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Protein

Poly [ADP-ribose] polymerase 1

Gene

Parp1

Organism
Mus musculus (Mouse)
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. 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. Mediates the poly(ADP-ribosyl)ation of a number of proteins, including itself, APLF and CHFR. Also mediates serine ADP-ribosylation of target proteins following interaction with HPF1; HPF1 conferring serine specificity. Probably also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1. Catalyzes the poly-ADP-ribosylation of histones in a HPF1-dependent manner. 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. ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. 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. 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. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. Acts as a regulator of transcription: positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. 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. Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming.By similarity

<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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 – 372By similarityAdd BLAST371
<p>This subsection of the ‘Function’ 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

<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:2.4.2.30By similarity)
Short name:
PARP-1
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 1
Short name:
ARTD1
DNA ADP-ribosyltransferase PARP1Curated (EC:2.4.2.-By similarity)
NAD(+) ADP-ribosyltransferase 1
Short name:
ADPRT 1
Poly[ADP-ribose] synthase 1
Short name:
msPARP
Protein poly-ADP-ribosyltransferase PARP1Curated (EC:2.4.2.-By similarity)
<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:Parp1
Synonyms:Adprp, Adprt, Adprt1
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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: Unplaced

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:1340806 Parp1

<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; 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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice show a complete lack of nuclear poly-ADP-ribosylation (PubMed:7578427). Mice are however viable and fertile (PubMed:7578427). Moreover, repair of UV and MNNG induced DNA damage are not affected (PubMed:7578427). However, about 30% of the mutant mice developed pathological skin aberrations on a mixed 129/Sv x C57B1/6 genetic background (PubMed:7578427). Mice lacking both Parp1 and Parp2 are not viable and die at the onset of gastrulation (PubMed:12727891).2 Publications

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3740

<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 methionineiRemovedBy similarity
<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_00000232592 – 1013Poly [ADP-ribose] polymerase 1Add BLAST1012

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-acetylalanineBy similarity1
Modified residuei41PhosphoserineBy similarity1
Modified residuei97N6-acetyllysineCombined sources1
Modified residuei105N6-acetyllysineBy similarity1
Modified residuei131N6-acetyllysineBy similarity1
Modified residuei177PhosphoserineBy similarity1
Modified residuei179PhosphoserineBy similarity1
Modified residuei185PhosphoserineBy similarity1
<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)By similarity
Cross-linki203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei274PhosphoserineBy similarity1
Modified residuei277PhosphoserineBy similarity1
Modified residuei387PolyADP-ribosyl aspartic acidBy similarity1
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)By similarity
Modified residuei484PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei488PolyADP-ribosyl glutamic acidBy similarity1
Modified residuei491PolyADP-ribosyl glutamic acidBy similarity1
Modified residuei499ADP-ribosylserineBy similarity1
Modified residuei506ADP-ribosylserineBy similarity1
Cross-linki511Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei512PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei513PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei518ADP-ribosylserineBy similarity1
Modified residuei519PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki527Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei599N6-acetyllysineBy similarity1
Modified residuei620N6-acetyllysineBy similarity1
Cross-linki747Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki747Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei781PhosphoserineBy similarity1
Modified residuei785PhosphoserineBy similarity1

<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

S-nitrosylated, leading to inhibit transcription regulation activity.1 Publication
Phosphorylated by PRKDC and TXK.By similarity
Poly-ADP-ribosylated on glutamate and aspartate residues by autocatalysis. Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites. ADP-ribosylated on serine by autocatalysis; serine ADP-ribosylation takes place following interaction with HPF1.By similarity

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P11103

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P11103

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

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PaxDbi
P11103

PeptideAtlas

More...
PeptideAtlasi
P11103

PRoteomics IDEntifications database

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PRIDEi
P11103

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P11103

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

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PhosphoSitePlusi
P11103

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P11103

<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 (PubMed:9642267). Expression is correlated with proliferation, with higher levels occurring during early fetal development and organogenesis and in the highly proliferative cell compartments of adult (PubMed:9642267). Expressed in B-cells that have been induced to switch to various Ig isotypes (PubMed:9642267).1 Publication

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

At stage E12.5, expressed at high level in the developing liver and kidneys (PubMed:11948190). Expressed at higher level in the genital ridge and the spinal ganglia (PubMed:11948190). At E18.5, preferentially expressed in the thymus and in regions of the nervous system (PubMed:11948190). Within the developing trunk, preferential expression persisted in the liver and became restricted to the cortical region of the kidney, spleen, adrenal gland, and to stomach and intestinal epithelia (PubMed:11948190). From E14.5 to E18.5, as well as in the adult, expressed at the highest level in thymus (PubMed:11948190). Expression is particularly high in the subcapsular zone of the thymus where immature lymphocytes proliferate (PubMed:11948190). Expressed at high level in the seminiferous tubules of the developing testis (PubMed:11948190).1 Publication

Gene expression databases

CleanEx database of gene expression profiles

More...
CleanExi
MM_PARP1

<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 (By similarity). Interacts with APTX (By similarity). Component of a base excision repair (BER) complex, containing at least XRCC1, PARP1, PARP2, POLB and LRIG3 (PubMed:11948190). Interacts with SRY (By similarity). The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70 (PubMed:9642267). Interacts with TIAM2 (PubMed:17320046). Interacts with PARP3; leading to activate PARP1 in absence of DNA (By similarity). Interacts (when poly-ADP-ribosylated) with CHD1L (By similarity). Interacts with the DNA polymerase alpha catalytic subunit POLA1; this interaction functions as part of the control of replication fork progression (By similarity). Interacts with EEF1A1 and TXK (By similarity). Interacts with RNF4 (PubMed:19779455). Interacts with RNF146 (By similarity). Interacts with ZNF423 (PubMed:14623329). Interacts with APLF (By similarity). 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 (By similarity). 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 (By similarity). Interacts (via the PARP catalytic domain) with HPF1 (By similarity). Interacts with ZNF365 (By similarity). Interacts with RRP1B (By similarity). Interacts with TIMELESS; the interaction is direct (By similarity). Interacts with CGAS; leading to impede the formation of the PARP1-TIMELESS complex (By similarity).By similarity6 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

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P11103

Database of interacting proteins

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DIPi
DIP-39371N

Protein interaction database and analysis system

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IntActi
P11103, 20 interactors

Molecular INTeraction database

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MINTi
P11103

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000027777

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P11103

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P11103

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

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SMRi
P11103

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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>Domaini385 – 476BRCTPROSITE-ProRule annotationAdd BLAST92
Domaini661 – 778PARP alpha-helicalPROSITE-ProRule annotationAdd BLAST118
Domaini787 – 1013PARP 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 – 523Automodification domainBy similarityAdd BLAST151

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 signalBy similarity3
Motifi221 – 226Nuclear localization signalBy similarity6

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

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eggNOGi
KOG1037 Eukaryota
ENOG410XP18 LUCA

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG053513

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P11103

Database for complete collections of gene phylogenies

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PhylomeDBi
P11103

Family and domain databases

Conserved Domains Database

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CDDi
cd00027 BRCT, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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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

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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

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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

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PIRSFi
PIRSF000489 NAD_ADPRT, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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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

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SUPFAMi
SSF142921 SSF142921, 1 hit
SSF47587 SSF47587, 1 hit
SSF52113 SSF52113, 1 hit

PROSITE; a protein domain and family database

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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>.<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_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 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.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P11103-1) [UniParc]FASTAAdd to basket
Also known as: Long

This isoform has been chosen as the 'canonical' 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
MAEASERLYR VQYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH
60 70 80 90 100
WYHFSCFWKV GQSIRHPDVE VDGFSELRWD DQQKVKKTAE AGGVAGKGQD
110 120 130 140 150
GSGGKAEKTL GDFAAEYAKS NRSMCKGCLE KIEKGQMRLS KKMVDPEKPQ
160 170 180 190 200
LGMIDRWYHP TCFVKKRDEL GFRPEYSASQ LKGFSLLSAE DKEALKKQLP
210 220 230 240 250
AIKNEGKRKG DEVDGTDEVA KKKSRKETDK YSKLEKALKA QNELIWNIKD
260 270 280 290 300
ELKKACSTND LKELLIFNQQ QVPSGESAIL DRVADGMAFG ALLPCKECSG
310 320 330 340 350
QLVFKSDAYY CTGDVTAWTK CMVKTQNPSR KEWVTPKEFR EISYLKKLKV
360 370 380 390 400
KKQDRIFPPE SSAPITVHWP LSVTSAPTAV NSSAPADKPL SNMKILTLGK
410 420 430 440 450
LSQNKDEAKA VIEKLGGKLT GSANKASLCI SIKKEVEKMN KKMEEVKEAN
460 470 480 490 500
IRVVSEDFLQ DVSASTKSLQ DLLSAHSLSP WGAEVKAEPG EVVAPRGKSA
510 520 530 540 550
APSKKSKGCF KEEGVNKSEK RMKLTLKGGA AVDPDSGLEH SAHVLEKGGK
560 570 580 590 600
VFSATLGLVD IVKGTNSYYK LQLLEDDKES RYWIFRSWGR LGTVIGSNKL
610 620 630 640 650
EQMPSKEEAV EQFMKLYEEK TGNAWHSKNF TKYPKKFYPL EIDYGQDEEA
660 670 680 690 700
VKKLTVKPGT KSKLPKPVQE LVGMIFDVDS MKKALVEYEI DLQKMPLGKL
710 720 730 740 750
SRRQIQAAYS ILSEVQQPVS QGSSESQILD LSNRFYTLIP HDFGMKKPPL
760 770 780 790 800
LNNADSVQAK VEMLDNLLDI EVAYSLLRGG SDDSSKDPID VNYEKLKTDI
810 820 830 840 850
KVVDRDSEEA EVIRKYVKNT HATTHNAYDL EVIDIFKIER EGESQRYKPF
860 870 880 890 900
RQLHNRRLLW HGSRTTNFAG ILSQGLRIAP PEAPVTGYMF GKGIYFADMV
910 920 930 940 950
SKSANYCHTS QGDPIGLIML GEVALGNMYE LKHASHISKL PKGKHSVKGL
960 970 980 990 1000
GKTTPDPSAS ITLEGVEVPL GTGIPSGVND TALLYNEYIV YDIAQVNLKY
1010
LLKLKFNFKT SLW
Length:1,013
Mass (Da):113,100
Last modified:January 23, 2007 - v3
<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:i5E54C3E5F60BB922
GO
Isoform 2 (identifier: P11103-2) [UniParc]FASTAAdd to basket
Also known as: Short1 Publication, sPARP-11 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-521: Missing.

Note: No experimental confirmation available.
Show »
Length:492
Mass (Da):55,237
Checksum:i6F429A5F21D15246
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q921K2Q921K2_MOUSE
Poly [ADP-ribose] polymerase
Parp1 Adprt1, mCG_19846
1,014Annotation 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>
A0A0A6YVX0A0A0A6YVX0_MOUSE
Poly [ADP-ribose] polymerase
Parp1
99Annotation 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>
A0A0A6YX03A0A0A6YX03_MOUSE
Poly [ADP-ribose] polymerase 1
Parp1
67Annotation 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>
A0A0A6YY63A0A0A6YY63_MOUSE
Poly [ADP-ribose] polymerase 1
Parp1
68Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAF61293 differs from that shown. Reason: Erroneous initiation.Curated

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 conflicti114A → L AA sequence (PubMed:9642267).Curated1
Sequence conflicti591L → V in AAF61293 (PubMed:10809783).Curated1
Sequence conflicti608E → D in AAF61293 (PubMed:10809783).Curated1
Sequence conflicti612Q → H in AAF61293 (PubMed:10809783).Curated1
Sequence conflicti629N → D in AAF61293 (PubMed:10809783).Curated1
Sequence conflicti679D → E in AAF61293 (PubMed:10809783).Curated1
Sequence conflicti717Q → E in AAF61293 (PubMed:10809783).Curated1
Sequence conflicti758Q → L in AAF61293 (PubMed:10809783).Curated1
Sequence conflicti982A → C in AAF61293 (PubMed:10809783).Curated1

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0189701 – 521Missing in isoform 2. 1 PublicationAdd BLAST521

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
X14206 mRNA Translation: CAA32421.1
AF126717 mRNA Translation: AAF61293.1 Different initiation.

Protein sequence database of the Protein Information Resource

More...
PIRi
S04200

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.277779

Keywords - Coding sequence diversityi

Alternative initiation

<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
X14206 mRNA Translation: CAA32421.1
AF126717 mRNA Translation: AAF61293.1 Different initiation.
PIRiS04200
UniGeneiMm.277779

3D structure databases

ProteinModelPortaliP11103
SMRiP11103
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

CORUMiP11103
DIPiDIP-39371N
IntActiP11103, 20 interactors
MINTiP11103
STRINGi10090.ENSMUSP00000027777

Chemistry databases

BindingDBiP11103
ChEMBLiCHEMBL3740

PTM databases

iPTMnetiP11103
PhosphoSitePlusiP11103
SwissPalmiP11103

Proteomic databases

EPDiP11103
MaxQBiP11103
PaxDbiP11103
PeptideAtlasiP11103
PRIDEiP11103

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1340806 Parp1

Phylogenomic databases

eggNOGiKOG1037 Eukaryota
ENOG410XP18 LUCA
HOVERGENiHBG053513
InParanoidiP11103
PhylomeDBiP11103

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P11103

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

CleanExiMM_PARP1

Family and domain databases

CDDicd00027 BRCT, 1 hit
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...

<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_MOUSE
<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: P11103
Secondary accession number(s): Q9JLX4, Q9QVQ3
<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: January 16, 2019
This is version 201 of the entry and version 3 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

<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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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