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Entry version 190 (31 Jul 2019)
Sequence version 4 (23 Jan 2007)
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Protein

Poly [ADP-ribose] polymerase 1

Gene

Parp1

Organism
Rattus norvegicus (Rat)
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 <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi2 – 373By similarityAdd BLAST372
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri9 – 93PARP-type 1PROSITE-ProRule annotationAdd BLAST85
Zinc fingeri113 – 203PARP-type 2PROSITE-ProRule annotationAdd BLAST91

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

GO - Biological processi

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

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-110362 POLB-Dependent Long Patch Base Excision Repair
R-RNO-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-RNO-3108214 SUMOylation of DNA damage response and repair proteins
R-RNO-5685939 HDR through MMEJ (alt-NHEJ)
R-RNO-5696394 DNA Damage Recognition in GG-NER
R-RNO-5696395 Formation of Incision Complex in GG-NER
R-RNO-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 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 PARP1By similarity (EC:2.4.2.-By similarity)
NAD(+) ADP-ribosyltransferase 1
Short name:
ADPRT 1
Poly[ADP-ribose] synthase 1
Protein poly-ADP-ribosyltransferase PARP1By similarity (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:Adprt
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 13

Organism-specific databases

Rat genome database

More...
RGDi
2053 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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4664

<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_00002113212 – 1014Poly [ADP-ribose] polymerase 1Add BLAST1013

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineBy similarity1
Modified residuei41PhosphoserineBy similarity1
Modified residuei97N6-acetyllysineBy similarity1
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-linki250Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei275PhosphoserineBy similarity1
Modified residuei278PhosphoserineBy similarity1
Modified residuei388PolyADP-ribosyl aspartic acidBy similarity1
Modified residuei408PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei414PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei436PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei438PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei445PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei446PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei457PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki468Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei485PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki487Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki487Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei489PolyADP-ribosyl glutamic acidBy similarity1
Modified residuei492PolyADP-ribosyl glutamic acidBy similarity1
Modified residuei500ADP-ribosylserineBy similarity1
Modified residuei507ADP-ribosylserineBy similarity1
Cross-linki512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei513PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei514PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei519ADP-ribosylserineBy similarity1
Modified residuei520PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki528Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei600N6-acetyllysineBy similarity1
Modified residuei621N6-acetyllysineBy similarity1
Cross-linki748Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki748Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei782PhosphoserineBy similarity1
Modified residuei786PhosphoserineBy 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

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
S-nitrosylated, leading to inhibit transcription regulation activity.By similarity

Keywords - PTMi

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

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P27008

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

More...
PaxDbi
P27008

PRoteomics IDEntifications database

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PRIDEi
P27008

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P27008

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P27008

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

More...
PhosphoSitePlusi
P27008

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000003084 Expressed in 9 organ(s), highest expression level in heart

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P27008 RN

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

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

Homo- and heterodimer with PARP2.

Interacts with APTX (By similarity).

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

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

Interacts with TIAM2 (By similarity).

Interacts with PARP3; leading to activate PARP1 in absence of DNA (By similarity).

Interacts (when poly-ADP-ribosylated) with CHD1L.

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

Interacts with EEF1A1 and TXK.

Interacts with RNF4.

Interacts with RNF146.

Interacts with ZNF423.

Interacts with APLF.

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

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 (PubMed:25625556).

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.

Interacts (via the PARP catalytic domain) with HPF1.

Interacts with ZNF365.

Interacts with RRP1B.

Interacts with TIMELESS; the interaction is direct.

Interacts with CGAS; leading to impede the formation of the PARP1-TIMELESS complex (By similarity).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
247621, 16 interactors

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000004232

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P27008

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

Secondary structure

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

3D structure databases

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

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SMRi
P27008

Database of comparative protein structure models

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ModBasei
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>Domaini386 – 477BRCTPROSITE-ProRule annotationAdd BLAST92
Domaini662 – 779PARP alpha-helicalPROSITE-ProRule annotationAdd BLAST118
Domaini788 – 1014PARP catalyticPROSITE-ProRule annotationAdd BLAST227

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni374 – 524Automodification 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

More...
eggNOGi
KOG1037 Eukaryota
ENOG410XP18 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156058

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000030402

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P27008

KEGG Orthology (KO)

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KOi
K10798

Identification of Orthologs from Complete Genome Data

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OMAi
WNHASCI

Database of Orthologous Groups

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OrthoDBi
909382at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P27008

TreeFam database of animal gene trees

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TreeFami
TF316616

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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

Integrated resource of protein families, domains and functional sites

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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

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

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000489 NAD_ADPRT, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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

PROSITE; a protein domain and family database

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

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

<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.

P27008-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEATERLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH
60 70 80 90 100
WYHFSCFWKV GHSIRQPDTE VDGFSELRWD DQQKVKKTAE AGGVAGKGQH
110 120 130 140 150
GGGGKAEKTL GDFAAEYAKS NRSTCKGCME KIEKGQMRLS KKMLDPEKPQ
160 170 180 190 200
LGMIDRWYHP TCFVKNRDEL GFRPEYSASQ LKGFSLLSAE DKEALKKQLP
210 220 230 240 250
AVKSEGKRKC DEVDGIDEVA KKKSKKGKDK ESSKLEKALK AQNELVWNIK
260 270 280 290 300
DELKKACSTN DLKELLIFNQ QQVPSGESAI LDRVADGMAF GALLPCKECS
310 320 330 340 350
GQLVFKSDAY YCTGDVTAWT KCMVKTQNPS RKEWVTPKEF REISYLKKLK
360 370 380 390 400
IKKQDRLFPP ESSAPAPPAP PVSITSAPTA VNSSAPADKP LSNMKILTLG
410 420 430 440 450
KLSQNKDEAK AMIEKLGGKL TGSANKASLC ISTKKEVEKM SKKMEEVKAA
460 470 480 490 500
NVRVVCEDFL QDVSASAKSL QELLSAHSLS SWGAEVKVEP GEVVVPKGKS
510 520 530 540 550
AAPSKKSKGA VKEEGVNKSE KRMKLTLKGG AAVDPDSGLE HSAHVLEKGG
560 570 580 590 600
KVFSATLGLV DIVKGTNSYY KLQLLESDKE SRYWIFRSWG RVGTVIGSNK
610 620 630 640 650
LEQMPSKEDA VEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE
660 670 680 690 700
AVKKLAVKPG TKSKLPKPVQ ELVGMIFDVE SMKKALVEYE IDLQKMPLGK
710 720 730 740 750
LSRRQIQAAY SILSEVQQAV SQGSSESQIL DLSNRFYTLI PHDFGMKKPP
760 770 780 790 800
LLNNTDSVQA KVEMLDNLLD IEVAYSLLRG GSDDSSKDPI DVNYEKLKTD
810 820 830 840 850
IKVVDRDSEE AEVIRKYVKN THATTHNAYD LEVIDIFKIE REGESQRYKP
860 870 880 890 900
FRQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM
910 920 930 940 950
VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG
960 970 980 990 1000
LGKTAPDPSA SITLDGVEVP LGTGIPSGVN DTCLLYNEYI VYDIAQVNLK
1010
YLLKLKFNFK TSLW
Length:1,014
Mass (Da):112,660
Last modified:January 23, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBE1B6F2B29B887ED
GO

<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 CAA46478 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 conflicti639Y → H in CAA46478 (PubMed:2508731).Curated1
Sequence conflicti642E → A in CAA46478 (PubMed:2508731).Curated1
Sequence conflicti753N → D in CAA46478 (PubMed:2508731).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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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
U94340 mRNA Translation: AAC53544.1
BC085765 mRNA Translation: AAH85765.1
X65496 Genomic DNA Translation: CAA46477.1
X65497 Genomic DNA Translation: CAA46478.1 Different initiation.

Protein sequence database of the Protein Information Resource

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PIRi
S21163
S26057

NCBI Reference Sequences

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RefSeqi
NP_037195.1, NM_013063.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000004232; ENSRNOP00000004232; ENSRNOG00000003084

Database of genes from NCBI RefSeq genomes

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GeneIDi
25591

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:25591

UCSC genome browser

More...
UCSCi
RGD:2053 rat

<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
U94340 mRNA Translation: AAC53544.1
BC085765 mRNA Translation: AAH85765.1
X65496 Genomic DNA Translation: CAA46477.1
X65497 Genomic DNA Translation: CAA46478.1 Different initiation.
PIRiS21163
S26057
RefSeqiNP_037195.1, NM_013063.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LE0NMR-A389-487[»]
SMRiP27008
ModBaseiSearch...

Protein-protein interaction databases

BioGridi247621, 16 interactors
STRINGi10116.ENSRNOP00000004232

Chemistry databases

BindingDBiP27008
ChEMBLiCHEMBL4664

PTM databases

CarbonylDBiP27008
iPTMnetiP27008
PhosphoSitePlusiP27008

Proteomic databases

jPOSTiP27008
PaxDbiP27008
PRIDEiP27008

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000004232; ENSRNOP00000004232; ENSRNOG00000003084
GeneIDi25591
KEGGirno:25591
UCSCiRGD:2053 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
142
RGDi2053 Parp1

Phylogenomic databases

eggNOGiKOG1037 Eukaryota
ENOG410XP18 LUCA
GeneTreeiENSGT00940000156058
HOGENOMiHOG000030402
InParanoidiP27008
KOiK10798
OMAiWNHASCI
OrthoDBi909382at2759
PhylomeDBiP27008
TreeFamiTF316616

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P27008

Gene expression databases

BgeeiENSRNOG00000003084 Expressed in 9 organ(s), highest expression level in heart
GenevisibleiP27008 RN

Family and domain databases

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPARP1_RAT
<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: P27008
Secondary accession number(s): O35937
<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: August 1, 1992
Last sequence update: January 23, 2007
Last modified: July 31, 2019
This is version 190 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<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
UniProt is an ELIXIR core data resource
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