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Entry version 128 (02 Jun 2021)
Sequence version 1 (01 Jul 1993)
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Protein

Poly [ADP-ribose] polymerase 1

Gene

parp1

Organism
Xenopus laevis (African clawed frog)
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 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.

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 sitei854NAD; via carbonyl oxygenBy similarity1
Binding sitei861NADBy similarity1
Binding sitei887NADBy 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 sitei971For 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 fingeri‹1 – 78PARP-type 1PROSITE-ProRule annotationAdd BLAST›78
Zinc fingeri99 – 189PARP-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 bindingi845 – 847NADBy 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
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
<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>OrganismiXenopus laevis (African clawed frog)
<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 identifieri8355 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

<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 describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000211324‹1 – 998Poly [ADP-ribose] polymerase 1Add BLAST›998

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 residuei391PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei397PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei419PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei428PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei429PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei445PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei447PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei454PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei467PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei471PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei477PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei495PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei496PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei503PolyADP-ribosyl glutamic acidSequence analysis1

<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.By similarity

Keywords - PTMi

ADP-ribosylation

<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

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P31669, 1 interactor

<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
P31669

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>Domaini369 – 460BRCTPROSITE-ProRule annotationAdd BLAST92
Domaini537 – 613WGRSequence analysisAdd BLAST77
Domaini645 – 762PARP alpha-helicalPROSITE-ProRule annotationAdd BLAST118
Domaini771 – 997PARP 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>Regioni185 – 211DisorderedSequence analysisAdd BLAST27
Regioni348 – 370DisorderedSequence analysisAdd BLAST23
Regioni357 – 507Automodification domainBy similarityAdd BLAST151
Regioni471 – 510DisorderedSequence analysisAdd BLAST40

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>Motifi193 – 195Nuclear localization signalBy similarity3
Motifi207 – 212Nuclear localization signalBy similarity6

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 biasi348 – 362Pro residuesSequence analysisAdd BLAST15
Compositional biasi490 – 510Basic and acidic residuesSequence analysisAdd BLAST21

<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 fingeri‹1 – 78PARP-type 1PROSITE-ProRule annotationAdd BLAST›78
Zinc fingeri99 – 189PARP-type 2PROSITE-ProRule annotationAdd BLAST91

Keywords - Domaini

Repeat, Zinc-finger

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: Fragment.

P31669-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
AKSGRASCKK CGDNIAKESL GLAIMVQSPM FDGKVPHWHH YSCFWKRARV
60 70 80 90 100
LSQGDIYGYT ELRWEDQEMI KKAIETGGAA AGAGGDSKGG KGEMTLNDFA
110 120 130 140 150
AEYAKSNRSA CKGCEQKIEK GQIRISKKSV DVERPQLGMI DRWYHPDCFV
160 170 180 190 200
SSREELDFLP SYSASQLKGF TILSAEDKDS LKKKLPAVKN EGKRKADEVD
210 220 230 240 250
GHSAATKKKI KKEKEKESKL EKLLKEQTEL IWHIKDELKK VCSTNDLKEL
260 270 280 290 300
LIANKQQVPS GETNIVDRVS DGMAFGALLP CEECSGQFVF KGDAYYCTGD
310 320 330 340 350
LSAWTKCVAK TQTPNRKDWV TPKEFHEIPY LKKFKFKRHD RAFPPCAAPT
360 370 380 390 400
PISPPAAPEP KPTVEETFPE GKPLTNTKVL LIGKLSKNKD EVKTLIEGLG
410 420 430 440 450
GKVAGSAHKA NLCISTNKEV KKMSKKMEEV KAANVRVVSD DFLKEVESGK
460 470 480 490 500
SVQELLSQFG ISSWGAEIKQ EAVQPTEKQP SSGPVAGKSS GKVKEEKGSN
510 520 530 540 550
KSEKKMKLTV KGGAAIDPDS ELEDSCHVLE TGGKIFSATL GLVDITRGTN
560 570 580 590 600
SYYKLQLIEH DRDSRYWVFR SWGRVGTVIG SKKLEEMSSK EDAIEHFLNL
610 620 630 640 650
YQDKTGNAWH SPNFTKYPKK FYPLEIDYGQ EEDVVKKLSV GAGTKSKLAK
660 670 680 690 700
PVQELIKLIF DVESMKKAMV EFEIDLQKMP LGKLSKRQIQ SAYSILSQVQ
710 720 730 740 750
QAVSESLSEA RLLDLSNQFY TLIPHDFGMK KPPLLNNLEY IQAKVQMLDN
760 770 780 790 800
LLDIEVAYSL LRGGADDGEK DPIDVKYEKI KTDIKVVAKD SEESRIICDY
810 820 830 840 850
VKNTHADTHN AYDLEVLEIF KIDREGEYQR YKPFKQLHNR QLLWHGSRTT
860 870 880 890 900
NFAGILSQGL RIAPPEAPVT GYMFGKGIYF ADMVSKSANY CHAMPGSPIG
910 920 930 940 950
LILLGEVALG NMHELKAASQ ITKLPKGKHS VKGLGRTAPD PSATVQLDGV
960 970 980 990
DVPLGKGTSA NISDTSLLYN EYIVYDIAQV NLKYLLKLKF NYKGGMMW
Length:998
Mass (Da):111,126
Last modified:July 1, 1993 - v1
<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:iF5A25E4A3366BAE7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.<p><a href='/help/non_ter' target='_top'>More...</a></p>Non-terminal residuei11
<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 conflicti746Q → E (PubMed:8503897).Curated1

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
Z12139 mRNA Translation: CAA78126.1
D13810 mRNA Translation: BAA02966.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S31735

<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
Z12139 mRNA Translation: CAA78126.1
D13810 mRNA Translation: BAA02966.1
PIRiS31735

3D structure databases

SMRiP31669
ModBaseiSearch...

Protein-protein interaction databases

IntActiP31669, 1 interactor

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

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_XENLA
<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: P31669
<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, 1993
Last sequence update: July 1, 1993
Last modified: June 2, 2021
This is version 128 of the entry and version 1 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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