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Entry version 243 (16 Oct 2019)
Sequence version 4 (23 Jan 2007)
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Protein

Poly [ADP-ribose] polymerase 1

Gene

PARP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:17177976, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:23230272, PubMed:25043379, PubMed:26344098). Mainly mediates glutamate and aspartate ADP-ribosylation of target proteins: the ADP-D-ribosyl group of NAD+ is transferred to the acceptor carboxyl group of glutamate and aspartate 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). Mediates the poly(ADP-ribosyl)ation of a number of proteins, including itself, APLF and CHFR (PubMed:17396150, PubMed:19764761). Also mediates serine ADP-ribosylation of target proteins following interaction with HPF1; HPF1 conferring serine specificity (PubMed:28190768). Probably also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1 (PubMed:30257210). Catalyzes the poly-ADP-ribosylation of histones in a HPF1-dependent manner (PubMed:27067600). Involved in the base excision repair (BER) pathway by catalyzing the poly-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism (PubMed:17177976, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:23230272). ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks (PubMed:17177976, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:23230272). 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). 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). Acts as a regulator of transcription: positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150 (PubMed:19344625). With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production (PubMed:17177976). 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).17 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 390 sec(-1) for NAD+.1 Publication
  1. KM=130 µM for NAD+1 Publication

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi2 – 3721 PublicationAdd BLAST371
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri9 – 93PARP-type 1PROSITE-ProRule annotationAdd BLAST85
    Zinc fingeri113 – 203PARP-type 2PROSITE-ProRule annotationAdd BLAST91

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionDNA-binding, Glycosyltransferase, Transferase
    Biological processDNA damage, DNA repair, Transcription, Transcription regulation
    LigandMetal-binding, NAD, Zinc

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.4.2.30 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-110362 POLB-Dependent Long Patch Base Excision Repair
    R-HSA-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
    R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
    R-HSA-5685939 HDR through MMEJ (alt-NHEJ)
    R-HSA-5696394 DNA Damage Recognition in GG-NER
    R-HSA-5696395 Formation of Incision Complex in GG-NER
    R-HSA-5696400 Dual Incision in GG-NER

    SignaLink: a signaling pathway resource with multi-layered regulatory networks

    More...
    SignaLinki
    P09874

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    P09874

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Poly [ADP-ribose] polymerase 1 (EC:2.4.2.306 Publications)
    Short name:
    PARP-1
    Alternative name(s):
    ADP-ribosyltransferase diphtheria toxin-like 1
    Short name:
    ARTD1
    DNA ADP-ribosyltransferase PARP1Curated (EC:2.4.2.-1 Publication)
    NAD(+) ADP-ribosyltransferase 11 Publication
    Short name:
    ADPRT 11 Publication
    Poly[ADP-ribose] synthase 1
    Protein poly-ADP-ribosyltransferase PARP1Curated (EC:2.4.2.-2 Publications)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:PARP1Imported
    Synonyms:ADPRT1 Publication, PPOL
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:270 PARP1

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    173870 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P09874

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Chromosome, Nucleus

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi490 – 493VEVV → GEVQ: Strongly reduced interaction with TIMELESS. 1 Publication4
    Mutagenesisi499S → A: Abolishes automodification on serine following interaction with HPF1; when associated with A-507 and A-519. 1 Publication1
    Mutagenesisi507S → A: Abolishes automodification on serine following interaction with HPF1; when associated with A-499 and A-519. 1 Publication1
    Mutagenesisi519S → A: Abolishes automodification on serine following interaction with HPF1; when associated with A-499 and A-507. 1 Publication1
    Mutagenesisi797L → P: 1.5% of wild-type activity. 1 Publication1
    Mutagenesisi850 – 851Missing : Abolished interaction with TIMELESS. 1 Publication2
    Mutagenesisi862H → A: Poly-ADP-ribosyltransferase activity is impaired while mono-ADP-ribosyltransferase activity is not affected; produces a mixture of short and mono ADP-ribose chains. 1 Publication1
    Mutagenesisi868N → S: 4% of wild-type activity. 1 Publication1
    Mutagenesisi883E → Q: Does not affect ADP-ribosyltransferase activity. 1 Publication1
    Mutagenesisi890M → V: <0.5% of wild-type activity. 1 Publication1
    Mutagenesisi893K → I: Abolishes enzymatic activity. 1 Publication1
    Mutagenesisi897F → S: 10% of wild-type activity. 1 Publication1
    Mutagenesisi899D → N: 0.6% of wild-type activity. 1 Publication1
    Mutagenesisi908C → R: <0.5% of wild-type activity. 1 Publication1
    Mutagenesisi923E → Q: Does not affect ADP-ribosyltransferase activity. 1 Publication1
    Mutagenesisi926L → F: 1.5% of wild-type activity. 1 Publication1
    Mutagenesisi931E → Q: Does not affect ADP-ribosyltransferase activity. 1 Publication1
    Mutagenesisi986Y → H: 14% of wild-type activity and increased branching 15-fold. 1 Publication1
    Mutagenesisi988E → A, D, Q or K: Poly-ADP-ribosyltransferase activity is inhibited while mono-ADP-ribosyltransferase activity is not affected; only monomers are added. 2 Publications1
    Mutagenesisi993D → G: Abolished interaction with TIMELESS. 1 Publication1
    Mutagenesisi1003L → P: 1.5% of wild-type activity. 1

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    142

    Open Targets

    More...
    OpenTargetsi
    ENSG00000143799

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA32

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    P09874

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3105

    Drug and drug target database

    More...
    DrugBanki
    DB04010 2-(3'-Methoxyphenyl) Benzimidazole-4-Carboxamide
    DB03509 2-(4-Chlorophenyl)-5-Quinoxalinecarboxamide
    DB03072 2-{3-[4-(4-Fluorophenyl)-3,6-Dihydro-1(2h)-Pyridinyl]Propyl}-8-Methyl-4(3h)-Quinazolinone
    DB03722 3,4-Dihydro-5-Methyl-Isoquinolinone
    DB03073 3-Methoxybenzamide
    DB07787 5-FLUORO-1-[4-(4-PHENYL-3,6-DIHYDROPYRIDIN-1(2H)-YL)BUTYL]QUINAZOLINE-2,4(1H,3H)-DIONE
    DB07096 6-AMINO-BENZO[DE]ISOQUINOLINE-1,3-DIONE
    DB02498 Carba-Nicotinamide-Adenine-Dinucleotide
    DB13877 Iniparib
    DB02701 Nicotinamide
    DB11793 Niraparib
    DB02690 NU1025
    DB09074 Olaparib
    DB12332 Rucaparib
    DB11760 Talazoparib
    DB00277 Theophylline
    DB07330 trans-4-(7-carbamoyl-1H-benzimidazol-2-yl)-1-propylpiperidinium
    DB07232 Veliparib
    DB01593 Zinc
    DB14487 Zinc acetate
    DB14533 Zinc chloride

    DrugCentral

    More...
    DrugCentrali
    P09874

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    2771

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    PARP1

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    130781

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002113202 – 1014Poly [ADP-ribose] polymerase 1Add BLAST1013

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1 Publication1
    Modified residuei41PhosphoserineCombined sources1
    Modified residuei97N6-acetyllysineCombined sources1
    Modified residuei105N6-acetyllysineCombined sources1
    Modified residuei131N6-acetyllysineCombined sources1
    Modified residuei177PhosphoserineCombined sources1
    Modified residuei179PhosphoserineCombined sources1
    Modified residuei185PhosphoserineCombined sources1
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki192Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Cross-linki203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
    Cross-linki203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
    Cross-linki249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Modified residuei274PhosphoserineCombined sources1
    Modified residuei277PhosphoserineCombined sources1
    Modified residuei364PhosphoserineCombined sources1
    Modified residuei368PhosphothreonineCombined sources1
    Modified residuei387PolyADP-ribosyl aspartic acid1 Publication1
    Modified residuei407PolyADP-ribosyl glutamic acidSequence analysis1
    Modified residuei413PolyADP-ribosyl glutamic acidSequence analysis1
    Modified residuei435PolyADP-ribosyl glutamic acidSequence analysis1
    Modified residuei437PolyADP-ribosyl glutamic acidSequence analysis1
    Modified residuei444PolyADP-ribosyl glutamic acidSequence analysis1
    Modified residuei445PolyADP-ribosyl glutamic acidSequence analysis1
    Modified residuei448PolyADP-ribosyl glutamic acidSequence analysis1
    Modified residuei456PolyADP-ribosyl glutamic acidSequence analysis1
    Cross-linki467Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Modified residuei471PolyADP-ribosyl glutamic acidSequence analysis1
    Modified residuei484PolyADP-ribosyl glutamic acidSequence analysis1
    Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
    Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
    Modified residuei488PolyADP-ribosyl glutamic acid1 Publication1
    Modified residuei491PolyADP-ribosyl glutamic acid1 Publication1
    Modified residuei499ADP-ribosylserine1 Publication1
    Modified residuei507ADP-ribosylserine1 Publication1
    Cross-linki512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Modified residuei513PolyADP-ribosyl glutamic acidSequence analysis1
    Modified residuei514PolyADP-ribosyl glutamic acidSequence analysis1
    Modified residuei519ADP-ribosylserine1 Publication1
    Modified residuei520PolyADP-ribosyl glutamic acidSequence analysis1
    Cross-linki528Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Modified residuei600N6-acetyllysineCombined sources1
    Modified residuei621N6-acetyllysineCombined sources1
    Cross-linki748Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
    Cross-linki748Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
    Modified residuei782PhosphoserineCombined sources1
    Modified residuei786PhosphoserineCombined sources1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Phosphorylated by PRKDC and TXK.2 Publications
    Poly-ADP-ribosylated on glutamate and aspartate residues by autocatalysis (PubMed:19764761). Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites (PubMed:19661379). ADP-ribosylated on serine by autocatalysis; serine ADP-ribosylation takes place following interaction with HPF1 (PubMed:28190768).3 Publications
    S-nitrosylated, leading to inhibit transcription regulation activity.By similarity

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    The CPTAC Assay portal

    More...
    CPTACi
    CPTAC-3240
    CPTAC-3241
    CPTAC-556
    CPTAC-557

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P09874

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P09874

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    P09874

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P09874

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P09874

    PeptideAtlas

    More...
    PeptideAtlasi
    P09874

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P09874

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    52271

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...
    SWISS-2DPAGEi
    P09874

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P09874

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P09874

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P09874

    Miscellaneous databases

    CutDB - Proteolytic event database

    More...
    PMAP-CutDBi
    P09874

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000143799 Expressed in 233 organ(s), highest expression level in heart left ventricle

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P09874 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P09874 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB000147
    CAB003839
    CAB003840
    CAB075726
    CAB075727
    HPA045168

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homo- and heterodimer with PARP2.

    Interacts with APTX (PubMed:15044383).

    Component of a base excision repair (BER) complex, containing at least XRCC1, PARP1, PARP2, POLB and LRIG3 (By similarity).

    Interacts with SRY (PubMed:16904257). The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70 (By similarity).

    Interacts with TIAM2 (By similarity).

    Interacts with PARP3; leading to activate PARP1 in absence of DNA (PubMed:20064938).

    Interacts (when poly-ADP-ribosylated) with CHD1L (PubMed:19661379).

    Interacts with the DNA polymerase alpha catalytic subunit POLA1; this interaction functions as part of the control of replication fork progression (PubMed:9518481).

    Interacts with EEF1A1 and TXK (PubMed:17177976).

    Interacts with RNF4 (PubMed:19779455).

    Interacts with RNF146 (PubMed:21799911).

    Interacts with ZNF423 (PubMed:22863007).

    Interacts with APLF (PubMed:17396150).

    Interacts with SNAI1 (via zinc fingers); the interaction requires SNAI1 to be poly-ADP-ribosylated and non-phosphorylated (active) by GSK3B (PubMed:21577210).

    Interacts (when poly-ADP-ribosylated) with PARP9 (PubMed:23230272).

    Interacts with NR4A3; activates PARP1 by improving acetylation of PARP1 and suppressing the interaction between PARP1 and SIRT1 (By similarity).

    Interacts (via catalytic domain) with PUM3; the interaction inhibits the poly-ADP-ribosylation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress (PubMed:21266351).

    Interacts (via the PARP catalytic domain) with HPF1 (PubMed:27067600, PubMed:28190768).

    Interacts with ZNF365 (PubMed:23966166).

    Interacts with RRP1B (PubMed:19710015).

    Interacts with TIMELESS; the interaction is direct (PubMed:26344098).

    Interacts with CGAS; leading to impede the formation of the PARP1-TIMELESS complex (PubMed:30356214).

    By similarity19 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    106652, 319 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    P09874

    Database of interacting proteins

    More...
    DIPi
    DIP-38N

    The Eukaryotic Linear Motif resource for Functional Sites in Proteins

    More...
    ELMi
    P09874

    Protein interaction database and analysis system

    More...
    IntActi
    P09874, 145 interactors

    Molecular INTeraction database

    More...
    MINTi
    P09874

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000355759

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P09874

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    11014
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P09874

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P09874

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini385 – 476BRCTPROSITE-ProRule annotationAdd BLAST92
    Domaini662 – 779PARP alpha-helicalPROSITE-ProRule annotationAdd BLAST118
    Domaini788 – 1014PARP catalyticPROSITE-ProRule annotationAdd BLAST227

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni373 – 524Automodification domain1 PublicationAdd BLAST152

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi207 – 209Nuclear localization signal1 Publication3
    Motifi221 – 226Nuclear localization signal1 Publication6

    Zinc finger

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Zinc fingeri9 – 93PARP-type 1PROSITE-ProRule annotationAdd BLAST85
    Zinc fingeri113 – 203PARP-type 2PROSITE-ProRule annotationAdd BLAST91

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1037 Eukaryota
    ENOG410XP18 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000156058

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000030402

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P09874

    KEGG Orthology (KO)

    More...
    KOi
    K10798

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    YLKKFKC

    Database of Orthologous Groups

    More...
    OrthoDBi
    909382at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P09874

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF316616

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.20.142.10, 1 hit
    2.20.140.10, 1 hit
    2.20.25.630, 1 hit
    3.30.1740.10, 2 hits
    3.40.50.10190, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001357 BRCT_dom
    IPR036420 BRCT_dom_sf
    IPR012982 PADR1
    IPR038650 PADR1_dom_sf
    IPR008288 PARP
    IPR012317 Poly(ADP-ribose)pol_cat_dom
    IPR004102 Poly(ADP-ribose)pol_reg_dom
    IPR036616 Poly(ADP-ribose)pol_reg_dom_sf
    IPR036930 WGR_dom_sf
    IPR008893 WGR_domain
    IPR001510 Znf_PARP
    IPR036957 Znf_PARP_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00533 BRCT, 1 hit
    PF08063 PADR1, 1 hit
    PF00644 PARP, 1 hit
    PF02877 PARP_reg, 1 hit
    PF05406 WGR, 1 hit
    PF00645 zf-PARP, 2 hits

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000489 NAD_ADPRT, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00292 BRCT, 1 hit
    SM01335 PADR1, 1 hit
    SM00773 WGR, 1 hit
    SM01336 zf-PARP, 2 hits

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF142921 SSF142921, 1 hit
    SSF47587 SSF47587, 1 hit
    SSF52113 SSF52113, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50172 BRCT, 1 hit
    PS51060 PARP_ALPHA_HD, 1 hit
    PS51059 PARP_CATALYTIC, 1 hit
    PS00347 PARP_ZN_FINGER_1, 2 hits
    PS50064 PARP_ZN_FINGER_2, 2 hits

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

    P09874-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAESSDKLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH
    60 70 80 90 100
    WYHFSCFWKV GHSIRHPDVE VDGFSELRWD DQQKVKKTAE AGGVTGKGQD
    110 120 130 140 150
    GIGSKAEKTL GDFAAEYAKS NRSTCKGCME KIEKGQVRLS KKMVDPEKPQ
    160 170 180 190 200
    LGMIDRWYHP GCFVKNREEL GFRPEYSASQ LKGFSLLATE DKEALKKQLP
    210 220 230 240 250
    GVKSEGKRKG DEVDGVDEVA KKKSKKEKDK DSKLEKALKA QNDLIWNIKD
    260 270 280 290 300
    ELKKVCSTND LKELLIFNKQ QVPSGESAIL DRVADGMVFG ALLPCEECSG
    310 320 330 340 350
    QLVFKSDAYY CTGDVTAWTK CMVKTQTPNR KEWVTPKEFR EISYLKKLKV
    360 370 380 390 400
    KKQDRIFPPE TSASVAATPP PSTASAPAAV NSSASADKPL SNMKILTLGK
    410 420 430 440 450
    LSRNKDEVKA MIEKLGGKLT GTANKASLCI STKKEVEKMN KKMEEVKEAN
    460 470 480 490 500
    IRVVSEDFLQ DVSASTKSLQ ELFLAHILSP WGAEVKAEPV EVVAPRGKSG
    510 520 530 540 550
    AALSKKSKGQ VKEEGINKSE KRMKLTLKGG AAVDPDSGLE HSAHVLEKGG
    560 570 580 590 600
    KVFSATLGLV DIVKGTNSYY KLQLLEDDKE NRYWIFRSWG RVGTVIGSNK
    610 620 630 640 650
    LEQMPSKEDA IEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE
    660 670 680 690 700
    AVKKLTVNPG TKSKLPKPVQ DLIKMIFDVE SMKKAMVEYE IDLQKMPLGK
    710 720 730 740 750
    LSKRQIQAAY SILSEVQQAV SQGSSDSQIL DLSNRFYTLI PHDFGMKKPP
    760 770 780 790 800
    LLNNADSVQA KVEMLDNLLD IEVAYSLLRG GSDDSSKDPI DVNYEKLKTD
    810 820 830 840 850
    IKVVDRDSEE AEIIRKYVKN THATTHNAYD LEVIDIFKIE REGECQRYKP
    860 870 880 890 900
    FKQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM
    910 920 930 940 950
    VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG
    960 970 980 990 1000
    LGKTTPDPSA NISLDGVDVP LGTGISSGVN DTSLLYNEYI VYDIAQVNLK
    1010
    YLLKLKFNFK TSLW
    Length:1,014
    Mass (Da):113,084
    Last modified:January 23, 2007 - v4
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6A5FC01EB91C046B
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    Q5VX84Q5VX84_HUMAN
    Poly [ADP-ribose] polymerase 1
    PARP1
    108Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    Q5VX85Q5VX85_HUMAN
    Poly [ADP-ribose] polymerase 1
    PARP1
    155Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti17G → E in AAB59447 (PubMed:2824474).Curated1
    Sequence conflicti70E → Q in AAA60137 (PubMed:3120710).Curated1
    Sequence conflicti212E → K in AAB59447 (PubMed:2824474).Curated1
    Sequence conflicti613H → Q in AAA60155 (PubMed:2891139).Curated1
    Sequence conflicti827N → S in AAA60155 (PubMed:2891139).Curated1
    Sequence conflicti908C → Y in AAA60155 (PubMed:2891139).Curated1
    Sequence conflicti980N → I in AAA60155 (PubMed:2891139).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_05046054F → L. Corresponds to variant dbSNP:rs3738708Ensembl.1
    Natural variantiVAR_014714188A → T1 PublicationCorresponds to variant dbSNP:rs1805409Ensembl.1
    Natural variantiVAR_019171334V → I1 PublicationCorresponds to variant dbSNP:rs3219057Ensembl.1
    Natural variantiVAR_050461377P → S. Corresponds to variant dbSNP:rs2230484Ensembl.1
    Natural variantiVAR_019172383S → Y1 PublicationCorresponds to variant dbSNP:rs3219062Ensembl.1
    Natural variantiVAR_035852488E → V in a breast cancer sample; somatic mutation. 1 Publication1
    Natural variantiVAR_014715762V → A2 PublicationsCorresponds to variant dbSNP:rs1136410Ensembl.1
    Natural variantiVAR_019173940K → R2 PublicationsCorresponds to variant dbSNP:rs3219145Ensembl.1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    M18112 mRNA Translation: AAA60137.1
    J03473 mRNA Translation: AAB59447.1
    M32721 mRNA Translation: AAA60155.1
    M29786
    , M29545, M29766, M29767, M29768, M29769, M29770, M29771, M29772, M29773, M29774, M29775, M29776, M29777, M29778, M29779, M29780, M29781, M29783, M29784, M29785, M29544, M29782 Genomic DNA Translation: AAA51663.1
    AF524947 Genomic DNA Translation: AAM75364.1
    AL359704 Genomic DNA No translation available.
    AL359742 Genomic DNA No translation available.
    CH471098 Genomic DNA Translation: EAW69783.1
    BC037545 mRNA Translation: AAH37545.1
    X56140, X56141 Genomic DNA Translation: CAA39606.1
    X16674 Genomic DNA Translation: CAA34663.1
    M60436 Genomic DNA Translation: AAA60000.1
    M17081 mRNA Translation: AAA51599.1 Sequence problems.

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS1554.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A29725

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001609.2, NM_001618.3

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000366794; ENSP00000355759; ENSG00000143799

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    142

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:142

    UCSC genome browser

    More...
    UCSCi
    uc001hqd.5 human

    Keywords - Coding sequence diversityi

    Polymorphism

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M18112 mRNA Translation: AAA60137.1
    J03473 mRNA Translation: AAB59447.1
    M32721 mRNA Translation: AAA60155.1
    M29786
    , M29545, M29766, M29767, M29768, M29769, M29770, M29771, M29772, M29773, M29774, M29775, M29776, M29777, M29778, M29779, M29780, M29781, M29783, M29784, M29785, M29544, M29782 Genomic DNA Translation: AAA51663.1
    AF524947 Genomic DNA Translation: AAM75364.1
    AL359704 Genomic DNA No translation available.
    AL359742 Genomic DNA No translation available.
    CH471098 Genomic DNA Translation: EAW69783.1
    BC037545 mRNA Translation: AAH37545.1
    X56140, X56141 Genomic DNA Translation: CAA39606.1
    X16674 Genomic DNA Translation: CAA34663.1
    M60436 Genomic DNA Translation: AAA60000.1
    M17081 mRNA Translation: AAA51599.1 Sequence problems.
    CCDSiCCDS1554.1
    PIRiA29725
    RefSeqiNP_001609.2, NM_001618.3

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1UK0X-ray3.00A/B662-1011[»]
    1UK1X-ray3.00A/B662-1011[»]
    1WOKX-ray3.00A/B/C/D662-1011[»]
    2COKNMR-A387-486[»]
    2CR9NMR-A518-643[»]
    2CS2NMR-A103-223[»]
    2DMJNMR-A1-93[»]
    2JVNNMR-A233-358[»]
    2L30NMR-A1-108[»]
    2L31NMR-A103-214[»]
    2N8ANMR-A1-214[»]
    2RCWX-ray2.80A662-1011[»]
    2RD6X-ray2.30A662-1011[»]
    2RIQX-ray1.70A216-366[»]
    3GJWX-ray2.30A662-1011[»]
    3GN7X-ray2.50A662-1011[»]
    3L3LX-ray2.50A662-1011[»]
    3L3MX-ray2.50A662-1011[»]
    3OD8X-ray2.40A/B/C/D/E/F/G/H2-96[»]
    3ODAX-ray2.64A/B/C/D/E/F/G/H2-96[»]
    3ODCX-ray2.80A/B105-206[»]
    3ODEX-ray2.95A/B105-206[»]
    4AV1X-ray3.10A/B/C/D5-202[»]
    4DQYX-ray3.25A/D1-96[»]
    B/E216-366[»]
    C/F518-1014[»]
    4GV7X-ray2.89A/B/C/D662-1011[»]
    4HHYX-ray2.36A/B/C/D660-1011[»]
    4HHZX-ray2.72A/B/C/D660-1011[»]
    4L6SX-ray2.20A/B662-1011[»]
    4OPXX-ray3.31A/D1-97[»]
    A/D207-366[»]
    C/F518-1014[»]
    4OQAX-ray3.65A/D1-97[»]
    A/D207-366[»]
    C/F518-1014[»]
    4OQBX-ray3.36A/D1-97[»]
    A/D207-366[»]
    C/F518-1014[»]
    4PJTX-ray2.35A/B/C/D662-1011[»]
    4R5WX-ray2.84A/B662-1011[»]
    4R6EX-ray2.20A/B/C/D662-1011[»]
    4RV6X-ray3.19A/B/C/D662-1011[»]
    4UNDX-ray2.20A/B662-1011[»]
    4UXBX-ray3.22A/B662-1011[»]
    4XHUX-ray2.09A/C661-1014[»]
    4ZZZX-ray1.90A/B655-1014[»]
    5A00X-ray2.75A655-1014[»]
    5DS3X-ray2.60A788-1012[»]
    5HA9X-ray4.01A/B662-1011[»]
    5KPNX-ray2.30A/B662-1011[»]
    5KPOX-ray2.65A/B662-1011[»]
    5KPPX-ray2.33A/B662-1011[»]
    5KPQX-ray2.55A/B662-1011[»]
    5WRQX-ray2.65A/B662-1011[»]
    5WRYX-ray2.30A/B662-1011[»]
    5WRZX-ray2.20A/B662-1011[»]
    5WS0X-ray2.60A/B662-1011[»]
    5WS1X-ray1.90A/B662-1011[»]
    5WTCX-ray2.20A/B662-1011[»]
    5XSRX-ray2.30A662-1011[»]
    5XSTX-ray2.30A662-1010[»]
    5XSUX-ray2.40A/B/C/D662-1011[»]
    6BHVX-ray2.30A/B/C/D788-1012[»]
    6GHKX-ray2.28A/B662-1011[»]
    6NRFX-ray2.00A788-1012[»]
    6NRGX-ray1.70A788-1012[»]
    6NRHX-ray1.50A788-1012[»]
    6NRIX-ray2.20A788-1012[»]
    6NRJX-ray1.65A788-1012[»]
    SMRiP09874
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi106652, 319 interactors
    CORUMiP09874
    DIPiDIP-38N
    ELMiP09874
    IntActiP09874, 145 interactors
    MINTiP09874
    STRINGi9606.ENSP00000355759

    Chemistry databases

    BindingDBiP09874
    ChEMBLiCHEMBL3105
    DrugBankiDB04010 2-(3'-Methoxyphenyl) Benzimidazole-4-Carboxamide
    DB03509 2-(4-Chlorophenyl)-5-Quinoxalinecarboxamide
    DB03072 2-{3-[4-(4-Fluorophenyl)-3,6-Dihydro-1(2h)-Pyridinyl]Propyl}-8-Methyl-4(3h)-Quinazolinone
    DB03722 3,4-Dihydro-5-Methyl-Isoquinolinone
    DB03073 3-Methoxybenzamide
    DB07787 5-FLUORO-1-[4-(4-PHENYL-3,6-DIHYDROPYRIDIN-1(2H)-YL)BUTYL]QUINAZOLINE-2,4(1H,3H)-DIONE
    DB07096 6-AMINO-BENZO[DE]ISOQUINOLINE-1,3-DIONE
    DB02498 Carba-Nicotinamide-Adenine-Dinucleotide
    DB13877 Iniparib
    DB02701 Nicotinamide
    DB11793 Niraparib
    DB02690 NU1025
    DB09074 Olaparib
    DB12332 Rucaparib
    DB11760 Talazoparib
    DB00277 Theophylline
    DB07330 trans-4-(7-carbamoyl-1H-benzimidazol-2-yl)-1-propylpiperidinium
    DB07232 Veliparib
    DB01593 Zinc
    DB14487 Zinc acetate
    DB14533 Zinc chloride
    DrugCentraliP09874
    GuidetoPHARMACOLOGYi2771

    PTM databases

    iPTMnetiP09874
    PhosphoSitePlusiP09874
    SwissPalmiP09874

    Polymorphism and mutation databases

    BioMutaiPARP1
    DMDMi130781

    2D gel databases

    SWISS-2DPAGEiP09874

    Proteomic databases

    CPTACiCPTAC-3240
    CPTAC-3241
    CPTAC-556
    CPTAC-557
    EPDiP09874
    jPOSTiP09874
    MassIVEiP09874
    MaxQBiP09874
    PaxDbiP09874
    PeptideAtlasiP09874
    PRIDEiP09874
    ProteomicsDBi52271

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    142

    Genome annotation databases

    EnsembliENST00000366794; ENSP00000355759; ENSG00000143799
    GeneIDi142
    KEGGihsa:142
    UCSCiuc001hqd.5 human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    142
    DisGeNETi142

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    PARP1
    HGNCiHGNC:270 PARP1
    HPAiCAB000147
    CAB003839
    CAB003840
    CAB075726
    CAB075727
    HPA045168
    MIMi173870 gene
    neXtProtiNX_P09874
    OpenTargetsiENSG00000143799
    PharmGKBiPA32

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG1037 Eukaryota
    ENOG410XP18 LUCA
    GeneTreeiENSGT00940000156058
    HOGENOMiHOG000030402
    InParanoidiP09874
    KOiK10798
    OMAiYLKKFKC
    OrthoDBi909382at2759
    PhylomeDBiP09874
    TreeFamiTF316616

    Enzyme and pathway databases

    BRENDAi2.4.2.30 2681
    ReactomeiR-HSA-110362 POLB-Dependent Long Patch Base Excision Repair
    R-HSA-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
    R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
    R-HSA-5685939 HDR through MMEJ (alt-NHEJ)
    R-HSA-5696394 DNA Damage Recognition in GG-NER
    R-HSA-5696395 Formation of Incision Complex in GG-NER
    R-HSA-5696400 Dual Incision in GG-NER
    SignaLinkiP09874
    SIGNORiP09874

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    PARP1 human
    EvolutionaryTraceiP09874

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    PARP1

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    142
    PharosiP09874
    PMAP-CutDBiP09874

    Protein Ontology

    More...
    PROi
    PR:P09874

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000143799 Expressed in 233 organ(s), highest expression level in heart left ventricle
    ExpressionAtlasiP09874 baseline and differential
    GenevisibleiP09874 HS

    Family and domain databases

    Gene3Di1.20.142.10, 1 hit
    2.20.140.10, 1 hit
    2.20.25.630, 1 hit
    3.30.1740.10, 2 hits
    3.40.50.10190, 1 hit
    InterProiView protein in InterPro
    IPR001357 BRCT_dom
    IPR036420 BRCT_dom_sf
    IPR012982 PADR1
    IPR038650 PADR1_dom_sf
    IPR008288 PARP
    IPR012317 Poly(ADP-ribose)pol_cat_dom
    IPR004102 Poly(ADP-ribose)pol_reg_dom
    IPR036616 Poly(ADP-ribose)pol_reg_dom_sf
    IPR036930 WGR_dom_sf
    IPR008893 WGR_domain
    IPR001510 Znf_PARP
    IPR036957 Znf_PARP_sf
    PfamiView protein in Pfam
    PF00533 BRCT, 1 hit
    PF08063 PADR1, 1 hit
    PF00644 PARP, 1 hit
    PF02877 PARP_reg, 1 hit
    PF05406 WGR, 1 hit
    PF00645 zf-PARP, 2 hits
    PIRSFiPIRSF000489 NAD_ADPRT, 1 hit
    SMARTiView protein in SMART
    SM00292 BRCT, 1 hit
    SM01335 PADR1, 1 hit
    SM00773 WGR, 1 hit
    SM01336 zf-PARP, 2 hits
    SUPFAMiSSF142921 SSF142921, 1 hit
    SSF47587 SSF47587, 1 hit
    SSF52113 SSF52113, 1 hit
    PROSITEiView protein in PROSITE
    PS50172 BRCT, 1 hit
    PS51060 PARP_ALPHA_HD, 1 hit
    PS51059 PARP_CATALYTIC, 1 hit
    PS00347 PARP_ZN_FINGER_1, 2 hits
    PS50064 PARP_ZN_FINGER_2, 2 hits

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPARP1_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P09874
    Secondary accession number(s): B1ANJ4, Q8IUZ9
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 16, 2019
    This is version 243 of the entry and version 4 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    5. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
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