AAVDPDSGLE 
    HSAHVLEKGG KVFSATLGLV DIVKGTNSYY KLQLLEDDKE NRYWIFRSWG RVGTVIGSNK 
    LEQMPSKEDA IEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE AVKKLTVNPG 
    TKSKLPKPVQ DLIKMIFDVE SMKKAMVEYE IDLQKMPLGK LSKRQIQAAY SILSEVQQAV 
    SQGSSDSQIL DLSNRFYTLI PHDFGMKKPP LLNNADSVQA KVEMLDNLLD IEVAYSLLRG 
    GSDDSSKDPI DVNYEKLKTD IKVVDRDSEE AEIIRKYVKN THATTHNAYD LEVIDIFKIE 
    REGECQRYKP FKQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM 
    VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG LGKTTPDPSA 
    NISLDGVDVP LGTGISSGVN DTSLLYNEYI VYDIAQVNLK YLLKLKFNFK TSLW

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.