Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 256 (23 Feb 2022)
Sequence version 4 (23 Jan 2007)
Previous versions | rss
Add a publicationFeedback
Protein

Poly [ADP-ribose] polymerase 1

Gene

PARP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:17177976, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:23230272, PubMed:25043379, PubMed:33186521, PubMed:32028527, PubMed:26344098).

Mediates glutamate, aspartate, serine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD+ is transferred to the acceptor carboxyl group of target 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 (PubMed:7852410, PubMed:9315851, PubMed:19764761, PubMed:25043379, PubMed:28190768, PubMed:29954836).

Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:33186521).

Mainly mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1 (PubMed:19764761, PubMed:25043379).

Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP1 active site (PubMed:28190768, PubMed:29954836, PubMed:33186521, PubMed:32028527).

Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1 (PubMed:30257210, PubMed:29954836).

PARP1 initiates the repair of DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (PubMed:17177976, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:23230272, PubMed:27067600).

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 (PubMed:26344098, PubMed:30356214).

Mediates the poly(ADP-ribosyl)ation of a number of proteins, including itself, APLF and CHFR (PubMed:17396150, PubMed:19764761).

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 (PubMed:27471034).

Required for PARP9 and DTX3L recruitment to DNA damage sites (PubMed:23230272).

PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (PubMed:23230272).

Acts as a regulator of transcription: positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150 (PubMed:19344625).

Plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and EEF1A1 (PubMed:17177976).

Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5 (PubMed:27257257).

Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257).

20 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 390 sec(-1) for NAD+.1 Publication
  1. KM=130 µM for NAD+1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei871NAD; via carbonyl oxygenBy similarity1
Binding sitei878NADBy similarity1
Binding sitei904NADBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei988For poly [ADP-ribose] polymerase activity3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi862 – 864NADBy similarity3

<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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.2.30, 2681

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
P09874

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-110362, POLB-Dependent Long Patch Base Excision Repair
R-HSA-192814, vRNA Synthesis
R-HSA-2173795, Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-HSA-3108214, SUMOylation of DNA damage response and repair proteins
R-HSA-5685939, HDR through MMEJ (alt-NHEJ)
R-HSA-5696394, DNA Damage Recognition in GG-NER
R-HSA-5696395, Formation of Incision Complex in GG-NER
R-HSA-5696400, Dual Incision in GG-NER

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

More...
SignaLinki
P09874

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P09874

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Poly [ADP-ribose] polymerase 1 (EC:2.4.2.306 Publications)
Short name:
PARP-1
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 11 Publication
Short name:
ARTD11 Publication
DNA ADP-ribosyltransferase PARP1Curated (EC:2.4.2.-1 Publication)
NAD(+) ADP-ribosyltransferase 11 Publication
Short name:
ADPRT 11 Publication
Poly[ADP-ribose] synthase 1
Protein poly-ADP-ribosyltransferase PARP1Curated (EC:2.4.2.-2 Publications)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PARP1Imported
Synonyms:ADPRT1 Publication, PPOL
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:270, PARP1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
173870, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P09874

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSG00000143799

<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

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi490 – 493VEVV → GEVQ: Strongly reduced interaction with TIMELESS. 1 Publication4
Mutagenesisi499S → A: Abolishes automodification on serine following interaction with HPF1; when associated with A-507 and A-519. 1 Publication1
Mutagenesisi507S → A: Abolishes automodification on serine following interaction with HPF1; when associated with A-499 and A-519. 1 Publication1
Mutagenesisi519S → A: Abolishes automodification on serine following interaction with HPF1; when associated with A-499 and A-507. 1 Publication1
Mutagenesisi797L → P: 1.5% of wild-type activity. 1 Publication1
Mutagenesisi826H → A: Strongly reduced serine ADP-ribosylation, caused by abolished interaction with HPF1. 1 Publication1
Mutagenesisi850 – 851Missing : Abolished interaction with TIMELESS. 1 Publication2
Mutagenesisi862H → A: Poly-ADP-ribosyltransferase activity is impaired while mono-ADP-ribosyltransferase activity is not affected; produces a mixture of short and mono ADP-ribose chains. 1 Publication1
Mutagenesisi868N → S: 4% of wild-type activity. 1 Publication1
Mutagenesisi883E → Q: Does not affect ADP-ribosyltransferase activity. 1 Publication1
Mutagenesisi890M → V: <0.5% of wild-type activity. 1 Publication1
Mutagenesisi893K → I: Abolishes enzymatic activity. 1 Publication1
Mutagenesisi897F → S: 10% of wild-type activity. 1 Publication1
Mutagenesisi899D → N: 0.6% of wild-type activity. 1 Publication1
Mutagenesisi908C → R: <0.5% of wild-type activity. 1 Publication1
Mutagenesisi923E → Q: Does not affect ADP-ribosyltransferase activity. 1 Publication1
Mutagenesisi926L → F: 1.5% of wild-type activity. 1 Publication1
Mutagenesisi931E → Q: Does not affect ADP-ribosyltransferase activity. 1 Publication1
Mutagenesisi986Y → H: 14% of wild-type activity and increased branching 15-fold. 1 Publication1
Mutagenesisi988E → A, D, Q or K: Poly-ADP-ribosyltransferase activity is inhibited while mono-ADP-ribosyltransferase activity is not affected; only monomers are added. Disrupts interaction with CHD1L. 4 Publications1
Mutagenesisi993D → G: Abolished interaction with TIMELESS. 1 Publication1
Mutagenesisi1003L → P: 1.5% of wild-type activity. 1 Publication1
Mutagenesisi1013 – 1014LW → EE: Strongly reduced serine ADP-ribosylation, caused by abolished interaction with HPF1. 1 Publication2

Organism-specific databases

DisGeNET

More...
DisGeNETi
142

Open Targets

More...
OpenTargetsi
ENSG00000143799

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA32

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
P09874, Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3105

Drug and drug target database

More...
DrugBanki
DB04010, 2-(3'-Methoxyphenyl) Benzimidazole-4-Carboxamide
DB03509, 2-(4-Chlorophenyl)-5-Quinoxalinecarboxamide
DB03072, 2-{3-[4-(4-Fluorophenyl)-3,6-Dihydro-1(2h)-Pyridinyl]Propyl}-8-Methyl-4(3h)-Quinazolinone
DB03722, 3,4-Dihydro-5-Methyl-Isoquinolinone
DB03073, 3-Methoxybenzamide
DB07787, 5-FLUORO-1-[4-(4-PHENYL-3,6-DIHYDROPYRIDIN-1(2H)-YL)BUTYL]QUINAZOLINE-2,4(1H,3H)-DIONE
DB07096, 6-AMINO-BENZO[DE]ISOQUINOLINE-1,3-DIONE
DB07330, A-620223
DB02498, Carba-nicotinamide-adenine-dinucleotide
DB13877, Iniparib
DB02701, Nicotinamide
DB11793, Niraparib
DB02690, NU1025
DB09074, Olaparib
DB12332, Rucaparib
DB11760, Talazoparib
DB00277, Theophylline
DB07232, Veliparib
DB01593, Zinc
DB14487, Zinc acetate
DB14533, Zinc chloride
DB14548, Zinc sulfate, unspecified form

DrugCentral

More...
DrugCentrali
P09874

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2771

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PARP1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
130781

<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%5Fprocessing%5Fsection">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 methionineiRemovedCombined sources1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002113202 – 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-acetylalanineCombined sources1 Publication1
Modified residuei41PhosphoserineCombined sources1
Modified residuei97N6-acetyllysineCombined sources1
Modified residuei105N6-acetyllysineCombined sources1
Modified residuei131N6-acetyllysineCombined sources1
Modified residuei177PhosphoserineCombined sources1
Modified residuei179PhosphoserineCombined sources1
Modified residuei185PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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)Combined sources
Cross-linki203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei274PhosphoserineCombined sources1
Modified residuei277PhosphoserineCombined sources1
Modified residuei364PhosphoserineCombined sources1
Modified residuei368PhosphothreonineCombined sources1
Modified residuei387PolyADP-ribosyl aspartic acid1 Publication1
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)Combined sources
Modified residuei471PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei484PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei488PolyADP-ribosyl glutamic acid1 Publication1
Modified residuei491PolyADP-ribosyl glutamic acid1 Publication1
Modified residuei499ADP-ribosylserine3 Publications1
Modified residuei504ADP-ribosylserine1 Publication1
Modified residuei507ADP-ribosylserine2 Publications1
Cross-linki512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei513PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei514PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei519ADP-ribosylserine2 Publications1
Modified residuei520PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki528Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei600N6-acetyllysineCombined sources1
Modified residuei621N6-acetyllysineCombined sources1
Cross-linki748Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki748Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei782PhosphoserineCombined sources1
Modified residuei786PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Poly-ADP-ribosylated on glutamate and aspartate residues by autocatalysis (PubMed:19764761). Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites (PubMed:19661379). ADP-ribosylated on serine by autocatalysis; serine ADP-ribosylation takes place following interaction with HPF1 (PubMed:28190768). Auto poly-ADP-ribosylated on serine residues, leading to dissociation of the PARP1-HPF1 complex from chromatin (By similarity).By similarity3 Publications
Phosphorylated by PRKDC (PubMed:10467406). Phosphorylated by TXK (PubMed:17177976).2 Publications
S-nitrosylated, leading to inhibit transcription regulation activity.By similarity

Keywords - PTMi

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

Proteomic databases

The CPTAC Assay portal

More...
CPTACi
CPTAC-3240
CPTAC-3241
CPTAC-556
CPTAC-557

Encyclopedia of Proteome Dynamics

More...
EPDi
P09874

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P09874

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
P09874

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P09874

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

More...
PaxDbi
P09874

PeptideAtlas

More...
PeptideAtlasi
P09874

PRoteomics IDEntifications database

More...
PRIDEi
P09874

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
52271

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P09874

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P09874, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P09874

MetOSite database of methionine sulfoxide sites

More...
MetOSitei
P09874

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

More...
PhosphoSitePlusi
P09874

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P09874

<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
ENSG00000143799, Expressed in ventricular zone and 247 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P09874, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P09874, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000143799, Low tissue specificity

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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homo- and heterodimer with PARP2.

Interacts with APTX (PubMed:15044383).

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

Interacts with SRY (PubMed:16904257). The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70 (By similarity).

Interacts with TIAM2 (By similarity).

Interacts with PARP3; leading to activate PARP1 in absence of DNA (PubMed:20064938).

Interacts (when poly-ADP-ribosylated) with CHD1L (via macro domain) (PubMed:19661379, PubMed:29220653).

Interacts with the DNA polymerase alpha catalytic subunit POLA1; this interaction functions as part of the control of replication fork progression (PubMed:9518481).

Interacts with EEF1A1 and TXK (PubMed:17177976).

Interacts with RNF4 (PubMed:19779455).

Interacts with RNF146 (PubMed:21799911).

Interacts with ZNF423 (PubMed:22863007).

Interacts with APLF (PubMed:17396150).

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 (PubMed:23230272).

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 (PubMed:21266351).

Interacts (via the PARP catalytic domain) with HPF1 (PubMed:27067600, PubMed:28190768, PubMed:29954836, PubMed:32028527).

Interacts with ZNF365 (PubMed:23966166).

Interacts with RRP1B (PubMed:19710015).

Interacts with TIMELESS; the interaction is direct (PubMed:26344098).

Interacts with CGAS; leading to impede the formation of the PARP1-TIMELESS complex (PubMed:30356214).

Interacts with KHDC3L, the interaction is increased following the formation of DNA double-strand breaks (PubMed:31609975).

By similarity23 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
106652, 734 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P09874

Database of interacting proteins

More...
DIPi
DIP-38N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P09874

Protein interaction database and analysis system

More...
IntActi
P09874, 169 interactors

Molecular INTeraction database

More...
MINTi
P09874

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000355759

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P09874

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P09874, protein

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

Secondary structure

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

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
P09874

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

More...
SMRi
P09874

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P09874

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini385 – 476BRCTPROSITE-ProRule annotationAdd BLAST92
Domaini542 – 638WGRPROSITE-ProRule annotationAdd BLAST97
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>Regioni198 – 233DisorderedSequence analysisAdd BLAST36
Regioni361 – 385DisorderedSequence analysisAdd BLAST25
Regioni373 – 524Automodification domain1 PublicationAdd BLAST152

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 signal1 Publication3
Motifi221 – 226Nuclear localization signal1 Publication6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi366 – 385Polar residuesSequence analysisAdd BLAST20

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

The N-terminal disordered region does not act as a key DNA-binding domain. The WGR and PARP catalytic domains function together to recruit PARP1 to sites of DNA breaks. The N-terminal disordered region is only required for activation on specific types of DNA damage.By similarity
The WGR domain bridges two nucleosomes, with the broken DNA aligned in a position suitable for ligation. The bridging induces structural changes in PARP1 that signal the recognition of a DNA break to the catalytic domain of PARP1, promoting HPF1 recruitment and subsequent activation of PARP1, licensing serine ADP-ribosylation of target proteins.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ARTD/PARP family.Curated

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

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156058

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_004841_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P09874

Identification of Orthologs from Complete Genome Data

More...
OMAi
HTNIDDT

Database of Orthologous Groups

More...
OrthoDBi
909382at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P09874

TreeFam database of animal gene trees

More...
TreeFami
TF316616

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.142.10, 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

More...
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
PS51977, WGR, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is 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 has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

P09874-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAESSDKLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH
60 70 80 90 100
WYHFSCFWKV GHSIRHPDVE VDGFSELRWD DQQKVKKTAE AGGVTGKGQD
110 120 130 140 150
GIGSKAEKTL GDFAAEYAKS NRSTCKGCME KIEKGQVRLS KKMVDPEKPQ
160 170 180 190 200
LGMIDRWYHP GCFVKNREEL GFRPEYSASQ LKGFSLLATE DKEALKKQLP
210 220 230 240 250
GVKSEGKRKG DEVDGVDEVA KKKSKKEKDK DSKLEKALKA QNDLIWNIKD
260 270 280 290 300
ELKKVCSTND LKELLIFNKQ QVPSGESAIL DRVADGMVFG ALLPCEECSG
310 320 330 340 350
QLVFKSDAYY CTGDVTAWTK CMVKTQTPNR KEWVTPKEFR EISYLKKLKV
360 370 380 390 400
KKQDRIFPPE TSASVAATPP PSTASAPAAV NSSASADKPL SNMKILTLGK
410 420 430 440 450
LSRNKDEVKA MIEKLGGKLT GTANKASLCI STKKEVEKMN KKMEEVKEAN
460 470 480 490 500
IRVVSEDFLQ DVSASTKSLQ ELFLAHILSP WGAEVKAEPV EVVAPRGKSG
510 520 530 540 550
AALSKKSKGQ VKEEGINKSE KRMKLTLKGG AAVDPDSGLE HSAHVLEKGG
560 570 580 590 600
KVFSATLGLV DIVKGTNSYY KLQLLEDDKE NRYWIFRSWG RVGTVIGSNK
610 620 630 640 650
LEQMPSKEDA IEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE
660 670 680 690 700
AVKKLTVNPG TKSKLPKPVQ DLIKMIFDVE SMKKAMVEYE IDLQKMPLGK
710 720 730 740 750
LSKRQIQAAY SILSEVQQAV SQGSSDSQIL DLSNRFYTLI PHDFGMKKPP
760 770 780 790 800
LLNNADSVQA KVEMLDNLLD IEVAYSLLRG GSDDSSKDPI DVNYEKLKTD
810 820 830 840 850
IKVVDRDSEE AEIIRKYVKN THATTHNAYD LEVIDIFKIE REGECQRYKP
860 870 880 890 900
FKQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM
910 920 930 940 950
VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG
960 970 980 990 1000
LGKTTPDPSA NISLDGVDVP LGTGISSGVN DTSLLYNEYI VYDIAQVNLK
1010
YLLKLKFNFK TSLW
Length:1,014
Mass (Da):113,084
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:i6A5FC01EB91C046B
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
A0A7I2V3E1A0A7I2V3E1_HUMAN
Poly [ADP-ribose] polymerase
PARP1
971Annotation score:

Annotation score:3 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>
A0A7I2V5E9A0A7I2V5E9_HUMAN
Poly [ADP-ribose] polymerase 1
PARP1
308Annotation 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>
A0A7I2V625A0A7I2V625_HUMAN
Poly [ADP-ribose] polymerase 1
PARP1
369Annotation 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>
A0A7I2V384A0A7I2V384_HUMAN
Poly [ADP-ribose] polymerase 1
PARP1
100Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti17G → E in AAB59447 (PubMed:2824474).Curated1
Sequence conflicti70E → Q in AAA60137 (PubMed:3120710).Curated1
Sequence conflicti212E → K in AAB59447 (PubMed:2824474).Curated1
Sequence conflicti613H → Q in AAA60155 (PubMed:2891139).Curated1
Sequence conflicti827N → S in AAA60155 (PubMed:2891139).Curated1
Sequence conflicti908C → Y in AAA60155 (PubMed:2891139).Curated1
Sequence conflicti980N → I in AAA60155 (PubMed:2891139).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_05046054F → L. Corresponds to variant dbSNP:rs3738708Ensembl.1
Natural variantiVAR_014714188A → T1 PublicationCorresponds to variant dbSNP:rs1805409EnsemblClinVar.1
Natural variantiVAR_019171334V → I1 PublicationCorresponds to variant dbSNP:rs3219057EnsemblClinVar.1
Natural variantiVAR_050461377P → S. Corresponds to variant dbSNP:rs2230484EnsemblClinVar.1
Natural variantiVAR_019172383S → Y1 PublicationCorresponds to variant dbSNP:rs3219062Ensembl.1
Natural variantiVAR_035852488E → V in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_014715762V → A2 PublicationsCorresponds to variant dbSNP:rs1136410Ensembl.1
Natural variantiVAR_019173940K → R2 PublicationsCorresponds to variant dbSNP:rs3219145Ensembl.1

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
M18112 mRNA Translation: AAA60137.1
J03473 mRNA Translation: AAB59447.1
M32721 mRNA Translation: AAA60155.1
M29786 M29782 Genomic DNA Translation: AAA51663.1
AF524947 Genomic DNA Translation: AAM75364.1
AL359704 Genomic DNA No translation available.
AL359742 Genomic DNA No translation available.
CH471098 Genomic DNA Translation: EAW69783.1
BC037545 mRNA Translation: AAH37545.1
X56140, X56141 Genomic DNA Translation: CAA39606.1
X16674 Genomic DNA Translation: CAA34663.1
M60436 Genomic DNA Translation: AAA60000.1
M17081 mRNA Translation: AAA51599.1 Sequence problems.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS1554.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A29725

NCBI Reference Sequences

More...
RefSeqi
NP_001609.2, NM_001618.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000366794; ENSP00000355759; ENSG00000143799

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
142

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:142

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...
MANE-Selecti
ENST00000366794.10; ENSP00000355759.5; NM_001618.4; NP_001609.2

UCSC genome browser

More...
UCSCi
uc001hqd.5, human

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs
Protein Spotlight

Catalysis - Issue 235 of April 2021

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18112 mRNA Translation: AAA60137.1
J03473 mRNA Translation: AAB59447.1
M32721 mRNA Translation: AAA60155.1
M29786 M29782 Genomic DNA Translation: AAA51663.1
AF524947 Genomic DNA Translation: AAM75364.1
AL359704 Genomic DNA No translation available.
AL359742 Genomic DNA No translation available.
CH471098 Genomic DNA Translation: EAW69783.1
BC037545 mRNA Translation: AAH37545.1
X56140, X56141 Genomic DNA Translation: CAA39606.1
X16674 Genomic DNA Translation: CAA34663.1
M60436 Genomic DNA Translation: AAA60000.1
M17081 mRNA Translation: AAA51599.1 Sequence problems.
CCDSiCCDS1554.1
PIRiA29725
RefSeqiNP_001609.2, NM_001618.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UK0X-ray3.00A/B662-1011[»]
1UK1X-ray3.00A/B662-1011[»]
1WOKX-ray3.00A/B/C/D662-1011[»]
2COKNMR-A387-486[»]
2CR9NMR-A518-643[»]
2CS2NMR-A103-223[»]
2DMJNMR-A1-93[»]
2JVNNMR-A233-358[»]
2L30NMR-A1-108[»]
2L31NMR-A103-214[»]
2N8ANMR-A1-214[»]
2RCWX-ray2.80A662-1011[»]
2RD6X-ray2.30A662-1011[»]
2RIQX-ray1.70A216-366[»]
3GJWX-ray2.30A662-1011[»]
3GN7X-ray2.50A662-1011[»]
3L3LX-ray2.50A662-1011[»]
3L3MX-ray2.50A662-1011[»]
3OD8X-ray2.40A/B/C/D/E/F/G/H2-96[»]
3ODAX-ray2.64A/B/C/D/E/F/G/H2-96[»]
3ODCX-ray2.80A/B105-206[»]
3ODEX-ray2.95A/B105-206[»]
4AV1X-ray3.10A/B/C/D5-202[»]
4DQYX-ray3.25A/D1-96[»]
B/E216-366[»]
C/F518-1014[»]
4GV7X-ray2.89A/B/C/D662-1011[»]
4HHYX-ray2.36A/B/C/D660-1011[»]
4HHZX-ray2.72A/B/C/D660-1011[»]
4L6SX-ray2.20A/B662-1011[»]
4OPXX-ray3.31A/D1-97[»]
A/D207-366[»]
C/F518-1014[»]
4OQAX-ray3.65A/D1-97[»]
A/D207-366[»]
C/F518-1014[»]
4OQBX-ray3.36A/D1-97[»]
A/D207-366[»]
C/F518-1014[»]
4PJTX-ray2.35A/B/C/D662-1011[»]
4R5WX-ray2.84A/B662-1011[»]
4R6EX-ray2.20A/B/C/D662-1011[»]
4RV6X-ray3.19A/B/C/D662-1011[»]
4UNDX-ray2.20A/B662-1011[»]
4UXBX-ray3.22A/B662-1011[»]
4XHUX-ray2.09A/C661-1014[»]
4ZZZX-ray1.90A/B655-1014[»]
5A00X-ray2.75A655-1014[»]
5DS3X-ray2.60A788-1012[»]
5HA9X-ray4.01A/B662-1011[»]
5KPNX-ray2.30A/B662-1011[»]
5KPOX-ray2.65A/B662-1011[»]
5KPPX-ray2.33A/B662-1011[»]
5KPQX-ray2.55A/B662-1011[»]
5WRQX-ray2.65A/B662-1011[»]
5WRYX-ray2.30A/B662-1011[»]
5WRZX-ray2.20A/B662-1011[»]
5WS0X-ray2.60A/B662-1011[»]
5WS1X-ray1.90A/B662-1011[»]
5WTCX-ray2.20A/B662-1011[»]
5XSRX-ray2.30A662-1011[»]
5XSTX-ray2.30A662-1010[»]
5XSUX-ray2.40A/B/C/D662-1011[»]
6BHVX-ray2.30A/B/C/D788-1012[»]
6GHKX-ray2.28A/B662-1011[»]
6M3IX-ray1.98B788-1014[»]
6NRFX-ray2.00A788-1012[»]
6NRGX-ray1.70A788-1012[»]
6NRHX-ray1.50A788-1012[»]
6NRIX-ray2.20A788-1012[»]
6NRJX-ray1.65A788-1012[»]
6NTUX-ray1.80A788-1012[»]
6VKKX-ray2.10A/B/C/D661-1011[»]
6VKOX-ray2.80A/B/C/D661-1011[»]
6VKQX-ray2.90A/B/C/D661-1011[»]
6XVWX-ray2.00A/B663-1014[»]
7AAAX-ray1.74A/B662-1011[»]
7AABX-ray2.80A/B662-1011[»]
7AACX-ray1.59A/B662-1011[»]
7AADX-ray2.21A/B662-1011[»]
7CMWX-ray2.70A/B662-1011[»]
7KK2X-ray1.70A/B662-1011[»]
7KK3X-ray2.06A/B/C/D662-1011[»]
7KK4X-ray1.96A/B662-1011[»]
7KK5X-ray1.70A/B/C/D662-1011[»]
7KK6X-ray2.06A/B662-1011[»]
7ONRX-ray2.05A/B662-1011[»]
7ONSX-ray1.97A/B662-1011[»]
7ONTX-ray1.85A/B662-1011[»]
BMRBiP09874
SMRiP09874
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi106652, 734 interactors
CORUMiP09874
DIPiDIP-38N
ELMiP09874
IntActiP09874, 169 interactors
MINTiP09874
STRINGi9606.ENSP00000355759

Chemistry databases

BindingDBiP09874
ChEMBLiCHEMBL3105
DrugBankiDB04010, 2-(3'-Methoxyphenyl) Benzimidazole-4-Carboxamide
DB03509, 2-(4-Chlorophenyl)-5-Quinoxalinecarboxamide
DB03072, 2-{3-[4-(4-Fluorophenyl)-3,6-Dihydro-1(2h)-Pyridinyl]Propyl}-8-Methyl-4(3h)-Quinazolinone
DB03722, 3,4-Dihydro-5-Methyl-Isoquinolinone
DB03073, 3-Methoxybenzamide
DB07787, 5-FLUORO-1-[4-(4-PHENYL-3,6-DIHYDROPYRIDIN-1(2H)-YL)BUTYL]QUINAZOLINE-2,4(1H,3H)-DIONE
DB07096, 6-AMINO-BENZO[DE]ISOQUINOLINE-1,3-DIONE
DB07330, A-620223
DB02498, Carba-nicotinamide-adenine-dinucleotide
DB13877, Iniparib
DB02701, Nicotinamide
DB11793, Niraparib
DB02690, NU1025
DB09074, Olaparib
DB12332, Rucaparib
DB11760, Talazoparib
DB00277, Theophylline
DB07232, Veliparib
DB01593, Zinc
DB14487, Zinc acetate
DB14533, Zinc chloride
DB14548, Zinc sulfate, unspecified form
DrugCentraliP09874
GuidetoPHARMACOLOGYi2771

PTM databases

GlyGeniP09874, 1 site, 1 O-linked glycan (1 site)
iPTMnetiP09874
MetOSiteiP09874
PhosphoSitePlusiP09874
SwissPalmiP09874

Genetic variation databases

BioMutaiPARP1
DMDMi130781

2D gel databases

SWISS-2DPAGEiP09874

Proteomic databases

CPTACiCPTAC-3240
CPTAC-3241
CPTAC-556
CPTAC-557
EPDiP09874
jPOSTiP09874
MassIVEiP09874
MaxQBiP09874
PaxDbiP09874
PeptideAtlasiP09874
PRIDEiP09874
ProteomicsDBi52271

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
3545, 1898 antibodies from 50 providers

The CPTC Antibody Portal

More...
CPTCi
P09874, 1 antibody

The DNASU plasmid repository

More...
DNASUi
142

Genome annotation databases

EnsembliENST00000366794; ENSP00000355759; ENSG00000143799
GeneIDi142
KEGGihsa:142
MANE-SelectiENST00000366794.10; ENSP00000355759.5; NM_001618.4; NP_001609.2
UCSCiuc001hqd.5, human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
142
DisGeNETi142

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PARP1
HGNCiHGNC:270, PARP1
HPAiENSG00000143799, Low tissue specificity
MIMi173870, gene
neXtProtiNX_P09874
OpenTargetsiENSG00000143799
PharmGKBiPA32
VEuPathDBiHostDB:ENSG00000143799

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1037, Eukaryota
GeneTreeiENSGT00940000156058
HOGENOMiCLU_004841_0_0_1
InParanoidiP09874
OMAiHTNIDDT
OrthoDBi909382at2759
PhylomeDBiP09874
TreeFamiTF316616

Enzyme and pathway databases

BRENDAi2.4.2.30, 2681
PathwayCommonsiP09874
ReactomeiR-HSA-110362, POLB-Dependent Long Patch Base Excision Repair
R-HSA-192814, vRNA Synthesis
R-HSA-2173795, Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-HSA-3108214, SUMOylation of DNA damage response and repair proteins
R-HSA-5685939, HDR through MMEJ (alt-NHEJ)
R-HSA-5696394, DNA Damage Recognition in GG-NER
R-HSA-5696395, Formation of Incision Complex in GG-NER
R-HSA-5696400, Dual Incision in GG-NER
SignaLinkiP09874
SIGNORiP09874

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
142, 27 hits in 1056 CRISPR screens

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

More...
ChiTaRSi
PARP1, human
EvolutionaryTraceiP09874

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PARP1

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

More...
GenomeRNAii
142
PharosiP09874, Tclin

Protein Ontology

More...
PROi
PR:P09874
RNActiP09874, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000143799, Expressed in ventricular zone and 247 other tissues
ExpressionAtlasiP09874, baseline and differential
GenevisibleiP09874, HS

Family and domain databases

Gene3Di1.20.142.10, 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
PS51977, WGR, 1 hit

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_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P09874
Secondary accession number(s): B1ANJ4, Q8IUZ9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: February 23, 2022
This is version 256 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
  7. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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

Do not show this banner again