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Entry version 149 (02 Jun 2021)
Sequence version 3 (23 Jan 2007)
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Protein

Poly [ADP-ribose] polymerase 1

Gene

PARP1

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
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 transcript 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. 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. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Mainly mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1. Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP1 active site. Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1. 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. 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. Mediates the poly(ADP-ribosyl)ation of a number of proteins, including itself, APLF and CHFR. 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. 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. 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%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

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 sitei870NAD; via carbonyl oxygenBy similarity1
Binding sitei877NADBy similarity1
Binding sitei903NADBy 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 sitei987For poly [ADP-ribose] polymerase activityBy similarity1

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 bindingi861 – 863NADBy 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

<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:2.4.2.30By 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%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:PARP1
Synonyms:ADPRT
<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>OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
<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 identifieri10029 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaCricetidaeCricetinaeCricetulus

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2321638

<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 methionineiRemovedBy similarity
<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_00002113192 – 1013Poly [ADP-ribose] polymerase 1Add BLAST1012

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineBy similarity1
Modified residuei41PhosphoserineBy similarity1
Modified residuei97N6-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%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)By similarity
Cross-linki203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei274PhosphoserineBy similarity1
Modified residuei277PhosphoserineBy similarity1
Modified residuei387PolyADP-ribosyl aspartic acidBy similarity1
Modified residuei407PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei413PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei435PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei437PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei444PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei445PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei456PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki467Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei471PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei484PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei488PolyADP-ribosyl glutamic acidBy similarity1
Modified residuei491PolyADP-ribosyl glutamic acidBy similarity1
Modified residuei499ADP-ribosylserineBy similarity1
Modified residuei503ADP-ribosylserineBy similarity1
Modified residuei506ADP-ribosylserineBy similarity1
Cross-linki511Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei512PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei513PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei518ADP-ribosylserineBy similarity1
Modified residuei519PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki527Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei599N6-acetyllysineBy similarity1
Modified residuei620N6-acetyllysineBy similarity1
Cross-linki747Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki747Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei781PhosphoserineBy similarity1
Modified residuei785PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%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. 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). Auto poly-ADP-ribosylated on serine residues, leading to dissociation of the PARP1-HPF1 complex from chromatin (By similarity).By similarity
S-nitrosylated, leading to inhibit transcription regulation activity.By similarity
Phosphorylated by PRKDC and TXK.By similarity

Keywords - PTMi

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

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q9R152

<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 (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 (via macro domain).

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 (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.

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 similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10029.NP_001233650.1

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

3D structure databases

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

More...
SMRi
Q9R152

Database of comparative protein structure models

More...
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%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
Domaini553 – 629WGRSequence analysisAdd BLAST77
Domaini661 – 778PARP alpha-helicalPROSITE-ProRule annotationAdd BLAST118
Domaini787 – 1013PARP catalyticPROSITE-ProRule annotationAdd BLAST227

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni198 – 233DisorderedSequence analysisAdd BLAST36
Regioni357 – 383DisorderedSequence analysisAdd BLAST27
Regioni373 – 523Automodification domainBy similarityAdd BLAST151
Regioni495 – 516DisorderedSequence analysisAdd BLAST22

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

<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

Database of Orthologous Groups

More...
OrthoDBi
909382at2759

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

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

<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>Sequencei

<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.

Q9R152-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEASERLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH
60 70 80 90 100
WYHFSCFWKV GHSIRQPDVE VDGFSELRWD DQQKVKKTAE AGGVAGKGQD
110 120 130 140 150
GSGGKSEKTL GDFAAEYAKS NRSTCKGCME KIEKGQVRLS KKMLDPEKPQ
160 170 180 190 200
LGMIDRWYHP TCFVKNREEL GFRPEYSASQ LKGFSLLSAE DKEVLKKQLP
210 220 230 240 250
GVKSEGKRKG DEVDGADEVA KKKSKKGKDK DSKLEKALKA QNDLIWNIKD
260 270 280 290 300
ELKKACSTSD LKELLIFNQQ QVPSGESAIL DRVADGMAFG ALLPCKECSG
310 320 330 340 350
QLVFKSDAYY CTGDVTAWTK CMVKTQTPSR KEWVTPKEFR EISYLKKLKV
360 370 380 390 400
KKQDRIFPPE TSAPAPPHLP PSVTSAPTAV NSSCPADKPL SNMKILTLGK
410 420 430 440 450
LSQSKDEAKA TIEKLGGKLT GSANNASLCI STKKEVEKMG KKMEEVQAAN
460 470 480 490 500
VRVVCEDFLQ DVAASTKSLQ ELLSAHSLSS WGAEVKVEPV EVAAPKGKSA
510 520 530 540 550
APSKKSKGLY KEEGVNKSEK RMKLTLKGGA AVDPDSGLEH SAHVLEKGGK
560 570 580 590 600
VFSATLGLVD IVKGTNSYYK LQLLEDDKES RYWIFRSWGR VGTVIGSNKL
610 620 630 640 650
EQMPSKEDAV EHFMKLYEEK TGNAWHSKNF TKYPKKFYPL EIDYGQDEEA
660 670 680 690 700
VKKLTVKPGT KSKLPKAVQE LVGMIFDVES MKKALVEYEI DLQKMPLGKL
710 720 730 740 750
SKRQIQAAYS ILSEVQQAVS QGSSDSQILD LSNRFYTLIP HDFGMKKPPL
760 770 780 790 800
LNNADSVQAK VEMLDNLLDI EVAYSLLRGG SDDSSKDPID VNYEKLKTDI
810 820 830 840 850
KVVDRDSEEA EVIRKYVKNT HATTHNAYDL EVMDIFKIER EGESQRYKPF
860 870 880 890 900
KQLHNRRLLW HGSRTTNFAG ILSQGLRIAP PEAPVTGYMF GKGIYFADMV
910 920 930 940 950
SKSANYCHTS QGDPIGLILL GEVALGNMYE LKHASHISKL PKGKHSVKGL
960 970 980 990 1000
GKTTPDPSAS ITLEGVEVPL GTGIPSGVND TCLLYNEYIV YDIAQVNLKY
1010
LLKLKFNFKT SLW
Length:1,013
Mass (Da):112,532
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i90617C4DB91C9DEC
GO

Sequence databases

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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
AF168781 mRNA Translation: AAD45817.1

NCBI Reference Sequences

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RefSeqi
NP_001233650.1, NM_001246721.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
100689463

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cge:100689463

<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
AF168781 mRNA Translation: AAD45817.1
RefSeqiNP_001233650.1, NM_001246721.1

3D structure databases

SMRiQ9R152
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10029.NP_001233650.1

Chemistry databases

ChEMBLiCHEMBL2321638

Proteomic databases

PRIDEiQ9R152

Genome annotation databases

GeneIDi100689463
KEGGicge:100689463

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
142

Phylogenomic databases

eggNOGiKOG1037, Eukaryota
OrthoDBi909382at2759

Miscellaneous databases

Protein Ontology

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PROi
PR:Q9R152

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

MobiDB: a database of protein disorder and mobility annotations

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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_CRIGR
<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: Q9R152
<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: September 26, 2001
Last sequence update: January 23, 2007
Last modified: June 2, 2021
This is version 149 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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