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Protein

Poly [ADP-ribose] polymerase 2

Gene

Parp2

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 (PubMed:10364231). 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 (By similarity). 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:10364231). Also mediates serine ADP-ribosylation of target proteins following interaction with HPF1; HPF1 conferring serine specificity (By similarity). In addition to proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex (By similarity).By similarity1 Publication

<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 bindingi1 – 65Sequence analysisAdd BLAST65

<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

  • base-excision repair Source: MGI
  • DNA repair Source: MGI
  • double-strand break repair Source: GO_Central
  • extrinsic apoptotic signaling pathway Source: MGI
  • negative regulation of neuron death Source: MGI
  • peptidyl-serine ADP-ribosylation Source: UniProtKB
  • positive regulation of cell growth involved in cardiac muscle cell development Source: MGI
  • protein poly-ADP-ribosylation Source: GO_Central

<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
LigandNAD

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-110362 POLB-Dependent Long Patch Base Excision Repair
R-MMU-5685939 HDR through MMEJ (alt-NHEJ)
R-MMU-5696394 DNA Damage Recognition in GG-NER
R-MMU-5696395 Formation of Incision Complex in GG-NER
R-MMU-5696400 Dual Incision in GG-NER

<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 2 (EC:2.4.2.30By similarity)
Short name:
PARP-2
Short name:
mPARP-2
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 2
Short name:
ARTD2
DNA ADP-ribosyltransferase PARP2Curated (EC:2.4.2.-By similarity)
NAD(+) ADP-ribosyltransferase 2
Short name:
ADPRT-2
Poly[ADP-ribose] synthase 2
Short name:
pADPRT-2
Protein poly-ADP-ribosyltransferase PARP2Curated (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:Parp2
Synonyms:Adprt2, Adprtl2, Aspartl2
<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: Chromosome 14

Organism-specific databases

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

More...
MGIi
MGI:1341112 Parp2

<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

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

No visible phenotype in normal conditions, but mutant mice are sensitive to ionizing radiation (PubMed:12727891). Following alkylating agent treatment, cells show increased post-replicative genomic instability, G2/M accumulation and chromosome missegregation accompanying kinetochore defects (PubMed:12727891). Mice lacking both Parp1 and Parp2 are not viable and die at the onset of gastrulation (PubMed:12727891).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>Mutagenesisi36K → R: Decreases levels of mono-ADP-ribosylation without loss of enzyme activity. 1 Publication1
Mutagenesisi37K → R: Decreases levels of mono-ADP-ribosylation without loss of enzyme activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2794

<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_00002113281 – 559Poly [ADP-ribose] polymerase 2Add BLAST559

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 residuei36N6-(ADP-ribosyl)lysine; alternate1 Publication1
Modified residuei36N6-acetyllysine; alternate1 Publication1
Modified residuei37N6-(ADP-ribosyl)lysine; alternate1 Publication1
Modified residuei37N6-acetyllysine; alternate1 Publication1
Modified residuei208PhosphoserineBy 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

Poly-ADP-ribosylated by PARP1.1 Publication
Acetylation reduces DNA binding and enzymatic activity.1 Publication

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
O88554

MaxQB - The MaxQuant DataBase

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MaxQBi
O88554

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

More...
PaxDbi
O88554

PeptideAtlas

More...
PeptideAtlasi
O88554

PRoteomics IDEntifications database

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PRIDEi
O88554

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O88554

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

More...
PhosphoSitePlusi
O88554

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
O88554

<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 were in testis followed by ovary. Expression is correlated with proliferation, with higher levels occurring during early fetal development and organogenesis and in the highly proliferative cell compartments of adult.

<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. At E18.5, preferentially expressed in the thymus and in regions of the nervous system. 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. From E14.5 to E18.5, as well as in the adult, expressed at the highest level in thymus. Expression is particularly high in the subcapsular zone of the thymus where immature lymphocytes proliferate.

<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

By high levels of DNA-damaging agents.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000036023 Expressed in 279 organ(s), highest expression level in embryo

CleanEx database of gene expression profiles

More...
CleanExi
MM_PARP2

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O88554 MM

<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

Component of a base excision repair (BER) complex, containing at least XRCC1, PARP1, POLB and LRIG3 (PubMed:11948190). Homo- and heterodimer with PARP1 (By similarity). Interacts weakly (via the PARP catalytic domain) with HPF1 (By similarity).By similarity1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
197999, 3 interactors

Protein interaction database and analysis system

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IntActi
O88554, 1 interactor

Molecular INTeraction database

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MINTi
O88554

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000048877

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
O88554

<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

1559
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GS0X-ray2.80A/B207-557[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
O88554

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

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SMRi
O88554

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...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O88554

<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>Domaini207 – 324PARP alpha-helicalPROSITE-ProRule annotationAdd BLAST118
Domaini332 – 559PARP catalyticPROSITE-ProRule annotationAdd BLAST228

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>Motifi3 – 9Nuclear localization signalSequence analysis7
Motifi33 – 39Nuclear localization signalSequence analysis7

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1037 Eukaryota
ENOG410XP18 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000158452

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000173055

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG053514

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O88554

KEGG Orthology (KO)

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KOi
K10798

Identification of Orthologs from Complete Genome Data

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OMAi
IPHVFGR

Database of Orthologous Groups

More...
OrthoDBi
909382at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O88554

TreeFam database of animal gene trees

More...
TreeFami
TF315407

Family and domain databases

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

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
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

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

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SMARTi
View protein in SMART
SM00773 WGR, 1 hit

Superfamily database of structural and functional annotation

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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_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>Sequence (1+)i

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

O88554-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPRRQRSGS GRRVLNEAKK VDNGNKATED DSPPGKKMRT CQRKGPMAGG
60 70 80 90 100
KDADRTKDNR DSVKTLLLKG KAPVDPECAA KLGKAHVYCE GDDVYDVMLN
110 120 130 140 150
QTNLQFNNNK YYLIQLLEDD AQRNFSVWMR WGRVGKTGQH SLVTCSGDLN
160 170 180 190 200
KAKEIFQKKF LDKTKNNWED RENFEKVPGK YDMLQMDYAA STQDESKTKE
210 220 230 240 250
EETLKPESQL DLRVQELLKL ICNVQTMEEM MIEMKYDTKR APLGKLTVAQ
260 270 280 290 300
IKAGYQSLKK IEDCIRAGQH GRALVEACNE FYTRIPHDFG LSIPPVIRTE
310 320 330 340 350
KELSDKVKLL EALGDIEIAL KLVKSERQGL EHPLDQHYRN LHCALRPLDH
360 370 380 390 400
ESNEFKVISQ YLQSTHAPTH KDYTMTLLDV FEVEKEGEKE AFREDLPNRM
410 420 430 440 450
LLWHGSRLSN WVGILSHGLR VAPPEAPITG YMFGKGIYFA DMSSKSANYC
460 470 480 490 500
FASRLKNTGL LLLSEVALGQ CNELLEANPK AQGLLRGKHS TKGMGKMAPS
510 520 530 540 550
PAHFITLNGS TVPLGPASDT GILNPEGYTL NYNEFIVYSP NQVRMRYLLK

IQFNFLQLW
Length:559
Mass (Da):63,397
Last modified:September 26, 2001 - 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:iE0AEDAEE412C1445
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A2I3BPY1A0A2I3BPY1_MOUSE
Poly [ADP-ribose] polymerase 2
Parp2
42Annotation 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 AAC25415 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 conflicti82L → V in AAK13253 (PubMed:11133988).Curated1
Sequence conflicti177V → I in AAK13253 (PubMed:11133988).Curated1
Sequence conflicti486R → Q in AAK13253 (PubMed:11133988).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AJ007780 mRNA Translation: CAA07679.1
AF191547 Genomic DNA Translation: AAK13253.1
BC062150 mRNA Translation: AAH62150.1
AF072521 mRNA Translation: AAC25415.1 Different initiation.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS27025.1

NCBI Reference Sequences

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RefSeqi
NP_033762.1, NM_009632.2
XP_006518505.1, XM_006518442.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.281482

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000036126; ENSMUSP00000048877; ENSMUSG00000036023

Database of genes from NCBI RefSeq genomes

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GeneIDi
11546

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:11546

UCSC genome browser

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UCSCi
uc007tlq.1 mouse

<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
AJ007780 mRNA Translation: CAA07679.1
AF191547 Genomic DNA Translation: AAK13253.1
BC062150 mRNA Translation: AAH62150.1
AF072521 mRNA Translation: AAC25415.1 Different initiation.
CCDSiCCDS27025.1
RefSeqiNP_033762.1, NM_009632.2
XP_006518505.1, XM_006518442.3
UniGeneiMm.281482

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GS0X-ray2.80A/B207-557[»]
ProteinModelPortaliO88554
SMRiO88554
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi197999, 3 interactors
IntActiO88554, 1 interactor
MINTiO88554
STRINGi10090.ENSMUSP00000048877

Chemistry databases

BindingDBiO88554
ChEMBLiCHEMBL2794

PTM databases

iPTMnetiO88554
PhosphoSitePlusiO88554

Proteomic databases

EPDiO88554
MaxQBiO88554
PaxDbiO88554
PeptideAtlasiO88554
PRIDEiO88554

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036126; ENSMUSP00000048877; ENSMUSG00000036023
GeneIDi11546
KEGGimmu:11546
UCSCiuc007tlq.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10038
MGIiMGI:1341112 Parp2

Phylogenomic databases

eggNOGiKOG1037 Eukaryota
ENOG410XP18 LUCA
GeneTreeiENSGT00940000158452
HOGENOMiHOG000173055
HOVERGENiHBG053514
InParanoidiO88554
KOiK10798
OMAiIPHVFGR
OrthoDBi909382at2759
PhylomeDBiO88554
TreeFamiTF315407

Enzyme and pathway databases

ReactomeiR-MMU-110362 POLB-Dependent Long Patch Base Excision Repair
R-MMU-5685939 HDR through MMEJ (alt-NHEJ)
R-MMU-5696394 DNA Damage Recognition in GG-NER
R-MMU-5696395 Formation of Incision Complex in GG-NER
R-MMU-5696400 Dual Incision in GG-NER

Miscellaneous databases

EvolutionaryTraceiO88554
PMAP-CutDBiO88554

Protein Ontology

More...
PROi
PR:O88554

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000036023 Expressed in 279 organ(s), highest expression level in embryo
CleanExiMM_PARP2
GenevisibleiO88554 MM

Family and domain databases

Gene3Di1.20.142.10, 1 hit
2.20.140.10, 1 hit
InterProiView protein in InterPro
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
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...

<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 nameiPARP2_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: O88554
Secondary accession number(s): Q99N29
<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: September 26, 2001
Last sequence update: September 26, 2001
Last modified: January 16, 2019
This is version 160 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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