{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9UGN5","secondaryAccessions":["Q8TEU4","Q9NUV2","Q9UMR4","Q9Y6C8"],"uniProtkbId":"PARP2_HUMAN","entryAudit":{"firstPublicDate":"2001-09-26","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2001-09-26","entryVersion":220,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Poly [ADP-ribose] polymerase 2"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"26704974"}],"value":"PARP-2"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"26704974"}],"value":"hPARP-2"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25043379"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30104678"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30321391"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32939087"}],"value":"2.4.2.30"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"30321391"}],"value":"ADP-ribosyltransferase diphtheria toxin-like 2"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"30321391"}],"value":"ARTD2"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"DNA ADP-ribosyltransferase PARP2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27471034"}],"value":"2.4.2.-"}]},{"fullName":{"value":"NAD(+) ADP-ribosyltransferase 2"},"shortNames":[{"value":"ADPRT-2"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10338144"}],"value":"Poly[ADP-ribose] synthase 2"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10338144"}],"value":"pADPRT-2"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Protein poly-ADP-ribosyltransferase PARP2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25043379"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32939087"}],"value":"2.4.2.-"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"20092359"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:272"}],"value":"PARP2"},"synonyms":[{"value":"ADPRT2"},{"value":"ADPRTL2"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10364231"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25043379"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27471034"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28190768"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29361132"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30104678"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30321391"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32028527"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32939087"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34108479"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34486521"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34732825"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34795260"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34874266"}],"value":"Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:10364231, PubMed:25043379, PubMed:27471034, PubMed:30104678, PubMed:32028527, PubMed:32939087, PubMed:34108479, PubMed:34486521, PubMed:34874266). Mediates glutamate, aspartate or serine 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:25043379, PubMed:30104678, PubMed:30321391). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:32939087). Mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1 (PubMed:25043379). Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP2 active site (PubMed:28190768, PubMed:32028527, PubMed:34108479, PubMed:34486521, PubMed:34874266). PARP2 initiates the repair of double-strand DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (PubMed:10364231, PubMed:32939087, PubMed:34108479). HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP2 in order to limit the length of poly-ADP-ribose chains (PubMed:34732825, PubMed:34795260). Specifically mediates formation of branched poly-ADP-ribosylation (PubMed:30104678). Branched poly-ADP-ribose chains are specifically recognized by some factors, such as APLF (PubMed:30104678). In addition to proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex (PubMed:27471034, PubMed:29361132)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).","ecNumber":"2.4.2.30","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25043379"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30104678"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30321391"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32939087"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + NAD(+) = O-(ADP-D-ribosyl)-L-seryl-[protein] + nicotinamide + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:58232"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:15091"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17154"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:142556"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32028527"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32939087"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34108479"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28190768"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:58233"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32028527"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32939087"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34108479"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28190768"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamide","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54424"},{"database":"Rhea","id":"RHEA-COMP:9867"},{"database":"Rhea","id":"RHEA-COMP:13832"},{"database":"ChEBI","id":"CHEBI:17154"},{"database":"ChEBI","id":"CHEBI:29961"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:138102"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25043379"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54425"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25043379"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + nicotinamide","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:58224"},{"database":"Rhea","id":"RHEA-COMP:10208"},{"database":"Rhea","id":"RHEA-COMP:15089"},{"database":"ChEBI","id":"CHEBI:17154"},{"database":"ChEBI","id":"CHEBI:29973"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:142540"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25043379"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:58225"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25043379"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33275888"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34108479"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35349716"}],"value":"ADP-ribosyltransferase activity is regulated via an allosteric activation mechanism (PubMed:34108479). In absence of activation signal, PARP2 is autoinhibited by the PARP alpha-helical domain (also named HD region), which prevents effective NAD(+)-binding (PubMed:34108479). Activity is highly stimulated by signals, which unfold the PARP alpha-helical domain, relieving autoinhibition (PubMed:34108479). Poly-ADP-ribosyltransferase activity is tightly regulated and PARP2 is removed from damaged chromatin following initial poly-ADP-ribosylation of chromatin to avoid prolonged residence (trapping) that has cytotoxic consequences (PubMed:33275888). CHD1L promotes PARP2 removal from chromatin (PubMed:33275888). ADP-ribosyltransferase activity is inhibited by a number of PARP inhibitors (PARPi) compounds, that are used the treatment of breast or ovarian cancers that have defects in DNA repair by homologous recombination (PubMed:35349716). PARPi molecules (niraparib, talazoparib, and, to a lesser extent, olaparib) also trap PARP2 at DNA damage sites (PubMed:33275888, PubMed:35349716)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O88554"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20092359"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27067600"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28190768"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32028527"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32939087"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33141820"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34108479"}],"value":"Component of a base excision repair (BER) complex, containing at least XRCC1, PARP1, POLB and LRIG3 (By similarity). Homo- and heterodimer with PARP1 (PubMed:20092359). Interacts (via the PARP catalytic domain) with HPF1 (PubMed:27067600, PubMed:28190768, PubMed:32028527, PubMed:32939087, PubMed:33141820, PubMed:34108479). Interacts with core nucleosomes (PubMed:32939087, PubMed:33141820)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q9UGN5","intActId":"EBI-2795348"},"interactantTwo":{"uniProtKBAccession":"Q8IW19","geneName":"APLF","intActId":"EBI-1256044"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9UGN5","intActId":"EBI-2795348"},"interactantTwo":{"uniProtKBAccession":"Q00688","geneName":"FKBP3","intActId":"EBI-1044081"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9UGN5","intActId":"EBI-2795348"},"interactantTwo":{"uniProtKBAccession":"P05204","geneName":"HMGN2","intActId":"EBI-1758689"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9UGN5","intActId":"EBI-2795348"},"interactantTwo":{"uniProtKBAccession":"Q99469","geneName":"STAC","intActId":"EBI-2652799"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26704974"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30104678"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30321391"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32939087"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33141820"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35349716"}],"value":"Recruited to DNA damage sites in a PARP1-dependent process: recognizes and binds poly-ADP-ribose chains produced by PARP1 at DNA damage sites via its N-terminus, leading to its recruitment"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10364231"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26704974"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26704974"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30104678"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30321391"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32939087"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33141820"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35349716"}],"value":"Chromosome","id":"SL-0468"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q9UGN5-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q9UGN5-2"],"sequenceIds":["VSP_004537"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10364231"}],"value":"Widely expressed, mainly in actively dividing tissues (PubMed:10364231). The highest levels are in the brain, heart, pancreas, skeletal muscle and testis; also detected in kidney, liver, lung, placenta, ovary and spleen; levels are low in leukocytes, colon, small intestine, prostate and thymus (PubMed:10364231)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30104678"}],"value":"The N-terminal region (NTR) recognizes and binds poly-ADP-ribose chains produced by PARP1, leading to its recruitment to DNA damage sites"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26704974"}],"value":"The N-terminal disordered region does not act as a key DNA-binding domain (PubMed:26704974). The WGR and PARP catalytic domains function together to recruit PARP2 to sites of DNA breaks. The N-terminal disordered region is only required for activation on specific types of DNA damage (PubMed:26704974)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30321391"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32939087"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33141820"}],"value":"The WGR domain bridges two nucleosomes, with the broken DNA aligned in a position suitable for ligation (PubMed:30321391, PubMed:32939087, PubMed:33141820). The bridging induces structural changes in PARP2 that signal the recognition of a DNA break to the catalytic domain of PARP2, promoting HPF1 recruitment and subsequent activation of PARP2, licensing serine ADP-ribosylation of target proteins (PubMed:32939087)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34108479"}],"value":"The PARP alpha-helical domain (also named HD region) prevents effective NAD(+)-binding in absence of activation signal (PubMed:34108479). Binding to damaged DNA unfolds the PARP alpha-helical domain, relieving autoinhibition (PubMed:34108479)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O88554"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32939087"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34108479"}],"value":"Auto poly-ADP-ribosylated on serine residues, leading to dissociation of the PARP2-HPF1 complex from chromatin (PubMed:32939087, PubMed:34108479). Poly-ADP-ribosylated by PARP1 (By similarity)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O88554"}],"value":"Acetylation reduces DNA binding and enzymatic activity"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O88554"}],"value":"Proteolytically cleaved by caspase-8 (CASP8) in response to apoptosis, leading to its inactivation"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the ARTD/PARP family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"AAD29857.1","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous gene model prediction","sequence":"AAL77437.1","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"CAB41505.2","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"WEB RESOURCE","resourceName":"Protein Spotlight","resourceUrl":"https://www.proteinspotlight.org/back_issues/235/","ftp":false,"note":"Catalysis - Issue 235 of April 2021"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":583,"modifier":"EXACT"}},"description":"Poly [ADP-ribose] polymerase 2","featureId":"PRO_0000211327"},{"type":"Domain","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"WGR","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01321"}]},{"type":"Domain","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"PARP 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dbSNP:rs3093925","featureCrossReferences":[{"database":"dbSNP","id":"rs3093925"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.5"}],"featureId":"VAR_019177","alternativeSequence":{"originalSequence":"I","alternativeSequences":["V"]}},{"type":"Natural variant","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"in dbSNP:rs3093926","featureCrossReferences":[{"database":"dbSNP","id":"rs3093926"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.5"}],"featureId":"VAR_019178","alternativeSequence":{"originalSequence":"R","alternativeSequences":["Q"]}},{"type":"Natural variant","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"in 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