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Entry version 143 (16 Oct 2019)
Sequence version 2 (10 Oct 2003)
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Protein

Protein mono-ADP-ribosyltransferase PARP9

Gene

PARP9

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

ADP-ribosyltransferase which, in association with E3 ligase DTX3L, plays a role in DNA damage repair and in immune responses including interferon-mediated antiviral defenses (PubMed:16809771, PubMed:23230272, PubMed:26479788, PubMed:27796300). Within the complex, enhances DTX3L E3 ligase activity which is further enhanced by PARP9 binding to poly(ADP-ribose) (PubMed:28525742). In association with DTX3L and in presence of E1 and E2 enzymes, mediates NAD+-dependent mono-ADP-ribosylation of ubiquitin which prevents ubiquitin conjugation to substrates such as histones (PubMed:28525742). During DNA repair, PARP1 recruits PARP9/BAL1-DTX3L complex to DNA damage sites via PARP9 binding to ribosylated PARP1 (PubMed:23230272). Subsequent PARP1-dependent PARP9/BAL1-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (PubMed:23230272, PubMed:28525742). In response to DNA damage, PARP9-DTX3L complex is required for efficient non-homologous end joining (NHEJ); the complex function is negatively modulated by PARP9 activity (PubMed:28525742). Dispensable for B-cell receptor (BCR) assembly through V(D)J recombination and class switch recombination (CSR) (By similarity). In macrophages, positively regulates pro-inflammatory cytokines production in response to IFNG stimulation by suppressing PARP14-mediated STAT1 ADP-ribosylation and thus promoting STAT1 phosphorylation (PubMed:27796300). Also suppresses PARP14-mediated STAT6 ADP-ribosylation (PubMed:27796300).By similarity5 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 <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Binding to poly(ADP-ribose) does not affect its activity.1 Publication

<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=196 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 functionTransferase
    Biological processAntiviral defense, DNA damage, DNA repair, Immunity, Innate immunity
    LigandNAD

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-197264 Nicotinamide salvaging

    <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:
    Protein mono-ADP-ribosyltransferase PARP9Curated (EC:2.4.2.-1 Publication)
    Alternative name(s):
    ADP-ribosyltransferase diphtheria toxin-like 9
    Short name:
    ARTD9
    B aggressive lymphoma protein1 Publication
    Poly [ADP-ribose] polymerase 9
    Short name:
    PARP-9
    <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:PARP9
    Synonyms:BAL1 Publication, BAL11 Publication
    <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 3

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:24118 PARP9

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    612065 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q8IXQ6

    <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

    Cytoplasm, 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

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Overexpressed at significantly higher levels in fatal high-risk diffuse large B-cell lymphomas (DLB-CL) compared to cured low-risk tumors. Overexpression in B-cell lymphoma transfectants may promote malignant B-cell migration. May therefore be involved in promoting B-cell migration and dissemination of high-risk DLB-CL tumors (PubMed:11110709).1 Publication

    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>Mutagenesisi147G → E: Reduces the binding to poly(ADP-ribose) by 50 percent and prevents increase in DTX3L-mediated histone ubiquitination without affecting ubiquitin ADP ribosylation, interaction with DTX3L and STAT1 and DTX3L catalytic activity; when associated with E-346. 2 Publications1
    Mutagenesisi346G → E: Reduces the binding to poly(ADP-ribose) by 50 percent and prevents increase in DTX3L-mediated histone ubiquitination without affecting ubiquitin ADP ribosylation, interaction with DTX3L and STAT1 and DTX3L catalytic activity; when associated with E-147. 2 Publications1
    Mutagenesisi719 – 722Missing : Loss of ADP ribosylation activity and interaction with DTX3L. 1 Publication4
    Mutagenesisi737Y → A: No defect in ubiquitin ADP ribosylation and the interaction with DTX3L. 1 Publication1
    Mutagenesisi738F → K: Severe reduction in ubiquitin ADP ribosylation. No effect on the interaction with DTX3L and on DTX3L E3 ligase activity. Increases DNA repair. 1 Publication1
    Mutagenesisi766 – 769Missing : Loss of ADP ribosylation activity and interaction with DTX3L. 1 Publication4
    Mutagenesisi780 – 784Missing : Reduces ADP ribosylation activity and interaction with DTX3L. 1 Publication5
    Mutagenesisi802 – 803PE → AA: No defect in ADP ribosylation and interaction with DTX3L. 1 Publication2
    Mutagenesisi831 – 854Missing : No defect in ADP ribosylation and interaction with DTX3L. 1 PublicationAdd BLAST24

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    83666

    Open Targets

    More...
    OpenTargetsi
    ENSG00000138496

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA134870403

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    Q8IXQ6

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    PARP9

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    48474734

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002113391 – 854Protein mono-ADP-ribosyltransferase PARP9Add BLAST854

    <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

    ADP-ribosylated by PARP14.1 Publication

    Keywords - PTMi

    ADP-ribosylation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q8IXQ6

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q8IXQ6

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    Q8IXQ6

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    Q8IXQ6

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

    More...
    PaxDbi
    Q8IXQ6

    PeptideAtlas

    More...
    PeptideAtlasi
    Q8IXQ6

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q8IXQ6

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    20136
    71045 [Q8IXQ6-1]
    71046 [Q8IXQ6-2]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q8IXQ6

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

    More...
    PhosphoSitePlusi
    Q8IXQ6

    <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

    Expressed in lymphocyte-rich tissues, spleen, lymph nodes, peripheral blood lymphocytes and colonic mucosa (PubMed:11110709, PubMed:16809771). Expressed in macrophages (PubMed:27796300). Also expressed in nonhematopoietic tissues such as heart and skeletal muscle (PubMed:11110709, PubMed:16809771). Isoform 2 is the predominant form (PubMed:11110709). Most abundantly expressed in lymphomas with a brisk host inflammatory response (PubMed:11110709, PubMed:16809771). In diffuse large B-cell lymphomas tumors, expressed specifically by malignant B-cells (PubMed:11110709, PubMed:16809771).3 Publications

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Up-regulated by IFNG in macrophages and in B-cell lymphoma cell lines (PubMed:16809771, PubMed:27796300, PubMed:26479788). Up-regulated by IFNB1 or viral infection (PubMed:26479788). Down-regulated by IL4 in macrophages (PubMed:27796300).3 Publications

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000138496 Expressed in 184 organ(s), highest expression level in ectocervix

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q8IXQ6 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q8IXQ6 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA066708

    <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

    Forms a stable complex with E3 ligase DTX3L; the interaction is required for PARP9 mediated ADP-ribosylation of ubiquitin (PubMed:12670957, PubMed:28525742).

    Interacts (via PARP catalytic domain) with DTX3L (via N-terminus) (PubMed:26479788).

    Forms a complex with STAT1 and DTX3L independently of IFNB1 or IFNG-mediated STAT1 'Tyr-701' phosphorylation (PubMed:26479788).

    Forms a complex with STAT1, DTX3L and histone H2B HIST1H2BH/H2BJ; the interaction is likely to induce HIST1H2BH/H2BJ ubiquitination (PubMed:26479788).

    Interacts (via N-terminus) with STAT1 (PubMed:26479788).

    Interacts with PARP14 in IFNG-stimulated macrophages; the interaction prevents PARP14-mediated STAT1 and STAT6 ADP-riboslylation (PubMed:27796300).

    Interacts with PARP1 (when poly-ADP-ribosylated) (PubMed:23230272).

    5 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    123723, 17 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    Q8IXQ6

    Protein interaction database and analysis system

    More...
    IntActi
    Q8IXQ6, 2 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000353512

    <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

    1854
    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
    Q8IXQ6

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <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>Domaini107 – 296Macro 1PROSITE-ProRule annotationAdd BLAST190
    Domaini306 – 487Macro 2PROSITE-ProRule annotationAdd BLAST182
    Domaini628 – 850PARP catalyticPROSITE-ProRule annotationAdd BLAST223

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    Macro domains 1 and 2 may be involved in the binding to poly(ADP-ribose) (PubMed:28525742, PubMed:26479788). Macro domain 2 is required for recruitment to DNA damage sites (PubMed:23230272). Macro domains 1 and 2 are probably dispensable for the interaction with STAT1 and DTX3L and for STAT1 phosphorylation (PubMed:26479788).3 Publications

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG2633 Eukaryota
    COG2110 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000158837

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000115452

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q8IXQ6

    KEGG Orthology (KO)

    More...
    KOi
    K15260

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    YNEKSGR

    Database of Orthologous Groups

    More...
    OrthoDBi
    681829at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q8IXQ6

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF328965

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002589 Macro_dom
    IPR012317 Poly(ADP-ribose)pol_cat_dom

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01661 Macro, 2 hits

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00506 A1pp, 2 hits

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51154 MACRO, 2 hits
    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_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>Sequences (3+)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.

    This entry describes 3 <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.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: Q8IXQ6-1) [UniParc]FASTAAdd to basket
    Also known as: Long, L

    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
    MDFSMVAGAA AYNEKSGRIT SLSLLFQKVF AQIFPQWRKG NTEECLPYKC
    60 70 80 90 100
    SETGALGENY SWQIPINHND FKILKNNERQ LCEVLQNKFG CISTLVSPVQ
    110 120 130 140 150
    EGNSKSLQVF RKMLTPRIEL SVWKDDLTTH AVDAVVNAAN EDLLHGGGLA
    160 170 180 190 200
    LALVKAGGFE IQEESKQFVA RYGKVSAGEI AVTGAGRLPC KQIIHAVGPR
    210 220 230 240 250
    WMEWDKQGCT GKLQRAIVSI LNYVIYKNTH IKTVAIPALS SGIFQFPLNL
    260 270 280 290 300
    CTKTIVETIR VSLQGKPMMS NLKEIHLVSN EDPTVAAFKA ASEFILGKSE
    310 320 330 340 350
    LGQETTPSFN AMVVNNLTLQ IVQGHIEWQT ADVIVNSVNP HDITVGPVAK
    360 370 380 390 400
    SILQQAGVEM KSEFLATKAK QFQRSQLVLV TKGFNLFCKY IYHVLWHSEF
    410 420 430 440 450
    PKPQILKHAM KECLEKCIEQ NITSISFPAL GTGNMEIKKE TAAEILFDEV
    460 470 480 490 500
    LTFAKDHVKH QLTVKFVIFP TDLEIYKAFS SEMAKRSKML SLNNYSVPQS
    510 520 530 540 550
    TREEKRENGL EARSPAINLM GFNVEEMYEA HAWIQRILSL QNHHIIENNH
    560 570 580 590 600
    ILYLGRKEHD ILSQLQKTSS VSITEIISPG RTELEIEGAR ADLIEVVMNI
    610 620 630 640 650
    EDMLCKVQEE MARKKERGLW RSLGQWTIQQ QKTQDEMKEN IIFLKCPVPP
    660 670 680 690 700
    TQELLDQKKQ FEKCGLQVLK VEKIDNEVLM AAFQRKKKMM EEKLHRQPVS
    710 720 730 740 750
    HRLFQQVPYQ FCNVVCRVGF QRMYSTPCDP KYGAGIYFTK NLKNLAEKAK
    760 770 780 790 800
    KISAADKLIY VFEAEVLTGF FCQGHPLNIV PPPLSPGAID GHDSVVDNVS
    810 820 830 840 850
    SPETFVIFSG MQAIPQYLWT CTQEYVQSQD YSSGPMRPFA QHPWRGFASG

    SPVD
    Length:854
    Mass (Da):96,343
    Last modified:October 10, 2003 - v2
    <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:iCBBB3B4B7CA1CDA4
    GO
    Isoform 2 (identifier: Q8IXQ6-2) [UniParc]FASTAAdd to basket
    Also known as: Short, S

    The sequence of this isoform differs from the canonical sequence as follows:
         17-51: Missing.

    Show »
    Length:819
    Mass (Da):92,271
    Checksum:i110B81666B857940
    GO
    Isoform 3 (identifier: Q8IXQ6-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         17-51: Missing.
         729-745: DPKYGAGIYFTKNLKNL → GRCQCLIIGATLWNLVS
         746-854: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:710
    Mass (Da):80,291
    Checksum:iE443D3E78BDF0E53
    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
    G5E9U8G5E9U8_HUMAN
    Poly (ADP-ribose) polymerase family...
    PARP9 hCG_17211
    399Annotation 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>
    C9K0E5C9K0E5_HUMAN
    Protein mono-ADP-ribosyltransferase...
    PARP9
    115Annotation 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 conflicti487S → P in BAF85648 (PubMed:14702039).Curated1
    Sequence conflicti839F → S in BAG36276 (PubMed:14702039).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_05665421S → L. Corresponds to variant dbSNP:rs34006803Ensembl.1
    Natural variantiVAR_056655517I → V1 PublicationCorresponds to variant dbSNP:rs28365795Ensembl.1
    Natural variantiVAR_056656528Y → C3 PublicationsCorresponds to variant dbSNP:rs9851180Ensembl.1
    Natural variantiVAR_056657651T → A. Corresponds to variant dbSNP:rs6780543Ensembl.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_00850517 – 51Missing in isoform 2 and isoform 3. 3 PublicationsAdd BLAST35
    Alternative sequenceiVSP_046086729 – 745DPKYG…NLKNL → GRCQCLIIGATLWNLVS in isoform 3. 1 PublicationAdd BLAST17
    Alternative sequenceiVSP_046087746 – 854Missing in isoform 3. 1 PublicationAdd BLAST109

    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
    AF307338 mRNA Translation: AAK07558.1
    AF307339 mRNA Translation: AAK07559.1
    AK292959 mRNA Translation: BAF85648.1
    AK313494 mRNA Translation: BAG36276.1
    AC092908 Genomic DNA No translation available.
    AC096861 Genomic DNA No translation available.
    BC017463 mRNA No translation available.
    BC039580 mRNA Translation: AAH39580.1
    AL713679 mRNA Translation: CAD28483.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS3014.1 [Q8IXQ6-1]
    CCDS54633.1 [Q8IXQ6-3]
    CCDS54634.1 [Q8IXQ6-2]

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001139574.1, NM_001146102.1 [Q8IXQ6-1]
    NP_001139575.1, NM_001146103.1 [Q8IXQ6-2]
    NP_001139576.1, NM_001146104.1 [Q8IXQ6-2]
    NP_001139577.1, NM_001146105.1 [Q8IXQ6-2]
    NP_113646.2, NM_031458.2 [Q8IXQ6-1]
    XP_005247877.1, XM_005247820.2 [Q8IXQ6-1]
    XP_016862793.1, XM_017007304.1 [Q8IXQ6-1]
    XP_016862794.1, XM_017007305.1 [Q8IXQ6-2]
    XP_016862795.1, XM_017007306.1 [Q8IXQ6-2]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000360356; ENSP00000353512; ENSG00000138496 [Q8IXQ6-1]
    ENST00000462315; ENSP00000418894; ENSG00000138496 [Q8IXQ6-3]
    ENST00000471785; ENSP00000419001; ENSG00000138496 [Q8IXQ6-2]
    ENST00000477522; ENSP00000419506; ENSG00000138496 [Q8IXQ6-2]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    83666

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:83666

    UCSC genome browser

    More...
    UCSCi
    uc003efh.5 human [Q8IXQ6-1]

    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
    AF307338 mRNA Translation: AAK07558.1
    AF307339 mRNA Translation: AAK07559.1
    AK292959 mRNA Translation: BAF85648.1
    AK313494 mRNA Translation: BAG36276.1
    AC092908 Genomic DNA No translation available.
    AC096861 Genomic DNA No translation available.
    BC017463 mRNA No translation available.
    BC039580 mRNA Translation: AAH39580.1
    AL713679 mRNA Translation: CAD28483.1
    CCDSiCCDS3014.1 [Q8IXQ6-1]
    CCDS54633.1 [Q8IXQ6-3]
    CCDS54634.1 [Q8IXQ6-2]
    RefSeqiNP_001139574.1, NM_001146102.1 [Q8IXQ6-1]
    NP_001139575.1, NM_001146103.1 [Q8IXQ6-2]
    NP_001139576.1, NM_001146104.1 [Q8IXQ6-2]
    NP_001139577.1, NM_001146105.1 [Q8IXQ6-2]
    NP_113646.2, NM_031458.2 [Q8IXQ6-1]
    XP_005247877.1, XM_005247820.2 [Q8IXQ6-1]
    XP_016862793.1, XM_017007304.1 [Q8IXQ6-1]
    XP_016862794.1, XM_017007305.1 [Q8IXQ6-2]
    XP_016862795.1, XM_017007306.1 [Q8IXQ6-2]

    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
    5AILX-ray1.55A/B310-493[»]
    SMRiQ8IXQ6
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi123723, 17 interactors
    CORUMiQ8IXQ6
    IntActiQ8IXQ6, 2 interactors
    STRINGi9606.ENSP00000353512

    PTM databases

    iPTMnetiQ8IXQ6
    PhosphoSitePlusiQ8IXQ6

    Polymorphism and mutation databases

    BioMutaiPARP9
    DMDMi48474734

    Proteomic databases

    EPDiQ8IXQ6
    jPOSTiQ8IXQ6
    MassIVEiQ8IXQ6
    MaxQBiQ8IXQ6
    PaxDbiQ8IXQ6
    PeptideAtlasiQ8IXQ6
    PRIDEiQ8IXQ6
    ProteomicsDBi20136
    71045 [Q8IXQ6-1]
    71046 [Q8IXQ6-2]

    Genome annotation databases

    EnsembliENST00000360356; ENSP00000353512; ENSG00000138496 [Q8IXQ6-1]
    ENST00000462315; ENSP00000418894; ENSG00000138496 [Q8IXQ6-3]
    ENST00000471785; ENSP00000419001; ENSG00000138496 [Q8IXQ6-2]
    ENST00000477522; ENSP00000419506; ENSG00000138496 [Q8IXQ6-2]
    GeneIDi83666
    KEGGihsa:83666
    UCSCiuc003efh.5 human [Q8IXQ6-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    83666
    DisGeNETi83666

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    PARP9
    HGNCiHGNC:24118 PARP9
    HPAiHPA066708
    MIMi612065 gene
    neXtProtiNX_Q8IXQ6
    OpenTargetsiENSG00000138496
    PharmGKBiPA134870403

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG2633 Eukaryota
    COG2110 LUCA
    GeneTreeiENSGT00940000158837
    HOGENOMiHOG000115452
    InParanoidiQ8IXQ6
    KOiK15260
    OMAiYNEKSGR
    OrthoDBi681829at2759
    PhylomeDBiQ8IXQ6
    TreeFamiTF328965

    Enzyme and pathway databases

    ReactomeiR-HSA-197264 Nicotinamide salvaging

    Miscellaneous databases

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

    More...
    ChiTaRSi
    PARP9 human

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

    More...
    GenomeRNAii
    83666
    PharosiQ8IXQ6

    Protein Ontology

    More...
    PROi
    PR:Q8IXQ6

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000138496 Expressed in 184 organ(s), highest expression level in ectocervix
    ExpressionAtlasiQ8IXQ6 baseline and differential
    GenevisibleiQ8IXQ6 HS

    Family and domain databases

    InterProiView protein in InterPro
    IPR002589 Macro_dom
    IPR012317 Poly(ADP-ribose)pol_cat_dom
    PfamiView protein in Pfam
    PF01661 Macro, 2 hits
    SMARTiView protein in SMART
    SM00506 A1pp, 2 hits
    PROSITEiView protein in PROSITE
    PS51154 MACRO, 2 hits
    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 nameiPARP9_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: Q8IXQ6
    Secondary accession number(s): A8KA94
    , B2R8S9, E9PFM7, Q8TCP3, Q9BZL8, Q9BZL9
    <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: October 10, 2003
    Last sequence update: October 10, 2003
    Last modified: October 16, 2019
    This is version 143 of the entry and version 2 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, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    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 entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
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