Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 191 (17 Jun 2020)
Sequence version 4 (27 Sep 2017)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Protein mono-ADP-ribosyltransferase PARP3

Gene

PARP3

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

Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins and plays a key role in the response to DNA damage (PubMed:16924674, PubMed:20064938, PubMed:21211721, PubMed:21270334, PubMed:25043379, PubMed:24598253). Mediates mono-ADP-ribosylation of glutamate, aspartate or lysine residues on target proteins (PubMed:20064938, PubMed:25043379). In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (PubMed:25043379). Associates with a number of DNA repair factors and is involved in the response to exogenous and endogenous DNA strand breaks (PubMed:16924674, PubMed:21211721, PubMed:21270334). Together with APLF, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ) (PubMed:21211721). Cooperates with the XRRC6-XRCC5 (Ku70-Ku80) heterodimer to limit end-resection thereby promoting accurate NHEJ (PubMed:24598253). Involved in DNA repair by mediating mono-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism, such as XRRC5 and XRCC6 (PubMed:16924674, PubMed:24598253). 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:16924674, PubMed:21211721, PubMed:21270334). May link the DNA damage surveillance network to the mitotic fidelity checkpoint (PubMed:16924674). In addition to proteins, also able to ADP-ribosylate DNA: mediates DNA mono-ADP-ribosylation of DNA strand break termini via covalent addition of a single ADP-ribose moiety to a 5'- or 3'-terminal phosphate residues in DNA containing multiple strand breaks (PubMed:29361132, PubMed:29520010). Acts as a negative regulator of immunoglobulin class switch recombination, probably by controlling the level of AICDA /AID on the chromatin (By similarity).By similarity8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  1. KM=130 µM for NAD+1 Publication

    <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 functionGlycosyltransferase, Transferase
    Biological processDNA damage, DNA repair
    LigandNAD

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.4.2.30 2681

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

    More...
    SignaLinki
    Q9Y6F1

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    Q9Y6F1

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    Protein mono-ADP-ribosyltransferase PARP3Curated (EC:2.4.2.-2 Publications)
    Alternative name(s):
    ADP-ribosyltransferase diphtheria toxin-like 31 Publication
    Short name:
    ARTD31 Publication
    DNA ADP-ribosyltransferase PARP3Curated (EC:2.4.2.-1 Publication)
    IRT1
    NAD(+) ADP-ribosyltransferase 31 Publication
    Short name:
    ADPRT-31 Publication
    Poly [ADP-ribose] polymerase 32 Publications
    Short name:
    PARP-31 Publication
    Short name:
    hPARP-31 Publication
    Poly[ADP-ribose] synthase 31 Publication
    Short name:
    pADPRT-31 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:PARP31 PublicationImported
    Synonyms:ADPRT31 Publication, ADPRTL3
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 3

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000041880.14

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:273 PARP3

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    607726 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q9Y6F1

    <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, Cytoplasm, Cytoskeleton, 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

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    10039

    Open Targets

    More...
    OpenTargetsi
    ENSG00000041880

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA24593

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    Q9Y6F1 Tclin

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL5083

    Drug and drug target database

    More...
    DrugBanki
    DB07677 2-methyl-3,5,7,8-tetrahydro-4H-thiopyrano[4,3-d]pyrimidin-4-one
    DB08058 4-[3-(1,4-diazepan-1-ylcarbonyl)-4-fluorobenzyl]phthalazin-1(2H)-one
    DB08348 N~2~,N~2~-DIMETHYL-N~1~-(6-OXO-5,6-DIHYDROPHENANTHRIDIN-2-YL)GLYCINAMIDE
    DB09074 Olaparib
    DB12332 Rucaparib

    DrugCentral

    More...
    DrugCentrali
    Q9Y6F1

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    2864

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    PARP3

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    224471880

    <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 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002113291 – 533Protein mono-ADP-ribosyltransferase PARP3Add BLAST533

    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 residuei6N6-(ADP-ribosyl)lysine1 Publication1
    Modified residuei12ADP-ribosyl glutamic acid1 Publication1
    Modified residuei15ADP-ribosyl glutamic acid1 Publication1
    Modified residuei26ADP-ribosyl glutamic acid1 Publication1
    Modified residuei34ADP-ribosyl glutamic acid1 Publication1
    Modified residuei37N6-(ADP-ribosyl)lysine1 Publication1
    Modified residuei141ADP-ribosyl aspartic acid1 Publication1
    Modified residuei163ADP-ribosyl glutamic acid1 Publication1
    Modified residuei210ADP-ribosyl aspartic acid1 Publication1
    Modified residuei231ADP-ribosyl glutamic acid1 Publication1
    Modified residuei309ADP-ribosyl glutamic acid1 Publication1
    Modified residuei310ADP-ribosyl glutamic acid1 Publication1
    Modified residuei344ADP-ribosyl glutamic acid1 Publication1
    Modified residuei449ADP-ribosyl glutamic acid1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

    Auto-mono-ADP-ribosylated.2 Publications

    Keywords - PTMi

    ADP-ribosylation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q9Y6F1

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    Q9Y6F1

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

    More...
    PaxDbi
    Q9Y6F1

    PeptideAtlas

    More...
    PeptideAtlasi
    Q9Y6F1

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9Y6F1

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    86661 [Q9Y6F1-1]
    86662 [Q9Y6F1-2]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q9Y6F1

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

    More...
    PhosphoSitePlusi
    Q9Y6F1

    <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

    <p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Widely expressed; the highest levels are in the kidney, skeletal muscle, liver, heart and spleen; also detected in pancreas, lung, placenta, brain, leukocytes, colon, small intestine, ovary, testis, prostate and thymus.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000041880 Expressed in left adrenal gland and 168 other tissues

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q9Y6F1 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q9Y6F1 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    ENSG00000041880 Low tissue specificity

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Interacts with PARP1; leading to activate PARP1 in absence of DNA (PubMed:16924674, PubMed:20064938).

    Interacts with PRKDC (PubMed:16924674).

    Interacts with XRCC5/Ku80; the interaction is dependent on nucleic acids (PubMed:16924674, PubMed:24598253).

    Interacts with XRCC6/Ku70; the interaction is dependent on nucleic acids (PubMed:16924674, PubMed:24598253).

    Interacts with EZH2, HDAC1, HDAC2, SUZ12, YY1, LRIG3 and LIG4 (PubMed:16924674).

    3 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    115351, 14 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    Q9Y6F1, 2 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000381740

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    Q9Y6F1

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    Q9Y6F1 protein

    <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

    1533
    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
    Q9Y6F1

    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
    Q9Y6F1

    <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%5Fand%5Fdomains%5Fsection">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>Domaini182 – 300PARP alpha-helicalPROSITE-ProRule annotationAdd BLAST119
    Domaini313 – 533PARP catalyticPROSITE-ProRule annotationAdd BLAST221

    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>Motifi14 – 20Nuclear localization signalSequence analysis7

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1037 Eukaryota
    ENOG410XP18 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000158855

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9Y6F1

    KEGG Orthology (KO)

    More...
    KOi
    K10798

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    AKRVQPC

    Database of Orthologous Groups

    More...
    OrthoDBi
    909382at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q9Y6F1

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF315407

    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

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR031275 PARP3
    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

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR10459:SF66 PTHR10459:SF66, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00644 PARP, 1 hit
    PF02877 PARP_reg, 1 hit
    PF05406 WGR, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00773 WGR, 1 hit

    Superfamily database of structural and functional annotation

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

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51060 PARP_ALPHA_HD, 1 hit
    PS51059 PARP_CATALYTIC, 1 hit

    <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%5Flength">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>Sequences (2+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

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

    Isoform 1 (identifier: Q9Y6F1-1) [UniParc]FASTAAdd to basket
    Also known as: Short

    This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide
            10         20         30         40         50
    MAPKPKPWVQ TEGPEKKKGR QAGREEDPFR STAEALKAIP AEKRIIRVDP
    60 70 80 90 100
    TCPLSSNPGT QVYEDYNCTL NQTNIENNNN KFYIIQLLQD SNRFFTCWNR
    110 120 130 140 150
    WGRVGEVGQS KINHFTRLED AKKDFEKKFR EKTKNNWAER DHFVSHPGKY
    160 170 180 190 200
    TLIEVQAEDE AQEAVVKVDR GPVRTVTKRV QPCSLDPATQ KLITNIFSKE
    210 220 230 240 250
    MFKNTMALMD LDVKKMPLGK LSKQQIARGF EALEALEEAL KGPTDGGQSL
    260 270 280 290 300
    EELSSHFYTV IPHNFGHSQP PPINSPELLQ AKKDMLLVLA DIELAQALQA
    310 320 330 340 350
    VSEQEKTVEE VPHPLDRDYQ LLKCQLQLLD SGAPEYKVIQ TYLEQTGSNH
    360 370 380 390 400
    RCPTLQHIWK VNQEGEEDRF QAHSKLGNRK LLWHGTNMAV VAAILTSGLR
    410 420 430 440 450
    IMPHSGGRVG KGIYFASENS KSAGYVIGMK CGAHHVGYMF LGEVALGREH
    460 470 480 490 500
    HINTDNPSLK SPPPGFDSVI ARGHTEPDPT QDTELELDGQ QVVVPQGQPV
    510 520 530
    PCPEFSSSTF SQSEYLIYQE SQCRLRYLLE VHL
    Note: More abundant isoform.1 Publication
    Length:533
    Mass (Da):60,089
    Last modified:September 27, 2017 - 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:i6296A0E439CC7767
    GO
    Isoform 2 (identifier: Q9Y6F1-2) [UniParc]FASTAAdd to basket
    Also known as: Long

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MSLLFLAM

    Show »
    Length:540
    Mass (Da):60,865
    Checksum:i728CF4D3E119DC86
    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
    C9J9C7C9J9C7_HUMAN
    Protein mono-ADP-ribosyltransferase...
    PARP3
    331Annotation score:

    Annotation score:2 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>
    F8WAY7F8WAY7_HUMAN
    Protein mono-ADP-ribosyltransferase...
    PARP3
    53Annotation 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 conflicti80N → K in AAD29855 (PubMed:10329013).Curated1
    Sequence conflicti171G → A in AAD29855 (PubMed:10329013).Curated1
    Sequence conflicti411K → E in CAB43246 (PubMed:17974005).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_05664391S → N. Corresponds to variant dbSNP:rs34224216Ensembl.1
    Natural variantiVAR_054622100R → H. Corresponds to variant dbSNP:rs28547534Ensembl.1
    Natural variantiVAR_056644269Q → R. Corresponds to variant dbSNP:rs323870Ensembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0078631M → MSLLFLAM in isoform 2. 2 Publications1

    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
    AF083068 mRNA Translation: AAD29855.1
    AY126341 mRNA Translation: AAM95460.1
    Y16836 mRNA Translation: CAC79988.1
    AC115284 Genomic DNA No translation available.
    BC014260 mRNA Translation: AAH14260.1
    AL050034 mRNA Translation: CAB43246.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS43097.1 [Q9Y6F1-1]
    CCDS46839.1 [Q9Y6F1-2]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    T08713

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001003931.3, NM_001003931.3 [Q9Y6F1-2]
    NP_005476.4, NM_005485.5 [Q9Y6F1-1]
    XP_005264836.2, XM_005264779.4
    XP_016860979.1, XM_017005490.1 [Q9Y6F1-1]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000398755; ENSP00000381740; ENSG00000041880 [Q9Y6F1-2]
    ENST00000417220; ENSP00000395951; ENSG00000041880 [Q9Y6F1-1]
    ENST00000431474; ENSP00000401511; ENSG00000041880 [Q9Y6F1-1]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    10039

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:10039

    UCSC genome browser

    More...
    UCSCi
    uc003dbz.4 human [Q9Y6F1-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, 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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF083068 mRNA Translation: AAD29855.1
    AY126341 mRNA Translation: AAM95460.1
    Y16836 mRNA Translation: CAC79988.1
    AC115284 Genomic DNA No translation available.
    BC014260 mRNA Translation: AAH14260.1
    AL050034 mRNA Translation: CAB43246.1
    CCDSiCCDS43097.1 [Q9Y6F1-1]
    CCDS46839.1 [Q9Y6F1-2]
    PIRiT08713
    RefSeqiNP_001003931.3, NM_001003931.3 [Q9Y6F1-2]
    NP_005476.4, NM_005485.5 [Q9Y6F1-1]
    XP_005264836.2, XM_005264779.4
    XP_016860979.1, XM_017005490.1 [Q9Y6F1-1]

    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
    2EOCNMR-A41-157[»]
    3C49X-ray2.80A178-532[»]
    3C4HX-ray2.10A178-532[»]
    3CE0X-ray2.80A178-532[»]
    3FHBX-ray2.30A178-532[»]
    4GV0X-ray1.90A178-532[»]
    4GV2X-ray1.80A178-532[»]
    4GV4X-ray1.80A178-532[»]
    4L6ZX-ray2.00A178-532[»]
    4L70X-ray2.00A178-532[»]
    4L7LX-ray2.10A178-532[»]
    4L7NX-ray1.80A178-532[»]
    4L7OX-ray2.00A178-532[»]
    4L7PX-ray2.30A178-532[»]
    4L7RX-ray2.20A178-532[»]
    4L7UX-ray2.80A178-532[»]
    SMRiQ9Y6F1
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi115351, 14 interactors
    IntActiQ9Y6F1, 2 interactors
    STRINGi9606.ENSP00000381740

    Chemistry databases

    BindingDBiQ9Y6F1
    ChEMBLiCHEMBL5083
    DrugBankiDB07677 2-methyl-3,5,7,8-tetrahydro-4H-thiopyrano[4,3-d]pyrimidin-4-one
    DB08058 4-[3-(1,4-diazepan-1-ylcarbonyl)-4-fluorobenzyl]phthalazin-1(2H)-one
    DB08348 N~2~,N~2~-DIMETHYL-N~1~-(6-OXO-5,6-DIHYDROPHENANTHRIDIN-2-YL)GLYCINAMIDE
    DB09074 Olaparib
    DB12332 Rucaparib
    DrugCentraliQ9Y6F1
    GuidetoPHARMACOLOGYi2864

    PTM databases

    iPTMnetiQ9Y6F1
    PhosphoSitePlusiQ9Y6F1

    Polymorphism and mutation databases

    BioMutaiPARP3
    DMDMi224471880

    Proteomic databases

    EPDiQ9Y6F1
    MassIVEiQ9Y6F1
    PaxDbiQ9Y6F1
    PeptideAtlasiQ9Y6F1
    PRIDEiQ9Y6F1
    ProteomicsDBi86661 [Q9Y6F1-1]
    86662 [Q9Y6F1-2]

    Protocols and materials databases

    Antibodypedia a portal for validated antibodies

    More...
    Antibodypediai
    7395 282 antibodies

    The DNASU plasmid repository

    More...
    DNASUi
    10039

    Genome annotation databases

    EnsembliENST00000398755; ENSP00000381740; ENSG00000041880 [Q9Y6F1-2]
    ENST00000417220; ENSP00000395951; ENSG00000041880 [Q9Y6F1-1]
    ENST00000431474; ENSP00000401511; ENSG00000041880 [Q9Y6F1-1]
    GeneIDi10039
    KEGGihsa:10039
    UCSCiuc003dbz.4 human [Q9Y6F1-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    10039
    DisGeNETi10039
    EuPathDBiHostDB:ENSG00000041880.14

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    PARP3
    HGNCiHGNC:273 PARP3
    HPAiENSG00000041880 Low tissue specificity
    MIMi607726 gene
    neXtProtiNX_Q9Y6F1
    OpenTargetsiENSG00000041880
    PharmGKBiPA24593

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG1037 Eukaryota
    ENOG410XP18 LUCA
    GeneTreeiENSGT00940000158855
    InParanoidiQ9Y6F1
    KOiK10798
    OMAiAKRVQPC
    OrthoDBi909382at2759
    PhylomeDBiQ9Y6F1
    TreeFamiTF315407

    Enzyme and pathway databases

    BRENDAi2.4.2.30 2681
    SignaLinkiQ9Y6F1
    SIGNORiQ9Y6F1

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

    More...
    BioGRID-ORCSi
    10039 6 hits in 791 CRISPR screens

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

    More...
    ChiTaRSi
    PARP3 human
    EvolutionaryTraceiQ9Y6F1

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    PARP3

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

    More...
    GenomeRNAii
    10039
    PharosiQ9Y6F1 Tclin

    Protein Ontology

    More...
    PROi
    PR:Q9Y6F1
    RNActiQ9Y6F1 protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000041880 Expressed in left adrenal gland and 168 other tissues
    ExpressionAtlasiQ9Y6F1 baseline and differential
    GenevisibleiQ9Y6F1 HS

    Family and domain databases

    Gene3Di1.20.142.10, 1 hit
    2.20.140.10, 1 hit
    InterProiView protein in InterPro
    IPR031275 PARP3
    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
    PANTHERiPTHR10459:SF66 PTHR10459:SF66, 1 hit
    PfamiView protein in Pfam
    PF00644 PARP, 1 hit
    PF02877 PARP_reg, 1 hit
    PF05406 WGR, 1 hit
    SMARTiView protein in SMART
    SM00773 WGR, 1 hit
    SUPFAMiSSF142921 SSF142921, 1 hit
    SSF47587 SSF47587, 1 hit
    PROSITEiView protein in PROSITE
    PS51060 PARP_ALPHA_HD, 1 hit
    PS51059 PARP_CATALYTIC, 1 hit

    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 nameiPARP3_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: Q9Y6F1
    Secondary accession number(s): Q8NER9, Q96CG2, Q9UG81
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: September 27, 2017
    Last modified: June 17, 2020
    This is version 191 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, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again