{ "uniprot_canonical_ac": "P09874-1", "uniprot_ac": "P09874", "uniprot_id": "PARP1_HUMAN", "mass": { "chemical_mass": 113084.0, "monoisotopic_mass": 113084.0 }, "refseq": { "ac": "NP_001609", "name": "poly [ADP-ribose] polymerase 1", "summary": "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].", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001609" }, "gene_names": [ { "name": "PARP1", "resource": "UniProtKB", "type": "recommended", "url": "https://www.uniprot.org/uniprot/P09874", "id": "P09874" }, { "name": "ADPRT; ADPRT 1; ADPRT1; ARTD1; pADPRT-1; PARP; PARP-1; PARS; Poly-PARP; PPOL", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001609", "id": "NP_001609" }, { "name": "ADPRT", "resource": "UniProtKB", "type": "synonym", "url": "https://www.uniprot.org/uniprot/P09874", "id": "P09874" }, { "name": "PARP1", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001609", "id": "NP_001609" }, { "name": "PPOL", "resource": "UniProtKB", "type": "synonym", "url": "https://www.uniprot.org/uniprot/P09874", "id": "P09874" } ], "protein_names": [ { "name": "Poly [ADP-ribose] polymerase 1", "resource": "UniProtKB", "type": "recommended", "url": "", "id": "P09874" }, { "name": "2.4.2.-", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P09874" }, { "name": "2.4.2.30", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P09874" }, { "name": "ADP-ribosyltransferase diphtheria toxin-like 1", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P09874" }, { "name": "ADPRT 1", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P09874" }, { "name": "ARTD1", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P09874" }, { "name": "DNA ADP-ribosyltransferase PARP1", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P09874" }, { "name": "NAD(+) ADP-ribosyltransferase 1", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P09874" }, { "name": "PARP-1", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P09874" }, { "name": "Poly [ADP-ribose] polymerase 1, 24-kDa form", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P09874" }, { "name": "Poly [ADP-ribose] polymerase 1, 28-kDa form", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P09874" }, { "name": "Poly [ADP-ribose] polymerase 1, 89-kDa form", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P09874" }, { "name": "Poly[ADP-ribose] synthase 1", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P09874" }, { "name": "Protein poly-ADP-ribosyltransferase PARP1", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P09874" }, { "name": "poly [ADP-ribose] polymerase 1", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001609", "id": "NP_001609" }, { "name": "poly(ADP-ribose) synthetase; ADP-ribosyltransferase NAD(+); poly (ADP-ribose) polymerase family, member 1; ADP-ribosyltransferase (NAD+; poly (ADP-ribose) polymerase); poly(ADP-ribosyl)transferase; poly[ADP-ribose] synthase 1; NAD(+) ADP-ribosyltransferase 1; ADP-ribosyltransferase diphtheria toxin-like 1; DNA ADP-ribosyltransferase PARP1; protein poly-ADP-ribosyltransferase PARP1", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001609", "id": "NP_001609" } ], "function": [ { "annotation": "Methyltransferase Set7/9 controls PARP1 expression and regulates cisplatin response of breast cancer cells.", "evidence": [ { "database": "RefSeq", "id": "NP_001609", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001609" }, { "database": "PubMed", "id": "38043199", "url": "https://glygen.org/publication/PubMed/38043199" } ] }, { "annotation": "Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:17177976, PubMed:18172500, PubMed:20388712, PubMed:19344625, PubMed:19661379, PubMed:21680843, PubMed:23230272, PubMed:25043379, PubMed:26344098, PubMed:32028527, PubMed:30104678, PubMed:33186521, PubMed:31796734, PubMed:32358582, PubMed:34737271, PubMed:34465625, PubMed:18055453, PubMed:22582261, PubMed:26626479, PubMed:26626480, PubMed:32241924). Mediates glutamate, aspartate, serine, histidine 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, PubMed:35393539). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:33186521, PubMed:34874266). Specificity for the different amino acids is conferred by interacting factors, such as HPF1 and NMNAT1 (PubMed:28190768, PubMed:29954836, PubMed:32028527, PubMed:33186521, PubMed:34874266, PubMed:34625544, PubMed:33589610). Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 confers serine specificity by completing the PARP1 active site (PubMed:28190768, PubMed:29954836, PubMed:32028527, PubMed:33186521, PubMed:34874266, PubMed:34625544, PubMed:33589610). Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1 (PubMed:30257210, PubMed:29954836). Following interaction with NMNAT1, catalyzes glutamate and aspartate ADP-ribosylation of target proteins; NMNAT1 confers glutamate and aspartate specificity (By similarity). 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 (H2BS6ADPr and H3S10ADPr), 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, PubMed:34874266, PubMed:34465625). HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP1 in order to limit the length of poly-ADP-ribose chains (PubMed:34732825, PubMed:33683197, PubMed:34795260). 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-ribosylation of a number of proteins, including itself, APLF, CHFR, RPA1 and NFAT5 (PubMed:17396150, PubMed:19764761, PubMed:24906880, PubMed:34049076). 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). PARP1-mediated DNA repair in neurons plays a role in sleep: senses DNA damage in neurons and promotes sleep, facilitating efficient DNA repair (By similarity). In addition to DNA repair, also involved in other processes, such as transcription regulation, programmed cell death, membrane repair, adipogenesis and innate immunity (PubMed:17177976, PubMed:19344625, PubMed:15607977, PubMed:27256882, PubMed:32844745, PubMed:32315358, PubMed:35124853, PubMed:35460603, PubMed:35393539). Acts as a repressor of transcription: binds to nucleosomes and modulates chromatin structure in a manner similar to histone H1, thereby altering RNA polymerase II (PubMed:15607977, PubMed:22464733). Acts both as a positive and negative regulator of transcription elongation, depending on the context (PubMed:27256882, PubMed:35393539). Acts as a positive regulator of transcription elongation by mediating poly-ADP-ribosylation of NELFE, preventing RNA-binding activity of NELFE and relieving transcription pausing (PubMed:27256882). Acts as a negative regulator of transcription elongation in response to DNA damage by catalyzing poly-ADP-ribosylation of CCNT1, disrupting the phase separation activity of CCNT1 and subsequent activation of CDK9 (PubMed:35393539). Involved in replication fork progression following interaction with CARM1: mediates poly-ADP-ribosylation at replication forks, slowing fork progression (PubMed:33412112). Poly-ADP-ribose chains generated by PARP1 also play a role in poly-ADP-ribose-dependent cell death, a process named parthanatos (By similarity). Also acts as a negative regulator of the cGAS-STING pathway (PubMed:32844745, PubMed:32315358, PubMed:35460603). Acts by mediating poly-ADP-ribosylation of CGAS: PARP1 translocates into the cytosol following phosphorylation by PRKDC and catalyzes poly-ADP-ribosylation and inactivation of CGAS (PubMed:35460603). Acts as a negative regulator of adipogenesis: catalyzes poly-ADP-ribosylation of histone H2B on 'Glu-35' (H2BE35ADPr) following interaction with NMNAT1, inhibiting phosphorylation of H2B at 'Ser-36' (H2BS36ph), thereby blocking expression of pro-adipogenetic genes (By similarity). 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).", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874#function" }, { "database": "PubMed", "id": "18172500", "url": "https://glygen.org/publication/PubMed/18172500" }, { "database": "PubMed", "id": "19661379", "url": "https://glygen.org/publication/PubMed/19661379" }, { "database": "PubMed", "id": "17396150", "url": "https://glygen.org/publication/PubMed/17396150" }, { "database": "PubMed", "id": "27257257", "url": "https://glygen.org/publication/PubMed/27257257" }, { "database": "PubMed", "id": "17177976", "url": "https://glygen.org/publication/PubMed/17177976" }, { "database": "PubMed", "id": "27067600", "url": "https://glygen.org/publication/PubMed/27067600" }, { "database": "PubMed", "id": "19344625", "url": "https://glygen.org/publication/PubMed/19344625" }, { "database": "UniProtKB", "id": "P11103", "url": "https://www.uniprot.org/uniprot/P11103#function" }, { "database": "PubMed", "id": "28190768", "url": "https://glygen.org/publication/PubMed/28190768" }, { "database": "PubMed", "id": "18055453", "url": "https://glygen.org/publication/PubMed/18055453" }, { "database": "PubMed", "id": "22582261", "url": "https://glygen.org/publication/PubMed/22582261" }, { "database": "PubMed", "id": "9315851", "url": "https://glygen.org/publication/PubMed/9315851" }, { "database": "PubMed", "id": "26626479", "url": "https://glygen.org/publication/PubMed/26626479" }, { "database": "PubMed", "id": "7852410", "url": "https://glygen.org/publication/PubMed/7852410" }, { "database": "PubMed", "id": "26626480", "url": "https://glygen.org/publication/PubMed/26626480" }, { "database": "PubMed", "id": "30104678", "url": "https://glygen.org/publication/PubMed/30104678" }, { "database": "PubMed", "id": "22464733", "url": "https://glygen.org/publication/PubMed/22464733" }, { "database": "PubMed", "id": "20388712", "url": "https://glygen.org/publication/PubMed/20388712" }, { "database": "PubMed", "id": "34737271", "url": "https://glygen.org/publication/PubMed/34737271" }, { "database": "PubMed", "id": "21680843", "url": "https://glygen.org/publication/PubMed/21680843" }, { "database": "PubMed", "id": "35460603", "url": "https://glygen.org/publication/PubMed/35460603" }, { "database": "PubMed", "id": "15607977", "url": "https://glygen.org/publication/PubMed/15607977" }, { "database": "PubMed", "id": "32358582", "url": "https://glygen.org/publication/PubMed/32358582" }, { "database": "PubMed", "id": "26344098", "url": "https://glygen.org/publication/PubMed/26344098" }, { "database": "PubMed", "id": "19764761", "url": "https://glygen.org/publication/PubMed/19764761" }, { "database": "PubMed", "id": "33412112", "url": "https://glygen.org/publication/PubMed/33412112" }, { "database": "PubMed", "id": "29954836", "url": "https://glygen.org/publication/PubMed/29954836" }, { "database": "PubMed", "id": "31796734", "url": "https://glygen.org/publication/PubMed/31796734" }, { "database": "PubMed", "id": "32028527", "url": "https://glygen.org/publication/PubMed/32028527" }, { "database": "PubMed", "id": "23230272", "url": "https://glygen.org/publication/PubMed/23230272" }, { "database": "PubMed", "id": "33589610", "url": "https://glygen.org/publication/PubMed/33589610" }, { "database": "PubMed", "id": "30356214", "url": "https://glygen.org/publication/PubMed/30356214" }, { "database": "PubMed", "id": "34625544", "url": "https://glygen.org/publication/PubMed/34625544" }, { "database": "PubMed", "id": "32241924", "url": "https://glygen.org/publication/PubMed/32241924" }, { "database": "PubMed", "id": "34795260", "url": "https://glygen.org/publication/PubMed/34795260" }, { "database": "PubMed", "id": "34732825", "url": "https://glygen.org/publication/PubMed/34732825" }, { "database": "PubMed", "id": "33683197", "url": "https://glygen.org/publication/PubMed/33683197" }, { "database": "PubMed", "id": "34874266", "url": "https://glygen.org/publication/PubMed/34874266" }, { "database": "PubMed", "id": "27471034", "url": "https://glygen.org/publication/PubMed/27471034" }, { "database": "PubMed", "id": "25043379", "url": "https://glygen.org/publication/PubMed/25043379" }, { "database": "PubMed", "id": "27256882", "url": "https://glygen.org/publication/PubMed/27256882" }, { "database": "PubMed", "id": "32315358", "url": "https://glygen.org/publication/PubMed/32315358" }, { "database": "PubMed", "id": "33186521", "url": "https://glygen.org/publication/PubMed/33186521" }, { "database": "PubMed", "id": "35124853", "url": "https://glygen.org/publication/PubMed/35124853" }, { "database": "PubMed", "id": "34049076", "url": "https://glygen.org/publication/PubMed/34049076" }, { "database": "PubMed", "id": "30257210", "url": "https://glygen.org/publication/PubMed/30257210" }, { "database": "PubMed", "id": "35393539", "url": "https://glygen.org/publication/PubMed/35393539" }, { "database": "PubMed", "id": "34465625", "url": "https://glygen.org/publication/PubMed/34465625" }, { "database": "PubMed", "id": "32844745", "url": "https://glygen.org/publication/PubMed/32844745" }, { "database": "PubMed", "id": "24906880", "url": "https://glygen.org/publication/PubMed/24906880" }, { "database": "UniProtKB", "id": "A0A7I2V3E1", "url": "https://www.uniprot.org/uniprot/A0A7I2V3E1#function" }, { "database": "UniProtKB", "id": "PIRNR000489", "url": "https://www.uniprot.org/uniprot/PIRNR000489#function" } ] }, { "annotation": "Promotes AIFM1-mediated apoptosis (PubMed:33168626). This form, which translocates into the cytoplasm following cleavage by caspase-3 (CASP3) and caspase-7 (CASP7) in response to apoptosis, is auto-poly-ADP-ribosylated and serves as a poly-ADP-ribose carrier to induce AIFM1-mediated apoptosis (PubMed:33168626).", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874#function" }, { "database": "PubMed", "id": "33168626", "url": "https://glygen.org/publication/PubMed/33168626" } ] }, { "annotation": "Regulatory apoptotic fragment of PARP1 complements catalytic fragment for PAR and DNA-dependent activity but inhibits DNA-induced catalytic stimulation of PARP2.", "evidence": [ { "database": "RefSeq", "id": "NP_001609", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001609" }, { "database": "PubMed", "id": "38029688", "url": "https://glygen.org/publication/PubMed/38029688" } ] }, { "annotation": "Spatiotemporal roles of AMPK in PARP-1- and autophagy-dependent retinal pigment epithelial cell death caused by UVA. Publication Status: Online-Only", "evidence": [ { "database": "RefSeq", "id": "NP_001609", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001609" }, { "database": "PubMed", "id": "37936170", "url": "https://glygen.org/publication/PubMed/37936170" } ] }, { "annotation": "This cleavage form irreversibly binds to DNA breaks and interferes with DNA repair, promoting DNA damage-induced apoptosis.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874#function" }, { "database": "PubMed", "id": "35104452", "url": "https://glygen.org/publication/PubMed/35104452" }, { "database": "UniProtKB", "id": "A0A7I2V3E1", "url": "https://www.uniprot.org/uniprot/A0A7I2V3E1#function" }, { "database": "UniProtKB", "id": "ARBA00034299", "url": "https://www.uniprot.org/uniprot/ARBA00034299#function" } ] }, { "annotation": "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].", "evidence": [ { "database": "RefSeq", "id": "NP_001609", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001609" } ] }, { "annotation": "Unraveling the allosteric inhibition mechanism of PARP-1 CAT and the D766/770A mutation effects via Gaussian accelerated molecular dynamics and Markov state model.", "evidence": [ { "database": "RefSeq", "id": "NP_001609", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001609" }, { "database": "PubMed", "id": "38000246", "url": "https://glygen.org/publication/PubMed/38000246" } ] } ], "disease": [], "snv": [ { "evidence": [ { "id": "P09874", "database": "BioMuta", "url": "https://hive.biochemistry.gwu.edu/biomuta/proteinview/P09874" } ], "glycoeffect": [], "start_pos": 762, "end_pos": 762, "subjects_tested": "0", "subjects_positive": "0", "frequency": "0.0", "sequence_org": "V", "sequence_mut": "A", "comment": "Somatic mutation passed 2 out of 6 filters: num. of cancers (3); Lit. mined (16).", "chr_id": "1", "chr_pos": "226367601", "ref_nt": "A", "alt_nt": "G", "minor_allelic_frequency": "", "site_lbl": "V762", "disease": [ { "disease_id": "DOID:1612", "recommended_name": { "id": "DOID:1612", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1612", "name": "breast cancer", "description": "A thoracic cancer that originates in the mammary gland." }, "synonyms": [ { "id": "DOID:1612", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1612", "name": "breast tumor", "description": "" }, { "id": "DOID:1612", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1612", "name": "malignant neoplasm of breast", "description": "" }, { "id": "DOID:1612", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1612", "name": "malignant tumor of the breast", "description": "" }, { "id": "DOID:1612", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1612", "name": "mammary cancer", "description": "" }, { "id": "DOID:1612", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1612", "name": "mammary tumor", "description": "" }, { "id": "DOID:1612", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1612", "name": "primary breast cancer", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "hereditary breast carcinoma", "description": "Breast carcinoma that has developed in relatives of patients with history of breast carcinoma." }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer susceptibility, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer, early-onset, susceptibility to, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer, invasive ductal, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer, lobular, somatic", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer, male, susceptibility to, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer, protection against, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer, somatic", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer, susceptibility to, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "familial breast cancer", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "familial breast carcinoma", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "familial cancer of breast", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "familial cancer of the breast", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "hereditary breast cancer", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "hereditary breast carcinoma", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer, familial", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer, familial Male", "description": "" }, { "id": "MIM:114480", "resource": "MIM", "url": "https://www.omim.org/entry/114480", "name": "Breast cancer", "description": "Breast cancer" } ] }, { "disease_id": "DOID:1324", "recommended_name": { "id": "DOID:1324", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1324", "name": "lung cancer", "description": "A respiratory system cancer that is 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Able to bind damaged DNA, however, defects in the interdomain communication prevent unfolding of the PARP alpha-helical domain, blocking catalytic activation.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "22582261", "url": "https://glygen.org/publication/PubMed/22582261" }, { "database": "PubMed", "id": "26626479", "url": "https://glygen.org/publication/PubMed/26626479" }, { "database": "PubMed", "id": "26626480", "url": "https://glygen.org/publication/PubMed/26626480" }, { "database": "PubMed", "id": "20388712", "url": "https://glygen.org/publication/PubMed/20388712" }, { "database": "PubMed", "id": "32241924", "url": "https://glygen.org/publication/PubMed/32241924" } ] }, { "start_pos": 318, "end_pos": 318, "sequence_org": "W", "sequence_mut": "F", "comment": "Does not affect auto-poly-ADP-ribosylation.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "20388712", "url": "https://glygen.org/publication/PubMed/20388712" } ] }, { "start_pos": 318, "end_pos": 318, "sequence_org": "W", "sequence_mut": "R", "comment": "Strongly reduced poly-ADP-ribosyltransferase activity. Able to bind damaged DNA, however, defects in the interdomain communication prevent unfolding of the PARP alpha-helical domain, blocking catalytic activation.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "22582261", "url": "https://glygen.org/publication/PubMed/22582261" }, { "database": "PubMed", "id": "26626479", "url": "https://glygen.org/publication/PubMed/26626479" }, { "database": "PubMed", "id": "26626480", "url": "https://glygen.org/publication/PubMed/26626480" }, { "database": "PubMed", "id": "20388712", "url": "https://glygen.org/publication/PubMed/20388712" }, { "database": "PubMed", "id": "32241924", "url": "https://glygen.org/publication/PubMed/32241924" } ] }, { "start_pos": 319, "end_pos": 319, "sequence_org": "T", "sequence_mut": "A", "comment": "Does not affect auto-poly-ADP-ribosylation.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "20388712", "url": "https://glygen.org/publication/PubMed/20388712" } ] }, { "start_pos": 320, "end_pos": 320, "sequence_org": "K", "sequence_mut": "A", "comment": "Does not affect auto-poly-ADP-ribosylation.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "20388712", "url": "https://glygen.org/publication/PubMed/20388712" } ] }, { "start_pos": 325, "end_pos": 325, "sequence_org": "T", "sequence_mut": "A", "comment": "Does not affect translocation into the cytosol.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "35460603", "url": "https://glygen.org/publication/PubMed/35460603" } ] }, { "start_pos": 348, "end_pos": 350, "sequence_org": "LKV", "sequence_mut": "DKD", "comment": "Does not affect auto-poly-ADP-ribosylation.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "20388712", "url": "https://glygen.org/publication/PubMed/20388712" } ] }, { "start_pos": 34, "end_pos": 34, "sequence_org": "R", "sequence_mut": "A", "comment": "Abolished DNA-binding.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "21233213", "url": "https://glygen.org/publication/PubMed/21233213" } ] }, { "start_pos": 34, "end_pos": 34, "sequence_org": "R", "sequence_mut": "E", "comment": "Abolished binding to DNA strand breaks.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "22683995", "url": "https://glygen.org/publication/PubMed/22683995" } ] }, { "start_pos": 357, "end_pos": 357, "sequence_org": "F", "sequence_mut": "Y", "comment": "Does not affect auto-poly-ADP-ribosylation.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "20388712", "url": "https://glygen.org/publication/PubMed/20388712" } ] }, { "start_pos": 358, "end_pos": 359, "sequence_org": "PP", "sequence_mut": "GG", "comment": "Does not affect auto-poly-ADP-ribosylation.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "20388712", "url": "https://glygen.org/publication/PubMed/20388712" } ] }, { "start_pos": 394, "end_pos": 394, "sequence_org": "K", "sequence_mut": "Q", "comment": "Strongly decreased ability of the BRCT domain to bind intact DNA; when associated with Q-418.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "34919819", "url": "https://glygen.org/publication/PubMed/34919819" } ] }, { "start_pos": 405, "end_pos": 409, "sequence_org": "KDEVK", "sequence_mut": "QDEVQ", "comment": "Strongly decreased ability of the BRCT domain to bind intact DNA.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "34919819", "url": "https://glygen.org/publication/PubMed/34919819" } ] }, { "start_pos": 40, "end_pos": 40, "sequence_org": "Q", "sequence_mut": "A", "comment": "Does not affect DNA-binding.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "21233213", "url": "https://glygen.org/publication/PubMed/21233213" } ] }, { "start_pos": 418, "end_pos": 418, "sequence_org": "K", "sequence_mut": "Q", "comment": "Strongly decreased ability of the BRCT domain to bind intact DNA; when associated with Q-394.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "34919819", "url": "https://glygen.org/publication/PubMed/34919819" } ] }, { "start_pos": 418, "end_pos": 425, "sequence_org": "KLTGTANK", "sequence_mut": "QLTGTANQ", "comment": "Strongly decreased ability of the BRCT domain to bind intact DNA.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "34919819", "url": "https://glygen.org/publication/PubMed/34919819" } ] }, { "start_pos": 41, "end_pos": 41, "sequence_org": "S", "sequence_mut": "A", "comment": "No effect.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "21233213", "url": "https://glygen.org/publication/PubMed/21233213" } ] }, { "start_pos": 42, "end_pos": 42, "sequence_org": "P", "sequence_mut": "G", "comment": "No effect.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "21233213", "url": "https://glygen.org/publication/PubMed/21233213" } ] }, { "start_pos": 43, "end_pos": 43, "sequence_org": "M", "sequence_mut": "A", "comment": "No effect.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "21233213", "url": "https://glygen.org/publication/PubMed/21233213" } ] }, { "start_pos": 43, "end_pos": 43, "sequence_org": "M", "sequence_mut": "D", "comment": "Strongly decreased homodimerization.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "22683995", "url": "https://glygen.org/publication/PubMed/22683995" } ] }, { "start_pos": 441, "end_pos": 442, "sequence_org": "KK", "sequence_mut": "QQ", "comment": "Strongly decreased ability of the BRCT domain to bind intact DNA.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "34919819", "url": "https://glygen.org/publication/PubMed/34919819" } ] }, { "start_pos": 44, "end_pos": 44, "sequence_org": "F", "sequence_mut": "A", "comment": "Abolished DNA-binding.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "21233213", "url": "https://glygen.org/publication/PubMed/21233213" } ] }, { "start_pos": 44, "end_pos": 44, "sequence_org": "F", "sequence_mut": "D", "comment": "Strongly decreased homodimerization.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "22683995", "url": "https://glygen.org/publication/PubMed/22683995" } ] }, { "start_pos": 44, "end_pos": 48, "sequence_org": "FDGKV", "sequence_mut": "ADGKA", "comment": "Abolished DNA-binding.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "21233213", "url": "https://glygen.org/publication/PubMed/21233213" } ] }, { "start_pos": 45, "end_pos": 45, "sequence_org": "D", "sequence_mut": "A", "comment": "Does not affect DNA-binding. Decreased poly-ADP-ribosyltransferase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "22582261", "url": "https://glygen.org/publication/PubMed/22582261" }, { "database": "PubMed", "id": "21233213", "url": "https://glygen.org/publication/PubMed/21233213" } ] }, { "start_pos": 490, "end_pos": 493, "sequence_org": "VEVV", "sequence_mut": "GEVQ", "comment": "Strongly reduced interaction with TIMELESS.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "26344098", "url": "https://glygen.org/publication/PubMed/26344098" } ] }, { "start_pos": 499, "end_pos": 499, "sequence_org": "S", "sequence_mut": "A", "comment": "Abolishes automodification on serine following interaction with HPF1, leading to delay dissociation from chromatin; when associated with A-507 and A-519.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "28190768", "url": "https://glygen.org/publication/PubMed/28190768" }, { "database": "PubMed", "id": "34210965", "url": "https://glygen.org/publication/PubMed/34210965" }, { "database": "PubMed", "id": "34625544", "url": "https://glygen.org/publication/PubMed/34625544" } ] }, { "start_pos": 507, "end_pos": 507, "sequence_org": "S", "sequence_mut": "A", "comment": "Abolishes automodification on serine following interaction with HPF1, leading to delay dissociation from chromatin; when associated with A-499 and A-519.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "28190768", "url": "https://glygen.org/publication/PubMed/28190768" }, { "database": "PubMed", "id": "34210965", "url": "https://glygen.org/publication/PubMed/34210965" }, { "database": "PubMed", "id": "34625544", "url": "https://glygen.org/publication/PubMed/34625544" } ] }, { "start_pos": 519, "end_pos": 519, "sequence_org": "S", "sequence_mut": "A", "comment": "Abolishes automodification on serine following interaction with HPF1, leading to delay dissociation from chromatin; when associated with A-499 and A-507.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "28190768", "url": "https://glygen.org/publication/PubMed/28190768" }, { "database": "PubMed", "id": "34210965", "url": "https://glygen.org/publication/PubMed/34210965" }, { "database": "PubMed", "id": "34625544", "url": "https://glygen.org/publication/PubMed/34625544" } ] }, { "start_pos": 567, "end_pos": 567, "sequence_org": "N", "sequence_mut": "A", "comment": "Decreased poly-ADP-ribosyltransferase activity upon binding to damaged DNA.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "22582261", "url": "https://glygen.org/publication/PubMed/22582261" }, { "database": "PubMed", "id": "26626479", "url": "https://glygen.org/publication/PubMed/26626479" } ] }, { "start_pos": 589, "end_pos": 589, "sequence_org": "W", "sequence_mut": "A", "comment": "Decreased poly-ADP-ribosyltransferase activity upon binding to damaged DNA. Abolished ability to mediate DNA intrastrand transfer (named 'monkey-bar mechanism').", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "22582261", "url": "https://glygen.org/publication/PubMed/22582261" }, { "database": "PubMed", "id": "26626479", "url": "https://glygen.org/publication/PubMed/26626479" } ] }, { "start_pos": 591, "end_pos": 591, "sequence_org": "R", "sequence_mut": "A", "comment": "Decreased poly-ADP-ribosyltransferase activity upon binding to damaged DNA.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "22582261", "url": "https://glygen.org/publication/PubMed/22582261" }, { "database": "PubMed", "id": "26626479", "url": "https://glygen.org/publication/PubMed/26626479" } ] }, { "start_pos": 594, "end_pos": 594, "sequence_org": "T", "sequence_mut": "A", "comment": "Abolished phosphorylation by PRKDC, inhibiting translocation into the cytosol.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "35460603", "url": "https://glygen.org/publication/PubMed/35460603" } ] }, { "start_pos": 633, "end_pos": 633, "sequence_org": "K", "sequence_mut": "A", "comment": "Decreased poly-ADP-ribosyltransferase activity upon binding to damaged DNA.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "22582261", "url": "https://glygen.org/publication/PubMed/22582261" }, { "database": "PubMed", "id": "26626479", "url": "https://glygen.org/publication/PubMed/26626479" } ] }, { "start_pos": 698, "end_pos": 701, "sequence_org": "LGKL", "sequence_mut": "AGKA", "comment": "Increased auto-poly-ADP-ribosylation.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "22582261", "url": "https://glygen.org/publication/PubMed/22582261" } ] }, { "start_pos": 713, "end_pos": 713, "sequence_org": "L", "sequence_mut": "A", "comment": "Increased auto-poly-ADP-ribosylation.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "22582261", "url": "https://glygen.org/publication/PubMed/22582261" } ] }, { "start_pos": 713, "end_pos": 713, "sequence_org": "L", "sequence_mut": "F", "comment": "Leads to constitutive activity in absence of DNA damage due to unfolding of the PARP alpha-helical domain, relieving autoinhibition.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "22582261", "url": "https://glygen.org/publication/PubMed/22582261" }, { "database": "PubMed", "id": "26626480", "url": "https://glygen.org/publication/PubMed/26626480" } ] }, { "start_pos": 763, "end_pos": 770, "sequence_org": "EMLDNLLD", "sequence_mut": "AMLANLLA", "comment": "Able to bind BAD inhibitor in absence of DNA.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "29487285", "url": "https://glygen.org/publication/PubMed/29487285" } ] }, { "start_pos": 765, "end_pos": 765, "sequence_org": "L", "sequence_mut": "A", "comment": "Increased auto-poly-ADP-ribosylation.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "22582261", "url": "https://glygen.org/publication/PubMed/22582261" } ] }, { "start_pos": 766, "end_pos": 770, "sequence_org": "DNLLD", "sequence_mut": "ANLLA", "comment": "Able to bind EB-47 or BAD inhibitors in absence of DNA. Released from DNA strand break independently of EB-47 or BAD inhibitors.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "29487285", "url": "https://glygen.org/publication/PubMed/29487285" }, { "database": "PubMed", "id": "32241924", "url": "https://glygen.org/publication/PubMed/32241924" } ] }, { "start_pos": 768, "end_pos": 768, "sequence_org": "L", "sequence_mut": "A", "comment": "Increased auto-poly-ADP-ribosylation.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "22582261", "url": "https://glygen.org/publication/PubMed/22582261" } ] }, { "start_pos": 774, "end_pos": 774, "sequence_org": "A", "sequence_mut": "L", "comment": "Increased DNA-independent poly-ADP-ribosyltransferase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "26626480", "url": "https://glygen.org/publication/PubMed/26626480" } ] }, { "start_pos": 774, "end_pos": 774, "sequence_org": "A", "sequence_mut": "S", "comment": "Increased DNA-independent poly-ADP-ribosyltransferase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "26626480", "url": "https://glygen.org/publication/PubMed/26626480" } ] }, { "start_pos": 797, "end_pos": 797, "sequence_org": "L", "sequence_mut": "P", "comment": "1.5% of wild-type activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "9315851", "url": "https://glygen.org/publication/PubMed/9315851" } ] }, { "start_pos": 826, "end_pos": 826, "sequence_org": "H", "sequence_mut": "A", "comment": "Strongly reduced serine ADP-ribosylation, caused by abolished interaction with HPF1.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "32028527", "url": "https://glygen.org/publication/PubMed/32028527" } ] }, { "start_pos": 826, "end_pos": 826, "sequence_org": "H", "sequence_mut": "E", "comment": "Decreased polymerase activity, leading to the production of short poly-ADP-ribose chains.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "34795260", "url": "https://glygen.org/publication/PubMed/34795260" } ] }, { "start_pos": 850, "end_pos": 851, "sequence_org": "PF", "sequence_mut": "", "comment": "Abolished interaction with TIMELESS.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "26344098", "url": "https://glygen.org/publication/PubMed/26344098" } ] }, { "start_pos": 862, "end_pos": 862, "sequence_org": "H", "sequence_mut": "A", "comment": "Poly-ADP-ribosyltransferase activity is impaired while mono-ADP-ribosyltransferase activity is not affected; produces a mixture of short and mono ADP-ribose chains.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "7852410", "url": "https://glygen.org/publication/PubMed/7852410" } ] }, { "start_pos": 865, "end_pos": 865, "sequence_org": "R", "sequence_mut": "A", "comment": "Increased affinity for DNA damage sites.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "34795260", "url": "https://glygen.org/publication/PubMed/34795260" } ] }, { "start_pos": 868, "end_pos": 868, "sequence_org": "N", "sequence_mut": "S", "comment": "4% of wild-type activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "9315851", "url": "https://glygen.org/publication/PubMed/9315851" } ] }, { "start_pos": 870, "end_pos": 870, "sequence_org": "A", "sequence_mut": "L", "comment": "Increased DNA-independent poly-ADP-ribosyltransferase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "26626480", "url": "https://glygen.org/publication/PubMed/26626480" } ] }, { "start_pos": 870, "end_pos": 870, "sequence_org": "A", "sequence_mut": "S", "comment": "Increased DNA-independent poly-ADP-ribosyltransferase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "26626480", "url": "https://glygen.org/publication/PubMed/26626480" } ] }, { "start_pos": 871, "end_pos": 871, "sequence_org": "G", "sequence_mut": "L", "comment": "Increased DNA-independent poly-ADP-ribosyltransferase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "26626480", "url": "https://glygen.org/publication/PubMed/26626480" } ] }, { "start_pos": 871, "end_pos": 871, "sequence_org": "G", "sequence_mut": "S", "comment": "Does not affect DNA-independent poly-ADP-ribosyltransferase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "26626480", "url": "https://glygen.org/publication/PubMed/26626480" } ] }, { "start_pos": 882, "end_pos": 882, "sequence_org": "P", "sequence_mut": "G", "comment": "Does not affect DNA-independent poly-ADP-ribosyltransferase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "26626480", "url": "https://glygen.org/publication/PubMed/26626480" } ] }, { "start_pos": 883, "end_pos": 883, "sequence_org": "E", "sequence_mut": "Q", "comment": "Does not affect ADP-ribosyltransferase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "7852410", "url": "https://glygen.org/publication/PubMed/7852410" } ] }, { "start_pos": 883, "end_pos": 887, "sequence_org": "EAPVT", "sequence_mut": "ASSVA", "comment": "Does not affect DNA-independent poly-ADP-ribosyltransferase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "26626480", "url": "https://glygen.org/publication/PubMed/26626480" } ] }, { "start_pos": 885, "end_pos": 885, "sequence_org": "P", "sequence_mut": "G", "comment": "Does not affect DNA-independent poly-ADP-ribosyltransferase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "26626480", "url": "https://glygen.org/publication/PubMed/26626480" } ] }, { "start_pos": 885, "end_pos": 885, "sequence_org": "P", "sequence_mut": "S", "comment": "Does not affect DNA-independent poly-ADP-ribosyltransferase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "26626480", "url": "https://glygen.org/publication/PubMed/26626480" } ] }, { "start_pos": 890, "end_pos": 890, "sequence_org": "M", "sequence_mut": "V", "comment": "<0.5% of wild-type activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "9315851", "url": "https://glygen.org/publication/PubMed/9315851" } ] }, { "start_pos": 893, "end_pos": 893, "sequence_org": "K", "sequence_mut": "I", "comment": "Abolishes enzymatic activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "9315851", "url": "https://glygen.org/publication/PubMed/9315851" } ] }, { "start_pos": 897, "end_pos": 897, "sequence_org": "F", "sequence_mut": "S", "comment": "10% of wild-type activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "9315851", "url": "https://glygen.org/publication/PubMed/9315851" } ] }, { "start_pos": 899, "end_pos": 899, "sequence_org": "D", "sequence_mut": "N", "comment": "0.6% of wild-type activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "9315851", "url": "https://glygen.org/publication/PubMed/9315851" } ] }, { "start_pos": 908, "end_pos": 908, "sequence_org": "C", "sequence_mut": "R", "comment": "<0.5% of wild-type activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "9315851", "url": "https://glygen.org/publication/PubMed/9315851" } ] }, { "start_pos": 923, "end_pos": 923, "sequence_org": "E", "sequence_mut": "Q", "comment": "Does not affect ADP-ribosyltransferase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "7852410", "url": "https://glygen.org/publication/PubMed/7852410" } ] }, { "start_pos": 926, "end_pos": 926, "sequence_org": "L", "sequence_mut": "F", "comment": "1.5% of wild-type activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "9315851", "url": "https://glygen.org/publication/PubMed/9315851" } ] }, { "start_pos": 931, "end_pos": 931, "sequence_org": "E", "sequence_mut": "Q", "comment": "Does not affect ADP-ribosyltransferase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "7852410", "url": "https://glygen.org/publication/PubMed/7852410" } ] }, { "start_pos": 986, "end_pos": 986, "sequence_org": "Y", "sequence_mut": "H", "comment": "14% of wild-type activity and increased branching 15-fold.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "9315851", "url": "https://glygen.org/publication/PubMed/9315851" } ] }, { "start_pos": 988, "end_pos": 988, "sequence_org": "E", "sequence_mut": "A", "comment": "Poly-ADP-ribosyltransferase activity is inhibited while mono-ADP-ribosyltransferase activity is not affected; only monomers are added. Disrupts interaction with CHD1L and ability to recruit PARP2 to DNA damage sites.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "9315851", "url": "https://glygen.org/publication/PubMed/9315851" }, { "database": "PubMed", "id": "7852410", "url": "https://glygen.org/publication/PubMed/7852410" }, { "database": "PubMed", "id": "30104678", "url": "https://glygen.org/publication/PubMed/30104678" }, { "database": "PubMed", "id": "29220653", "url": "https://glygen.org/publication/PubMed/29220653" }, { "database": "PubMed", "id": "32028527", "url": "https://glygen.org/publication/PubMed/32028527" } ] }, { "start_pos": 988, "end_pos": 988, "sequence_org": "E", "sequence_mut": "D", "comment": "Poly-ADP-ribosyltransferase activity is inhibited while mono-ADP-ribosyltransferase activity is not affected; only monomers are added. Disrupts interaction with CHD1L and ability to recruit PARP2 to DNA damage sites.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "9315851", "url": "https://glygen.org/publication/PubMed/9315851" }, { "database": "PubMed", "id": "7852410", "url": "https://glygen.org/publication/PubMed/7852410" }, { "database": "PubMed", "id": "30104678", "url": "https://glygen.org/publication/PubMed/30104678" }, { "database": "PubMed", "id": "29220653", "url": "https://glygen.org/publication/PubMed/29220653" }, { "database": "PubMed", "id": "32028527", "url": "https://glygen.org/publication/PubMed/32028527" } ] }, { "start_pos": 988, "end_pos": 988, "sequence_org": "E", "sequence_mut": "K", "comment": "Poly-ADP-ribosyltransferase activity is inhibited while mono-ADP-ribosyltransferase activity is not affected; only monomers are added. Disrupts interaction with CHD1L and ability to recruit PARP2 to DNA damage sites.", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "9315851", "url": "https://glygen.org/publication/PubMed/9315851" }, { "database": "PubMed", "id": "7852410", "url": "https://glygen.org/publication/PubMed/7852410" }, { "database": "PubMed", "id": "30104678", "url": "https://glygen.org/publication/PubMed/30104678" }, { "database": "PubMed", "id": "29220653", "url": "https://glygen.org/publication/PubMed/29220653" }, { "database": "PubMed", "id": "32028527", "url": "https://glygen.org/publication/PubMed/32028527" } ] }, { "start_pos": 988, "end_pos": 988, "sequence_org": "E", "sequence_mut": "Q", "comment": "Poly-ADP-ribosyltransferase activity is inhibited while mono-ADP-ribosyltransferase activity is not affected; only monomers are added. 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"tissue": { "name": "Uterus", "namespace": "UBERON", "id": "0000995", "url": "http://purl.obolibrary.org/obo/UBERON_0000995" }, "score": "87.86", "present": "MEDIUM", "evidence": [ { "database": "Bgee", "id": "ENSG00000143799", "url": "https://bgee.org/?page=gene&gene_id=ENSG00000143799" } ] }, { "tissue": { "name": "Esophagus", "namespace": "UBERON", "id": "0001043", "url": "http://purl.obolibrary.org/obo/UBERON_0001043" }, "score": "92.49", "present": "HIGH", "evidence": [ { "database": "Bgee", "id": "ENSG00000143799", "url": "https://bgee.org/?page=gene&gene_id=ENSG00000143799" } ] }, { "tissue": { "name": "Rectum", "namespace": "UBERON", "id": "0001052", "url": "http://purl.obolibrary.org/obo/UBERON_0001052" }, "score": "94.66", "present": "HIGH", "evidence": [ { "database": "Bgee", "id": "ENSG00000143799", "url": "https://bgee.org/?page=gene&gene_id=ENSG00000143799" } ] }, { "tissue": { "name": "Colon", "namespace": "UBERON", "id": "0001155", "url": 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"MONDO:0012758", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012758", "name": "prostate cancer, hereditary, 13", "description": "" }, { "id": "MONDO:0012758", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012758", "name": "prostate cancer, hereditary, type 13", "description": "" }, { "id": "MONDO:0012758", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012758", "name": "HPC13", "description": "" }, { "id": "MONDO:0011270", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011270", "name": "prostate cancer, hereditary, 8", "description": "" }, { "id": "MONDO:0011270", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011270", "name": "prostate cancer, hereditary, 8", "description": "" }, { "id": "MONDO:0011270", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011270", "name": "prostate cancer, hereditary, type 8", "description": "" }, { "id": "MONDO:0011270", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011270", "name": "HPC8", "description": "" }, { "id": "MONDO:0011270", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011270", "name": "predisposing for prostate cancer", "description": "" }, { "id": "MONDO:0011270", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011270", "name": "prostate cancer, susceptibility to", "description": "" }, { "id": "MONDO:0012300", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012300", "name": "prostate cancer, hereditary, 6", "description": "" }, { "id": "MONDO:0012300", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012300", "name": "prostate cancer, hereditary, 6", "description": "" }, { "id": "MONDO:0012300", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012300", "name": "prostate cancer, hereditary, type 6", "description": "" }, { "id": "MONDO:0012300", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012300", "name": "HPC6", "description": "" }, { "id": "MONDO:0012300", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012300", "name": "prostate cancer, susceptibility to", "description": "" }, { "id": "MONDO:0012620", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012620", "name": "prostate cancer, hereditary, 10", "description": "" }, { "id": "MONDO:0012620", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012620", "name": "HPC10", "description": "" }, { "id": "MONDO:0012620", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012620", "name": "prostate cancer, hereditary, 10", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "familial prostate carcinoma", "description": "Prostate carcinoma that has developed in relatives of patients with a history of prostate carcinoma." }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "familial prostate cancer", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "hereditary prostate cancer", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "hereditary prostate carcinoma", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "prostate cancer, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "prostate cancer, familial, susceptibility to, autosomal dominant, somatic 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"https://monarchinitiative.org/disease/MONDO:0012470", "name": "HPC7", "description": "" }, { "id": "MONDO:0012470", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012470", "name": "prostate cancer, hereditary, 7", "description": "" }, { "id": "MONDO:0012470", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012470", "name": "prostate cancer aggressiveness", "description": "" }, { "id": "MONDO:0011098", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011098", "name": "prostate cancer, hereditary, 1", "description": "Any familial prostate cancer in which the cause of the disease is a mutation in the RNASEL gene." }, { "id": "MONDO:0011098", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011098", "name": "RNASEL familial prostate cancer", "description": "" }, { "id": "MONDO:0011098", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011098", "name": "familial prostate cancer caused by mutation in RNASEL", "description": "" }, { "id": "MONDO:0011098", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011098", "name": "prostate cancer 1", "description": "" }, { "id": "MONDO:0011098", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011098", "name": "prostate cancer, hereditary, 1", "description": "" }, { "id": "MONDO:0011098", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011098", "name": "prostate cancer, hereditary, type 1", "description": "" }, { "id": "MONDO:0011098", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011098", "name": "HPC1", "description": "" }, { "id": "MONDO:0011098", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011098", "name": "Prca1", "description": "" }, { "id": "MONDO:0012768", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012768", "name": "prostate cancer, hereditary, 11", "description": "" }, { "id": "MONDO:0012768", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012768", "name": "HPC11", "description": "" }, { "id": "MONDO:0012768", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012768", "name": "prostate cancer, hereditary, 11", "description": "" }, { "id": "MONDO:0012769", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012769", "name": "prostate cancer, hereditary, 14", "description": "" }, { "id": "MONDO:0012769", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012769", "name": "HPC14", "description": "" }, { "id": "MONDO:0012769", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012769", "name": "prostate cancer, hereditary, 14", "description": "" }, { "id": "MONDO:0012770", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012770", "name": "prostate cancer, hereditary, 15", "description": "" }, { "id": "MONDO:0012770", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012770", "name": "HPC15", "description": "" }, { "id": "MONDO:0012770", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012770", "name": "prostate cancer, hereditary, 15", "description": "" }, { "id": "MONDO:0010257", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0010257", "name": "prostate cancer, hereditary, X-linked 1", "description": "" }, { "id": "MONDO:0010257", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0010257", "name": "HPCX1", "description": "" }, { "id": "MONDO:0010257", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0010257", "name": "prostate cancer, hereditary, X-linked 1", "description": "" }, { "id": "MONDO:0010257", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0010257", "name": "prostate cancer susceptibility, 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cancer", "description": "Prostate cancer" }, { "id": "MIM:601518", "resource": "MIM", "url": "https://www.omim.org/entry/601518", "name": "Prostate cancer, hereditary, 1", "description": "Prostate cancer, hereditary, 1" }, { "id": "MIM:611955", "resource": "MIM", "url": "https://www.omim.org/entry/611955", "name": "Prostate cancer, hereditary, 11", "description": "Prostate cancer, hereditary, 11" } ] } ] }, { "significant": "Yes", "trend": "up", "name": "Stomach cancer [DO disease name]", "url": "http://disease-ontology.org/term/DOID:10534", "evidence": [ { "database": "BioXpress", "id": "P09874", "url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P09874" } ], "disease": [ { "disease_id": "DOID:10534", "recommended_name": { "id": "DOID:10534", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:10534", "name": "stomach cancer", "description": "A gastrointestinal system cancer that is located_in the stomach." }, "synonyms": [ { "id": "DOID:10534", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:10534", "name": "gastric cancer", "description": "" }, { "id": "DOID:10534", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:10534", "name": "gastric neoplasm", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "gastric cancer", "description": "A primary or metastatic malignant neoplasm involving the stomach." }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "gastric neoplasm", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "Ca lesser curvature - stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "cancer of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "gastric cancer", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "gastric cancer risk after h. pylori infection", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "gastric cancer, somatic", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant gastric neoplasm", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant gastric tumor", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant gastric tumour", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant neoplasm of lesser curve of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant neoplasm of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant neoplasm of the stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant stomach neoplasm", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumor of body of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumor of greater curve of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumor of lesser curve of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumor of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumor of the stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumour of body of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumour of greater curve of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumour of lesser curve of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumour of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumour of the stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "stomach cancer", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "Ca body - stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "ca greater curvature of stomach", "description": "" }, { "id": "MONDO:0001056", 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"description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "familial cancer of breast", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "familial cancer of the breast", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "hereditary breast cancer", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "hereditary breast carcinoma", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer, familial", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer, familial Male", "description": "" }, { "id": "MIM:114480", "resource": "MIM", "url": "https://www.omim.org/entry/114480", "name": "Breast cancer", "description": "Breast cancer" } ] } ] }, { "significant": "No", "trend": "down", "name": "Thyroid cancer [DO disease name]", "url": "http://disease-ontology.org/term/DOID:1781", "evidence": [ { "database": "BioXpress", "id": "P09874", "url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P09874" } ], "disease": [ { "disease_id": "DOID:1781", "recommended_name": { "id": "DOID:1781", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1781", "name": "thyroid cancer", "description": "An endocrine gland cancer located in the thryoid gland located in the neck below the thyroid cartilage." }, "synonyms": [ { "id": "DOID:1781", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1781", "name": "thyroid gland cancer", "description": "" }, { "id": "DOID:1781", "resource": "Disease Ontology", 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"https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P09874" } ], "disease": [ { "disease_id": "DOID:263", "recommended_name": { "id": "DOID:263", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:263", "name": "kidney cancer", "description": "A urinary system cancer that is located_in the kidney." }, "synonyms": [ { "id": "DOID:263", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:263", "name": "malignant neoplasm of kidney except pelvis", "description": "" }, { "id": "DOID:263", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:263", "name": "malignant tumour of kidney", "description": "" }, { "id": "DOID:263", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:263", "name": "renal cancer", "description": "" } ] } ] }, { "significant": "Yes", "trend": "up", "name": "Liver cancer [DO disease name]", "url": "http://disease-ontology.org/term/DOID:3571", "evidence": [ { 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"https://www.rhea-db.org/rhea/58236", "database": "Rhea", "categories": [ "Enzyme and Pathway" ] }, { "id": "72071", "url": "https://www.rhea-db.org/rhea/72071", "database": "Rhea", "categories": [ "Enzyme and Pathway" ] }, { "id": "A0A7I2V384", "url": "https://www.uniprot.org/uniprot/A0A7I2V384", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "A0A7I2V384-1", "url": "https://www.uniprot.org/uniprot/A0A7I2V384-1", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "A0A7I2V3E1", "url": "https://www.uniprot.org/uniprot/A0A7I2V3E1", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "A0A7I2V3E1-1", "url": "https://www.uniprot.org/uniprot/A0A7I2V3E1-1", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "A0A7I2V5E9", "url": "https://www.uniprot.org/uniprot/A0A7I2V5E9", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "A0A7I2V5E9-1", "url": "https://www.uniprot.org/uniprot/A0A7I2V5E9-1", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "A0A7I2V625", "url": "https://www.uniprot.org/uniprot/A0A7I2V625", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "A0A7I2V625-1", "url": "https://www.uniprot.org/uniprot/A0A7I2V625-1", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "P09874-1", "url": "https://www.uniprot.org/uniprot/P09874-1", "database": "UniProtKB", "categories": [ "Protein" ] } ], "sequence": { "sequence": "MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPETSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSPWGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW", "length": 1014, "header": "sp|P09874-1|PARP1_HUMAN Isoform 1 of Poly [ADP-ribose] polymerase 1 OS=Homo sapiens OX=9606 GN=PARP1 PE=1 SV=4 CANONICAL=P09874-1" }, "isoforms": [ { "isoform_ac": "A0A7I2V384-1", "url": "", "sequence": { "sequence": "MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTEKKLY", "length": 100, "header": "tr|A0A7I2V384-1|A0A7I2V384_HUMAN Computationally mapped isoform of Poly(ADP-ribose) polymerase 1 OS=Homo sapiens OX=9606 GN=PARP1 PE=1 SV=1 CANONICAL=P09874-1" }, "locus": { "chromosome": "1", "start_pos": 226407929, "end_pos": 226392485, "strand": "+", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000678560.1", "url": "https://www.ensembl.org/id/ENST00000678560.1" }, { "database": "Ensembl Peptide", "id": "ENSP00000503293.1", "url": "https://www.ensembl.org/id/ENSP00000503293.1" } ] } }, { "isoform_ac": "A0A7I2V3E1-1", "url": "", "sequence": { "sequence": "MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPETSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSPWGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW", "length": 971, "header": "tr|A0A7I2V3E1-1|A0A7I2V3E1_HUMAN Computationally mapped isoform of Poly [ADP-ribose] polymerase OS=Homo sapiens OX=9606 GN=PARP1 PE=1 SV=1 CANONICAL=P09874-1" }, "locus": { "chromosome": "1", "start_pos": 226407929, "end_pos": 226361463, "strand": "+", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000677203.1", "url": "https://www.ensembl.org/id/ENST00000677203.1" }, { "database": "Ensembl Peptide", "id": "ENSP00000503396.1", "url": "https://www.ensembl.org/id/ENSP00000503396.1" } ] } }, { "isoform_ac": "A0A7I2V5E9-1", "url": "", "sequence": { "sequence": "MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLISHYPT", "length": 308, "header": "tr|A0A7I2V5E9-1|A0A7I2V5E9_HUMAN Computationally mapped isoform of Poly(ADP-ribose) polymerase 1 OS=Homo sapiens OX=9606 GN=PARP1 PE=1 SV=1 CANONICAL=P09874-1" }, "locus": { "chromosome": "1", "start_pos": 226407929, "end_pos": 226381191, "strand": "+", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000678144.1", "url": "https://www.ensembl.org/id/ENST00000678144.1" }, { "database": "Ensembl Peptide", "id": "ENSP00000504430.1", "url": "https://www.ensembl.org/id/ENSP00000504430.1" } ] } }, { "isoform_ac": "A0A7I2V625-1", "url": "", "sequence": { "sequence": "MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPETSASRRWKR", "length": 369, "header": "tr|A0A7I2V625-1|A0A7I2V625_HUMAN Computationally mapped isoform of NAD(+) ADP-ribosyltransferase OS=Homo sapiens OX=9606 GN=PARP1 PE=1 SV=1 CANONICAL=P09874-1" }, "locus": { "chromosome": "1", "start_pos": 226407929, "end_pos": 226380150, "strand": "+", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000677091.1", "url": "https://www.ensembl.org/id/ENST00000677091.1" }, { "database": "Ensembl Peptide", "id": "ENSP00000504745.1", "url": "https://www.ensembl.org/id/ENSP00000504745.1" } ] } }, { "isoform_ac": "P09874-1", "url": "", "sequence": { "sequence": "MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPETSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSPWGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW", "length": 1014, "header": "sp|P09874-1|PARP1_HUMAN Isoform 1 of Poly [ADP-ribose] polymerase 1 OS=Homo sapiens OX=9606 GN=PARP1 PE=1 SV=4 CANONICAL=P09874-1" }, "locus": { "chromosome": "1", "start_pos": 226407929, "end_pos": 226361463, "strand": "+", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000366794.10", "url": "https://www.ensembl.org/id/ENST00000366794.10" }, { "database": "Ensembl Peptide", "id": "ENSP00000355759.5", "url": "https://www.ensembl.org/id/ENSP00000355759.5" } ] } } ], "glycosylation": [ { "glytoucan_ac": "G49108TO", "type": "O-linked", "subtype": "O-GlcNAcylation", "site_category": "reported_with_glycan", "site_seq": "", "relation": "attached", "comment": "O-GlcNAcylation", "evidence": [ { "id": "P09874", "database": "O-GlcNAc Database", "url": "https://www.oglcnac.mcw.edu/search/?query_protein=P09874" }, { "id": "16408927", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/16408927" }, { "id": "33214551", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/33214551" }, { "id": "34725712", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/34725712" }, { "id": "35138101", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/35138101" }, { "id": "30397120", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/30397120" }, { "id": "35008409", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/35008409" }, { "id": "32522876", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/32522876" }, { "id": "26853435", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/26853435" }, { "id": "37217939", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/37217939" }, { "id": "34019948", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/34019948" }, { "id": "35083852", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/35083852" }, { "id": "32119511", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/32119511" }, { "id": "28510447", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/28510447" } ] } ], "phosphorylation": [ { "start_pos": 177, "end_pos": 177, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Ser", "comment": "Phosphoserine", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "23186163", "url": "https://glygen.org/publication/PubMed/23186163" }, { "database": "iPTMnet", "id": "P09874", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/P09874" }, { "database": "PubMed", "id": "20068231", "url": "https://glygen.org/publication/PubMed/20068231" }, { "database": "PubMed", "id": "23382195", "url": "https://glygen.org/publication/PubMed/23382195" } ], "site_lbl": "Ser177" }, { "start_pos": 179, "end_pos": 179, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Ser", "comment": "Phosphoserine", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "23186163", "url": "https://glygen.org/publication/PubMed/23186163" }, { "database": "PubMed", "id": "17525332", "url": "https://glygen.org/publication/PubMed/17525332" }, { "database": "iPTMnet", "id": "P09874", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/P09874" }, { "database": "PubMed", "id": "20068231", "url": "https://glygen.org/publication/PubMed/20068231" }, { "database": "phospho.ELM", "id": "P09874", "url": "http://phospho.elm.eu.org/byAccession/P09874.html" } ], "site_lbl": "Ser179" }, { "start_pos": 185, "end_pos": 185, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Ser", "comment": "Phosphoserine", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "23186163", "url": "https://glygen.org/publication/PubMed/23186163" }, { "database": "iPTMnet", "id": "P09874", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/P09874" } ], "site_lbl": "Ser185" }, { "start_pos": 274, "end_pos": 274, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Ser", "comment": "Phosphoserine", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "23186163", "url": "https://glygen.org/publication/PubMed/23186163" }, { "database": "iPTMnet", "id": "P09874", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/P09874" }, { "database": "PubMed", "id": "20068231", "url": "https://glygen.org/publication/PubMed/20068231" } ], "site_lbl": "Ser274" }, { "start_pos": 277, "end_pos": 277, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Ser", "comment": "Phosphoserine", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "23186163", "url": "https://glygen.org/publication/PubMed/23186163" }, { "database": "iPTMnet", "id": "P09874", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/P09874" } ], "site_lbl": "Ser277" }, { "start_pos": 364, "end_pos": 364, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Ser", "comment": "Phosphoserine", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "24275569", "url": "https://glygen.org/publication/PubMed/24275569" }, { "database": "iPTMnet", "id": "P09874", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/P09874" } ], "site_lbl": "Ser364" }, { "start_pos": 368, "end_pos": 368, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Thr", "comment": "Phosphothreonine", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": 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RAD23.", "journal": "The EMBO journal", "date": "1994", "authors": "Masutani C, Sugasawa K, Yanagisawa J, Sonoyama T, Ui M, Enomoto T, Takio K, Tanaka K, van der Spek PJ, Bootsma D, et al.", "evidence": [ { "database": "Reactome", "id": "R-HSA-5696394", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5696394" } ], "reference": [ { "type": "PubMed", "id": "8168482", "url": "https://glygen.org/publication/PubMed/8168482" } ] }, { "title": "Aberrant DNA repair and DNA replication due to an inherited enzymatic defect in human DNA ligase I.", "journal": "Molecular and cellular biology", "date": "1994", "authors": "Prigent C, Satoh MS, Daly G, Barnes DE, Lindahl T", "evidence": [ { "database": "Reactome", "id": "R-HSA-110362", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-110362" } ], "reference": [ { "type": "PubMed", "id": "8264597", "url": "https://glygen.org/publication/PubMed/8264597" } ] }, { "title": "Specific interaction of DNA polymerase beta and DNA ligase I in a 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"title": "Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching.", "journal": "Biochemistry", "date": "1997", "authors": "Rolli V, O'Farrell M, Menissier-de Murcia J, de Murcia G", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "reference": [ { "type": "PubMed", "id": "9315851", "url": "https://glygen.org/publication/PubMed/9315851" } ] }, { "title": "Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1.", "journal": "The Journal of cell biology", "date": "1997", "authors": "Sternsdorf T, Jensen K, Will H", "evidence": [ { "database": "Reactome", "id": "R-HSA-3108214", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3108214" } ], "reference": [ { "type": "PubMed", "id": "9412458", "url": "https://glygen.org/publication/PubMed/9412458" } ] }, { "title": "Covalent modification of PML by the sentrin family of ubiquitin-like proteins.", "journal": "The Journal of biological chemistry", "date": "1998", "authors": "Kamitani T, Nguyen HP, Kito K, Fukuda-Kamitani T, Yeh ET", "evidence": [ { "database": "Reactome", "id": "R-HSA-3108214", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3108214" } ], "reference": [ { "type": "PubMed", "id": "9452416", "url": "https://glygen.org/publication/PubMed/9452416" } ] }, { "title": "Functional association of poly(ADP-ribose) polymerase with DNA polymerase alpha-primase complex: a link between DNA strand break detection and DNA replication.", "journal": "Nucleic Acids Res.", "date": "1998", "authors": "Dantzer F, Nasheuer H P, Vonesch J L, de Murcia G, M\u00e9nissier-de Murcia J", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "reference": [ { "type": "PubMed", "id": "9518481", "url": "https://glygen.org/publication/PubMed/9518481" } ] }, { "title": "Thermodynamics of human DNA ligase I trimerization and association with DNA polymerase beta.", "journal": "The Journal of biological chemistry", "date": "1998", "authors": "Dimitriadis EK, Prasad R, Vaske MK, Chen L, Tomkinson AE, Lewis MS, Wilson SH", "evidence": [ { "database": "Reactome", "id": "R-HSA-110362", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-110362" } ], "reference": [ { "type": "PubMed", "id": "9685411", "url": "https://glygen.org/publication/PubMed/9685411" } ] }, { "title": "Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA.", "journal": "Nature structural biology", "date": "1998", "authors": "Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M", "evidence": [ { "database": "Reactome", "id": "R-HSA-5696395", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5696395" } ], "reference": [ { "type": "PubMed", "id": "9699634", "url": "https://glygen.org/publication/PubMed/9699634" } ] }, { "title": "DNA-binding 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"https://www.ebi.ac.uk/QuickGO/term/GO:0043504", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "mitochondrial DNA metabolic process", "id": "GO:0032042", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0032042", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "positive regulation of necroptotic process", "id": "GO:0060545", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0060545", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "positive regulation of SMAD protein signal transduction", "id": "GO:0060391", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0060391", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "macrophage differentiation", "id": "GO:0030225", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030225", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "negative regulation of transcription elongation by RNA polymerase II", "id": "GO:0034244", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0034244", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "negative regulation of innate immune response", "id": "GO:0045824", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045824", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "signal transduction involved in regulation of gene expression", "id": "GO:0023019", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0023019", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "protein localization to chromatin", "id": "GO:0071168", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0071168", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "ATP generation from poly-ADP-D-ribose", "id": "GO:1990966", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1990966", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "protein poly-ADP-ribosylation", "id": "GO:0070212", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0070212", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "positive regulation of DNA-templated transcription, elongation", "id": "GO:0032786", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0032786", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "negative regulation of telomere maintenance via telomere lengthening", "id": "GO:1904357", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1904357", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "positive regulation of double-strand break repair via homologous recombination", "id": "GO:1905168", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1905168", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "positive regulation of single strand break repair", "id": "GO:1903518", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1903518", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "replication fork reversal", "id": "GO:0071932", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0071932", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "negative regulation of adipose tissue development", "id": "GO:1904178", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1904178", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "DNA ADP-ribosylation", "id": "GO:0030592", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030592", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "negative regulation of cGAS/STING signaling pathway", "id": "GO:0160049", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0160049", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "regulation of base-excision repair", "id": "GO:1905051", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1905051", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" }, { "name": "regulation of DNA metabolic process", "id": "GO:0051052", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051052", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" } ], "pmid": "" } ] } ] }, "pro_annotation": [], "site_annotation": [ { "start_pos": 121, "end_pos": 123, "annotation": "n_glycosylation_sequon" }, { "start_pos": 381, "end_pos": 383, "annotation": "n_glycosylation_sequon" }, { "start_pos": 517, "end_pos": 519, "annotation": "n_glycosylation_sequon" }, { "start_pos": 630, "end_pos": 632, "annotation": "n_glycosylation_sequon" }, { "start_pos": 961, "end_pos": 963, "annotation": "n_glycosylation_sequon" }, { "start_pos": 980, "end_pos": 982, "annotation": "n_glycosylation_sequon" } ], "ptm_annotation": [ { "annotation": "Phosphorylated at Thr-594 by PRKDC in response to DNA damage following virus infection, promoting its translocation to the cytosol (PubMed:10467406, PubMed:35460603). Phosphorylated by TXK (PubMed:17177976).", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "10467406", "url": "https://glygen.org/publication/PubMed/10467406" }, { "database": "PubMed", "id": "17177976", "url": "https://glygen.org/publication/PubMed/17177976" }, { "database": "PubMed", "id": "35460603", "url": "https://glygen.org/publication/PubMed/35460603" } ] }, { "annotation": "Poly-ADP-ribosylated on serine, glutamate and aspartate residues by autocatalysis (PubMed:19764761, PubMed:20388712, PubMed:22582261). Auto-ADP-ribosylation on serine takes place following interaction with HPF1 (PubMed:28190768, PubMed:34625544). Auto poly-ADP-ribosylation on serine residues promotes its dissociation from chromatin (PubMed:15607977, PubMed:30675909, PubMed:32358582, PubMed:34210965, PubMed:34625544). Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites (PubMed:19661379). Mono-ADP-ribosylated at Lys-521 by SIRT6 in response to oxidative stress, promoting recruitment to double-strand breaks (DSBs) sites (PubMed:21680843, PubMed:22753495, PubMed:27568560).", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "19661379", "url": "https://glygen.org/publication/PubMed/19661379" }, { "database": "PubMed", "id": "28190768", "url": "https://glygen.org/publication/PubMed/28190768" }, { "database": "PubMed", "id": "22582261", "url": "https://glygen.org/publication/PubMed/22582261" }, { "database": "PubMed", "id": "27568560", "url": "https://glygen.org/publication/PubMed/27568560" }, { "database": "PubMed", "id": "20388712", "url": "https://glygen.org/publication/PubMed/20388712" }, { "database": "PubMed", "id": "21680843", "url": "https://glygen.org/publication/PubMed/21680843" }, { "database": "PubMed", "id": "30675909", "url": "https://glygen.org/publication/PubMed/30675909" }, { "database": "PubMed", "id": "15607977", "url": "https://glygen.org/publication/PubMed/15607977" }, { "database": "PubMed", "id": "32358582", "url": "https://glygen.org/publication/PubMed/32358582" }, { "database": "PubMed", "id": "22753495", "url": "https://glygen.org/publication/PubMed/22753495" }, { "database": "PubMed", "id": "19764761", "url": "https://glygen.org/publication/PubMed/19764761" }, { "database": "PubMed", "id": "34210965", "url": "https://glygen.org/publication/PubMed/34210965" }, { "database": "PubMed", "id": "34625544", "url": "https://glygen.org/publication/PubMed/34625544" } ] }, { "annotation": "Proteolytically cleaved by caspase-3 (CASP3) and caspase-7 (CASP7) in response to apoptosis to generate the Poly [ADP-ribose] polymerase 1, processed N-terminus and Poly [ADP-ribose] polymerase 1, processed C-terminus forms (PubMed:7596430, PubMed:10497198, PubMed:16374543, PubMed:22464733, PubMed:22451931, PubMed:33168626, PubMed:35104452). CASP3-mediated cleavage is promoted by the TP53/p53-induced long non-coding RNA SPARCLE, which binds PARP1 in response to genotoxic stress (PubMed:35104452).", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "33168626", "url": "https://glygen.org/publication/PubMed/33168626" }, { "database": "PubMed", "id": "7596430", "url": "https://glygen.org/publication/PubMed/7596430" }, { "database": "PubMed", "id": "22464733", "url": "https://glygen.org/publication/PubMed/22464733" }, { "database": "PubMed", "id": "10497198", "url": "https://glygen.org/publication/PubMed/10497198" }, { "database": "PubMed", "id": "16374543", "url": "https://glygen.org/publication/PubMed/16374543" }, { "database": "PubMed", "id": "35104452", "url": "https://glygen.org/publication/PubMed/35104452" }, { "database": "PubMed", "id": "22451931", "url": "https://glygen.org/publication/PubMed/22451931" } ] }, { "annotation": "Sumoylated with SUMO1 or SUMO2 by PIAS4 following prolonged residence (trapping) to chromatin (PubMed:35013556). Sumoylation promotes ubiquitination by RNF4 and removal from chromatin by VCP/p97 (PubMed:35013556).", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "35013556", "url": "https://glygen.org/publication/PubMed/35013556" } ] }, { "annotation": "Ubiquitinated by RNF4 following sumoylation by PIAS4 in response to prolonged residence (trapping) to chromatin (PubMed:35013556). Ubiquitination promotes removal from chromatin by VCP/p97 (PubMed:35013556).", "evidence": [ { "database": "UniProtKB", "id": "P09874", "url": "https://www.uniprot.org/uniprot/P09874" }, { "database": "PubMed", "id": "35013556", "url": "https://glygen.org/publication/PubMed/35013556" } ] } ], "interactions": [], "reactions": [ { "id": "54424", "name": "", "equation": "L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamide", "summary": "", "cellular_location": "", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q5U2Q4-1", "P27008-1", "Q2NL67-1", "Q53GL7-1", "Q8N5Y8-1", "Q7Z3E1-1", "P09874-1", "Q9UGN5-1", "Q460N3-1", "Q9UKK3-1", "Q9H0J9-1", "Q9NR21-4", "Q9Y6F1-1", "O95271-1", "Q9H2K2-1", "Q8CIE4-1", "Q8C1B2-1", "Q8CFF0-1", "Q8BZ20-1", "Q6P6P7-1", "O88554-1", "P11103-1", "Q7TMM8-1", "Q3UES3-1", "Q6PFX9-1", "E9PYK3-1", "Q3ULW8-1", "Q54YW4-1", "P35875-1", "Q9VBP3-1", "A1ZAG4-1" ], "evidence": [ { "id": "54424", "database": "Rhea", "url": "https://www.rhea-db.org/rhea/54424" } ] }, { "id": "58224", "name": "", "equation": "L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + nicotinamide", "summary": "", "cellular_location": "", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q5U2Q4-1", "P27008-1", "Q53GL7-1", "Q8N5Y8-1", "Q7Z3E1-1", "P09874-1", "Q9UGN5-1", "Q460N3-1", "Q460N5-6", "Q9UKK3-1", "Q9NR21-4", "Q9Y6F1-1", "O95271-1", "Q9H2K2-1", "Q8CIE4-1", "Q8C1B2-1", "Q8CFF0-1", "O88554-1", "P11103-1", "Q2EMV9-1", "Q7TMM8-1", "Q3UES3-1", "Q6PFX9-1", "E9PYK3-1", "Q3ULW8-1", "Q54YW4-1", "P35875-1", "Q9VBP3-1", "A1ZAG4-1" ], "evidence": [ { "id": "58224", "database": "Rhea", "url": "https://www.rhea-db.org/rhea/58224" } ] }, { "id": "58232", "name": "", "equation": "L-seryl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-ribosyl)-L-seryl-[protein]", "summary": "", "cellular_location": "", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P27008-1", "P09874-1", "Q9UGN5-1", "P11103-1", "O88554-1", "P35875-1" ], "evidence": [ { "id": "58232", "database": "Rhea", "url": "https://www.rhea-db.org/rhea/58232" } ] }, { "id": "58236", "name": "", "equation": "L-tyrosyl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-ribosyl)-L-tyrosyl-[protein]", "summary": "", "cellular_location": "", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P27008-1", "P09874-1", "P11103-1" ], "evidence": [ { "id": "58236", "database": "Rhea", "url": "https://www.rhea-db.org/rhea/58236" } ] }, { "id": "72071", "name": "", "equation": "L-histidyl-[protein] + NAD(+) = H(+) + N(tele)-(ADP-D-ribosyl)-L-histidyl-[protein] + nicotinamide", "summary": "", "cellular_location": "", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P27008-1", "P09874-1", "P11103-1" ], "evidence": [ { "id": "72071", "database": "Rhea", "url": "https://www.rhea-db.org/rhea/72071" } ] }, { "id": "R-HSA-192916", "name": "Initiation of vRNA Synthesis", "equation": "", "summary": "Initiation of synthesis of the viral genomic RNA (vRNA) is thought to require hairpin (or panhandle/corkscrew) RNA loop structures formed by both the 5' and 3' ends of the cRNA (Pritlove, 1995; Crow, 2004; Park, 2003; Deng, 2006). The cRNA promoter has a similar structure to the vRNA promoter, but slight sequence differences are believed to result in a stronger cRNA promoter. As with the vRNA promoter, the polymerase is thought to first bind to the 5' end of the cRNA, then to the 3' end, and subsequently initiate RNA synthesis.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P09874-1" ], "evidence": [ { "id": "R-HSA-192916", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-192916" } ] }, { "id": "R-HSA-2187325", "name": "PARP1 ADP-ribosylates SMAD3 and SMAD4", "equation": "", "summary": "PARP1 ADP-ribosylates SMAD3 and SMAD4 in SMAD2/3:SMAD4 heterotrimer. ADP-ribosyl group is attached to glutamic acid residues E50 and E52 of SMAD3 and unknown amino acid residues of SMAD4. ADP-ribose monomer attached to SMAD3 and SMAD4 is subsequently extended to poly (ADP-ribosyl) chains (i.e. PAR chains) by PARP1, which is not shown here. ADP-ribosylation (PARylation) of SMAD3 and SMAD4 by PARP1 inhibits binding of SMAD2/3:SMAD4 heterotrimers to SMAD binding elements (SBEs) in promoters of SMAD-target genes.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P09874-1" ], "evidence": [ { "id": "R-HSA-2187325", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2187325" } ] }, { "id": "R-HSA-2187330", "name": "PARP1 binds SMAD2/3:SMAD4 heterotrimer", "equation": "", "summary": "PARP1 (poly [ADP-ribose] polymerase 1) binds SMAD2/3:SMAD4 heterotrimers associated with DNA SMAD-binding elements (SBEs).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P09874-1" ], "evidence": [ { "id": "R-HSA-2187330", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2187330" } ] }, { "id": "R-HSA-4551604", "name": "PIAS4 SUMOylates PARP1 with SUMO1", "equation": "", "summary": "PIAS4 SUMOylates PARP1 at lysine-203 and lysine-486 with SUMO1 (Martin et al. 2009, Matafora et al. 2009, Messner et al. 2009, Zilio et al. 2013, Impens et al. 2014). SUMOylation abrogates acetylation of PARP1 by p300 (Messner et al. 2009). PARP1 reciprocally poly(ADP-ribose)ylates PIAS4 (Martin et al. 2009). PARP1 is SUMOylated in response to heat shock and SUMOylation is required for full activation of the HSP70.1 promoter (Martin et al 2009).", "cellular_location": "nucleoplasm", "input_participant_list": [ "R-HSA-201568" ], "output_participant_list": [ "R-HSA-4551686" ], "enzyme_list": [ "P09874-1", "P63279-1", "Q8N2W9-1" ], "evidence": [ { "id": "R-HSA-4551604", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4551604" } ] }, { "id": "R-HSA-4551768", "name": "PIAS4 SUMOylates PARP1 with SUMO2,3", "equation": "", "summary": "PIAS4 SUMOylates PARP1 at lysine-203 and lysine-486 with SUMO2,3 in response to heat shock (Martin et al. 2009, Lamoliatte et al. 2013, Hendriks et al. 2014, Tammsalu et al. 2014). PARP1 reciprocally poly(ADP-ribose)ylates PIAS4 (Martin et al. 2009). SUMOylation of PARP1 is required for full activation of the HSP70.1 promoter (Martin et al. 2009).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [ "R-HSA-4551617" ], "enzyme_list": [ "P09874-1", "P63279-1", "Q8N2W9-1" ], "evidence": [ { "id": "R-HSA-4551768", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4551768" } ] }, { "id": "R-HSA-5649873", "name": "PARP1,PARP2 dimers and FEN1 bind POLB and displace APEX1 from damaged AP site", "equation": "", "summary": "Homodimers and/or heterodimers of PARP1 and PARP2 bind single strand DNA (ssDNA) ends along with FEN1 (flap endonuclease), forming a ternary complex with POLB (DNA polymerase beta) and simultaneously displacing APEX1 (Prasad et al. 2001, Lavrik et al. 2001, Cistulli et al. 2004). While PARP2 is much less catalytically active than PARP1 in DNA damage-induced poly(ADP-ribosyl) (PAR) synthesis (Shieh et al. 1998, Ame et al. 1999, Fisher et al. 2007), the functional redundancy between PARP1 and PARP2 is probably important. Knockout of both PARP1 and PARP2 homologs is embryonic lethal in mice, while knockout of individual PARPs is not (Menissier de Murcia et al. 2003).", "cellular_location": "nucleoplasm", "input_participant_list": [ "R-HSA-54745" ], "output_participant_list": [ "R-HSA-50119" ], "enzyme_list": [ "Q86W56-1", "Q9UGN5-1", "P09874-1", "P27695-1", "P39748-1", "P06746-1" ], "evidence": [ { "id": "R-HSA-5649873", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5649873" } ] }, { "id": "R-HSA-5649883", "name": "POLB-mediated DNA strand displacement synthesis", "equation": "", "summary": "DNA polymerase beta (POLB) catalyzes DNA strand displacement synthesis. In this process, 2-10 nucleotides (dNMPs) are incorporated at the 3' end of the single strand break (SSB). Simultaneously, the other broken DNA strand, which contains a 5' oxidatively-damaged AP dideoxyribose phosphate residue (5'ddRP), is displaced as a flap structure. POLB-mediated DNA strand displacement synthesis is facilitated by PARP1 and/or PARP2 dimers, which bind the single strand DNA (ssDNA) ends and FEN1 (flap endonuclease) (Klungland and Lindahl 1997, Prasad et al. 2001, Lavrik et al. 2001, Liu et al. 2005).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q9UGN5-1", "P09874-1", "P39748-1", "P06746-1" ], "evidence": [ { "id": "R-HSA-5649883", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5649883" } ] }, { "id": "R-HSA-5651723", "name": "PARP1,PARP2 dimers bound to FEN1 and POLB autoPARylate", "equation": "", "summary": "PARP1 or PARP2 homodimers or heterodimers, bound to single strand DNA (ssDNA), POLB and FEN1 at the single strand break (SSB), undergo progressive auto-PARylation causing PARP1/PARP2 to become poly(ADP-ribosyl)ated (Satoh et al. 1994, Prasad et al. 2001).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q9UGN5-1", "P09874-1", "P39748-1", "P06746-1" ], "evidence": [ { "id": "R-HSA-5651723", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5651723" } ] }, { "id": "R-HSA-5651739", "name": "PAR-PARP1,PAR-PARP2 dissociate from FEN1 and POLB", "equation": "", "summary": "Auto-PARylated (poly(ADP-ribosylated)) PARP1 or PARP2 homodimers and heterodimers dissociate from DNA at single strand breaks (SSBs). The dissociation of PARP1 and/or PARP2 is necessary for completion of the long patch base excision repair (BER). In the presence of PARP inhibitors, PARP1 and/or PARP2 cannot auto-PARylate and remain bound to SSBs. This leads to persistence of SSBs, and generation of double strand breaks (DSBs) during DNA replication (Creissen and Shall 1982, Sukhanova et al. 2004, Sukhanova et al. 2005, Pachkowski et al. 2009, Heacock et al. 2010, Strom et al. 2011).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q9UGN5-1", "P09874-1", "P39748-1", "P06746-1" ], "evidence": [ { "id": "R-HSA-5651739", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5651739" } ] }, { "id": "R-HSA-5651828", "name": "PARG dePARylates PARP1,PARP2", "equation": "", "summary": "PARG acts as a poly(ADP-ribosyl)glycohydrolase (PAR glycohydrolase) that reverses auto(ADP-ribosyl)ation of PARP1 and/or PARP2 (Kim et al. 2004). PARG activity is required for the turnover of PARP1 and/or PARP2, which allows for the rapid completion of the single strand break (SSB) repair (Fisher et al. 2007). PARG may be recruited to DNA damage site through PCNA binding (Mortusewicz et al. 2011).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [ "R-ALL-5651834" ], "enzyme_list": [ "Q86W56-1", "Q9UGN5-1", "P09874-1" ], "evidence": [ { "id": "R-HSA-5651828", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5651828" } ] }, { "id": "R-HSA-5687484", "name": "PARP1 or PARP2, FEN1 and POLQ are recruited to MMEJ site", "equation": "", "summary": "Flap endonuclease FEN1, DNA polymerase theta (POLQ) and PARP1 or PARP2 homo- or heterodimers are recruited to DNA double strand breaks (DSBs) resected by MRN and RBBP8 (CtIP) in the process of microhomology-mediated end joining (MMEJ). The mechanism of recruitment of FEN1, PARP1 (or PARP2) and POLQ, which are all necessary for MMEJ progression (Liang et al. 2005, Mansour et al. 2010, Sharma et al. 2015, Mateos-Gomez et al. 2015, Ceccaldi et al. 2015, Kent et al. 2015), is poorly defined. PARP1 (or PARP2) recognizes ssDNA. In the DNA polymerase beta (POLB)-dependent long patch base excision repair (BER), PARPs form ternary complexes with FEN1 and POLB (Prasad et al. 2001, Lavrik et al. 2001, Cistulli et al. 2004), and it is possible that a similar mechanism involving PARPs, FEN1 and POLQ operates in MMEJ. POLQ functions as a homodimer and facilitates annealing of two 3'-ssDNA overhangs through their microhomology regions. POLQ requires <20 nucleotide (nt) long resected overhangs (Kent et al. 2015). Microhomology regions are optimally 10-19 nt long (Sharma et al. 2015), and the annealing is facilitated if the microhomology region is GC-rich (Kent et al. 2015).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q9UGN5-1", "P09874-1", "P39748-1", "P49959-1", "Q99708-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5687484", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5687484" } ] }, { "id": "R-HSA-5687640", "name": "POLQ extends annealed 3'-ssDNA overhangs in MMEJ", "equation": "", "summary": "DNA polymerase theta (POLQ) extends annealed microhomologous 3'-ssDNA overhangs at DNA double strand breaks (DSBs), using opposing overhangs as templates. POLQ can perform strand displacement synthesis, extending the overhangs beyond ssDNA-dsDNA junction point, which leads to the formation of displaced strand flaps (Kent et al. 2015). PARP1 (or possibly PARP2) is necessary for the recruitment of POLQ to DNA DSBs. POLQ-mediated DNA synthesis during microhomology mediated end joining (MMEJ) (also known as alternative nonhomologous end joining or alt-NHEJ or theta-mediated end joining - TMEJ) counteracts homologous recombination repair (HRR) and promotes survival of cells with a compromised HR pathway (Mateos-Gomez et al. 2015). POLQ is error-prone and introduces single nucleotide substitutions during DNA synthesis. HRR-deficient epithelial ovarian cancers frequently overexpress POLQ, which correlates with an increased frequency of somatic point mutations in these tumors (Ceccaldi et al. 2015).

BRCA2 regulates DSB repair pathway choice independent of RAD51 (Han et al. 2017) by inhibiting DNA polymerase theta-mediated end-joining (TMEJ) during the S and G2 phases of the cell cycle until M phase (Llorens-Agost et al. 2021). In BRCA2-deficient cells, TMEJ is inhibited by RAD52. Loss of RAD52 in BRCA2-deficient cells, leads to inappropriate DSB repair by TMEJ and cell death providing a rationale for the synthetic lethality of BRCA2 and RAD52 deficiencies (Llorens-Agost et al. 2021).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q9UGN5-1", "P09874-1", "P39748-1", "P49959-1", "Q99708-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5687640", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5687640" } ] }, { "id": "R-HSA-5687653", "name": "PARP1,PARP2 dimers bound to MMEJ sites autoPARylate", "equation": "", "summary": "PARP inihibitors that block catalytic activity of PARP1 (or PARP2) bound to single-stranded DNA (ssDNA), including PARP1 and PARP2 autoPARylation (auto-polyADPribosylation), also inhibit microhomology-mediated end joining (MMEJ). Thus, the catalytic activity of PARP1 (or PARP2), related to autoPARylation or PARylation of other proteins at MMEJ site, is necessary for the progression of MMEJ (Mansour et al. 2010, Ceccaldi et al. 2015). By analogy with the DNA polymerase beta (POLB)-dependent long patch base excision repair (Satoh et al. 1994, Prasad et al. 2001), autoPARylated PARPs dissociate from the repair site, thereby coordinating the termination of strand displacement DNA synthesis and the cleavage of displaced strand flaps by FEN1.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q9UGN5-1", "P09874-1", "P39748-1", "P49959-1", "Q99708-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5687653", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5687653" } ] }, { "id": "R-HSA-5689317", "name": "Formation of the pre-incision complex in GG-NER", "equation": "", "summary": "Once an open bubble structure is generated in damaged dsDNA through a DNA helicase activity of the TFIIH complex, the RPA heterotrimer composed of RPA1, RPA2 and RPA3, coats the undamaged single strand DNA (ssDNA) (de Laat et al. 1998), thereby protecting it from incision and enabling the correct positioning of the NER endonucleases. The interaction of RPA with XPA facilitates RPA recruitment to the global genome nucleotide excision repair (GG-NER) site (He et al. 1995, Ikegami et al. 1998). A DNA endonuclease ERCC5 (XPG) is recruited to the GG-NER site, 3' to the DNA damage, through its interaction with the TFIIH complex (Dunand-Sauthier et al. 2005, Zotter et al. 2006, Ito et al. 2007) and the RPA heterotrimer (de Laat et al. 1998).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P62877-1", "P18074-1", "P28715-1", "Q9UGN5-1", "P09874-1", "Q86WJ1-1", "P19447-1" ], "evidence": [ { "id": "R-HSA-5689317", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689317" } ] }, { "id": "R-HSA-5689861", "name": "Recruitment of XPA and release of CAK", "equation": "", "summary": "XPA binds the DNA damage site through interaction with the TFIIH complex subunit GTF2H5 (TTDA) (Ziani et al. 2014), and also interacts with the DDB2 subunit of the UV-DDB complex (Wakasugi et al. 2001, Wakasugi et al. 2009, Takedachi et al. 2010). PARylated PARP1 (or possibly PARP2) (King et al. 2012) facilitates XPA association with chromatin. Binding of XPA is accompanied by the release of the CAK subcomplex from the TFIIH complex (Coin et al. 2008).", "cellular_location": "nucleoplasm", "input_participant_list": [ "R-HSA-67437" ], "output_participant_list": [ "R-HSA-69221" ], "enzyme_list": [ "P62877-1", "P18074-1", "Q9UGN5-1", "P09874-1", "P50613-1", "P19447-1" ], "evidence": [ { "id": "R-HSA-5689861", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689861" } ] }, { "id": "R-HSA-5690213", "name": "DNA polymerases delta, epsilon or kappa bind the GG-NER site", "equation": "", "summary": "The DNA repair synthesis complex, consisting of PCNA, RFC, RPA and polymerase delta (POLD) or epsilon (POLE) complexes, or DNA translesion synthesis polymerase kappa (POLK) (Ogi et al. 2010), is formed at the nucleotide excision repair (NER) site following the incision of the damaged DNA strand 5' to the lesion by the ERCC1:ERCC4 (ERCC1:XPF) complex. 3' incision by XPG (ERCC5) is not required for the loading of the DNA polymerases and may not be required for the initiation of NER-mediated DNA synthesis (Staresincic et al. 2009). XPG and RPA promote the assembly of the DNA synthesis complex at the NER site (Mocquet et al. 2008).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q92889-1", "P62877-1", "P28340-1", "Q07864-1", "P18074-1", "P28715-1", "Q9UGN5-1", "Q9UBT6-1", "P09874-1", "Q86WJ1-1", "P19447-1" ], "evidence": [ { "id": "R-HSA-5690213", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5690213" } ] }, { "id": "R-HSA-5690988", "name": "3'-incision of DNA by ERCC5 (XPG) in GG-NER", "equation": "", "summary": "In global genome nucleotide excision repair (GG-NER), as well as transcription-coupled nucleotide excision repair (TC-NER), the cleavage of the damaged DNA strand 3' to the site of damage is carried out by a DNA endonuclease XPG (ERCC5). While the DNA repair synthesis may be initiated prior to the 3' incision (Staresincic et al. 2009), the components of the incision complex probably dissociate from the NER site shortly after the replicative complex assembly and 3' incision (Overmeer et al. 2011). The exception is the RPA heterotrimer, which is a constituent of the DNA synthesis complex, and also coats the undamaged DNA strand, thereby protecting it from endonucleolytic cleavage.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q92889-1", "P62877-1", "P28340-1", "Q07864-1", "P18074-1", "P28715-1", "Q9UGN5-1", "Q9UBT6-1", "P09874-1", "Q86WJ1-1", "P19447-1" ], "evidence": [ { "id": "R-HSA-5690988", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5690988" } ] }, { "id": "R-HSA-5690990", "name": "5'- incision of DNA by ERCC1:ERCC4 in GG-NER", "equation": "", "summary": "In global genome nucleotide excision repair (GG-NER), just like in transcription-coupled nucleotide excision repair (TC-NER), the cleavage of the damaged strand of DNA 5' to the site of damage occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex is unwound. The 5' incision is carried out by the ERCC1:XPF (ERCC1:ERCC4) complex and precedes the 3' incision (Staresincic et al. 2009).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q92889-1", "P62877-1", "P18074-1", "P28715-1", "Q9UGN5-1", "P09874-1", "Q86WJ1-1", "P19447-1" ], "evidence": [ { "id": "R-HSA-5690990", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5690990" } ] }, { "id": "R-HSA-5690991", "name": "Binding of ERCC1:ERCC4 (ERCC1:XPF) to pre-incision complex in GG-NER", "equation": "", "summary": "ERCC1:ERCC4 (ERCC1:XPF) DNA endonuclease complex binds 5' to the DNA damage at global genome nucleotide excision repair (GG-NER) sites to form the incision complex. Binding of ERCC5 (XPG) to the NER site precedes the recruitment of ERCC1:ERCC4 (Riedl et al. 2003). ERCC1 directly interacts with XPA, and this interaction is necessary for the loading of ERCC1:ERCC4 to the open bubble structure in damaged dsDNA and the progression of GG-NER (Tsodikov et al. 2007, Orelli et al. 2010).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q92889-1", "P62877-1", "P18074-1", "P28715-1", "Q9UGN5-1", "P09874-1", "Q86WJ1-1", "P19447-1" ], "evidence": [ { "id": "R-HSA-5690991", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5690991" } ] }, { "id": "R-HSA-5690996", "name": "ERCC2 and ERCC3 DNA helicases form an open bubble structure in damaged DNA", "equation": "", "summary": "Two DNA helicases XPB (ERCC3) and XPD (ERCC2), which are part of the TFIIH complex, unwind the distorted DNA duplex around the lesion to form an open bubble structure that exposes the damaged site. The helicase activity of the TFIIH complex is stimulated by the presence of XPA and the XPC:RAD23:CETN2 complex (Winkler et al. 2001). The 5'->3' directed helicase activity of ERCC2 (Kuper et al. 2012) is crucial for unwinding of the distorted dsDNA during nucleotide excision repair (NER) (Coin et al. 2007). The 3'->5' directed DNA helicase ERCC3 contributes to dsDNA unwinding during NER through ATP hydrolysis (Coin et al. 2007). In addition to DNA unwinding, ERCC2 and ERCC3 verify the presence of DNA damage (Oksenych et al. 2009, Mathieu et al. 2010, Mathieu et al. 2013). Verification of DNA damage also involves XPA (Camenisch et al. 2006). The binding site of XPC determines which DNA strand is selected by ERCC2 to verify the presence of lesions (Sugasawa et al. 2009).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P62877-1", "P18074-1", "Q9UGN5-1", "P09874-1", "Q86WJ1-1", "P19447-1" ], "evidence": [ { "id": "R-HSA-5690996", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5690996" } ] }, { "id": "R-HSA-5691000", "name": "TFIIH binds GG-NER site to form a verification complex", "equation": "", "summary": "Transcription factor II H (TFIIH) complex is recruited to DNA damage sites after the damage is recognized by the XPC:RAD23:CETN2 complex and the UV-DDB complex (DDB1:DDB2) (Volker et al. 2001, Araujo and Wood 1999).

TFIIH consists of ten subunits organized into a ring-like structure (Schultz et al. 2000). The TFIIH core, also forming a ring-like structure, includes a DNA helicase ERCC3 (XPB), GTF2H1 (BTF2-p62), GTF2H2 (BTF2-p44), GTF2H3 (BTF2-p34) and GTF2H4 (BTF2-p52). GTF2H4 directly interacts with ERCC3 and anchors it to the TFIIH complex (Jawhari et al. 2002). Another DNA helicase, ERCC2 (XPD) is anchored to the TFIIH complex by binding to the GTF2H2 subunit (Coin et al. 1998). The CDK-activating kinase (CAK) complex, consisting of CCNH (cyclin H), CDK7 and MNAT1 (MAT1) is included in the TFIIH complex through an interaction with ERCC2 (Reardon et al. 1996, Rossignol et al. 1997). The tenth subunit, GTF2H5 (TTDA, TFB5, BTF2-p5) is important for the stability of the TFIIH complex (Giglia-Mari et al. 2004). The TFIIH complex binds the DNA damage site after XPC:RAD23:CETN2 complex recognizes the damage (Volker et al. 2001, Riedl et al. 2003), and the ERCC3 and GTF2H1 subunits of TFIIH directly interact with XPC (Yokoi et al. 2003).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P62877-1", "P18074-1", "Q9UGN5-1", "P09874-1", "P50613-1", "P19447-1" ], "evidence": [ { "id": "R-HSA-5691000", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5691000" } ] }, { "id": "R-HSA-5696655", "name": "PARP1 or PARP2 PARylates DDB2 and autoPARylates", "equation": "", "summary": "PARP1 and/or PARP2 homo- or heterodimers recruited to global genomic nucleotide excision repair (GG-NER) site poly(ADP)ribosylate (PARylate) DDB2 and also progressively autoPARylate. PARylation promotes retention of DDB2 at DNA damage sites (Pines et al. 2012, Robu et al. 2013).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P62877-1", "Q9UGN5-1", "P09874-1" ], "evidence": [ { "id": "R-HSA-5696655", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5696655" } ] }, { "id": "R-HSA-5696664", "name": "PARP1 or PARP2 binds DDB2 at GG-NER site", "equation": "", "summary": "PARP1 (or PARP2) is recruited to global genomic nucleotide excision repair (GG-NER) site through interaction with DDB2 and, probably, distorted single strand DNA (Pines et al. 2012, Robu et al. 2013).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P62877-1", "Q9UGN5-1", "P09874-1" ], "evidence": [ { "id": "R-HSA-5696664", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5696664" } ] }, { "id": "R-HSA-5696670", "name": "CHD1L is recruited to GG-NER site", "equation": "", "summary": "A chromatin remodeling enzyme CHD1L (ALC1) is recruited to DNA damage sites through interaction with PARylated PARP1 (or possibly PARP2) (Ahel et al. 2009) or PARylated DDB2 (Pines et al. 2012). CHD1L catalyzes PARP-stimulated nucleosome sliding and is needed for efficient PARP-dependent DNA repair (Ahel et al. 2009). CHD1L depletion or PARP inhibition impair global genomic nucleotide excision repair (GG-NER) of UV-induced DNA damage (Pines et al. 2012).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P62877-1", "P18074-1", "Q9UGN5-1", "P09874-1", "Q86WJ1-1", "P19447-1" ], "evidence": [ { "id": "R-HSA-5696670", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5696670" } ] }, { "id": "R-HSA-6790454", "name": "SUMOylation of XPC", "equation": "", "summary": "XPC undergoes SUMOylation following UV irradiation on several consensus SUMOylation sites (van Cuijk et al. 2015). SUMOylation of XPC probably succeeds the UV-DDB mediated ubiquitination of XPC, as the presence of both DDB2 and XPA is required for SUMOylation (Wang et al. 2005), but it has also been reported that SUMOylation of XPC was DDB2-independent (Akita et al. 2015). It is unclear whether XPC is modified by SUMO1 (Wang et al. 2005, Akita et al. 2015) or poly-SUMO2/3 (Poulsen et al. 2013). SUMO conjugases PIAS1 and PIAS3 both interact with XPC and may catalyze XPC SUMOylation (Akita et al. 2015).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P62877-1", "P18074-1", "Q9UGN5-1", "P09874-1", "P63279-1", "Q86WJ1-1", "O75925-1", "P19447-1", "Q9Y6X2-1" ], "evidence": [ { "id": "R-HSA-6790454", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6790454" } ] }, { "id": "R-HSA-6790487", "name": "RNF111 ubiquitinates SUMOylated XPC", "equation": "", "summary": "SUMOylated XPC is recognized by the SUMO-targeted ubiquitin ligase RNF111 (Arcadia) that, together with the E2 ubiquitin conjugating complex of UBE2N (UBC13) and UBE2V2 (MMS2), generates K63-linked polyubiquitin chains on XPC (Poulsen et al. 2013) to efficiently release XPC from UV lesions (van Cuijk et al. 2015). The release of K63-polyubiquitinated XPC occurs from GG-NER pre-incision complexes that contain TFIIH and XPA and promotes optimal access/binding of ERCC5 (XPG) endonuclease to the pre-incision complex (van Cuijk et al. 2015). Successful binding of ERCC5 endonuclease 3' to the damage facilitates binding of the ERCC1:ERCC4 (ERCC1:XPF) endonuclease and progression of the NER reaction.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P62877-1", "P18074-1", "Q9UGN5-1", "P09874-1", "Q86WJ1-1", "P61088-1", "Q6ZNA4-1", "P19447-1" ], "evidence": [ { "id": "R-HSA-6790487", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6790487" } ] } ], "reaction_participants": [ { "participant_id": "R-ALL-5651834", "participant_name": "ADP-D-ribose [nucleoplasm]", "crossref": [ { "id": "16960", "database": "ChEBI", "url": "" }, { "id": "C00301", "database": "COMPOUND", "url": "" }, { "id": "000014880207", "database": "ZINC", "url": "" }, { "id": "000017654550", "database": "ZINC", "url": "" }, { "id": "HMDB0001178", "database": "HMDB Metabolite", "url": "" }, { "id": "000014880207", "database": "ZINC", "url": "" }, { "id": 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"database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P50613" } ] }, { "ec_number": "2.7.11.22", "activity": "", "evidence": [ { "id": "P50613", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P50613" } ] } ] }, { "uniprot_ac": "P61088", "gene_name": "UBE2N", "activity": [ { "ec_number": "2.3.2.23", "activity": "S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.", "evidence": [ { "id": "P61088", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P61088" } ] }, { "ec_number": "2.3.2.23", "activity": "", "evidence": [ { "id": "P61088", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P61088" } ] } ] }, { "uniprot_ac": "P62877", "gene_name": "RBX1", "activity": [ { "ec_number": "2.3.2.27", "activity": "S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor 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