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 202 (17 Jun 2020)
Sequence version 2 (14 Apr 2009)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Poly [ADP-ribose] polymerase tankyrase-1

Gene

TNKS

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 involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking (PubMed:10988299, PubMed:11739745, PubMed:16076287, PubMed:19759537, PubMed:21478859, PubMed:22864114, PubMed:23622245, PubMed:25043379). Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation (PARsylation) of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation (PubMed:19759537, PubMed:21478859). Also mediates PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination (PubMed:21478859). Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length (PubMed:11739745). Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI (PubMed:22864114). May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles (PubMed:10988299). May be involved in spindle pole assembly through PARsylation of NUMA1 (PubMed:16076287). Stimulates 26S proteasome activity (PubMed:23622245).8 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Specifically inhibited by XAV939, a small molecule, leading to inhibit the Wnt signaling pathway by stabilizing AXIN1 and AXIN2.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1234ZincCombined sources1 Publication1
Metal bindingi1237ZincCombined sources1 Publication1
Metal bindingi1242ZincCombined sources1 Publication1
Metal bindingi1245ZincCombined sources1 Publication1

<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 functionGlycosyltransferase, Transferase
Biological processCell cycle, Cell division, Mitosis, mRNA transport, Protein transport, Translocation, Transport, Wnt signaling pathway
LigandMetal-binding, NAD, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.2.30 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-201681 TCF dependent signaling in response to WNT
R-HSA-4641257 Degradation of AXIN
R-HSA-5545619 XAV939 inhibits tankyrase, stabilizing AXIN
R-HSA-5689880 Ub-specific processing proteases
R-HSA-8948751 Regulation of PTEN stability and activity

SIGNOR Signaling Network Open Resource

More...
SIGNORi
O95271

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.I.1.1.3 the nuclear pore complex (npc) family

<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 tankyrase-1Curated (EC:2.4.2.301 Publication)
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 51 Publication
Short name:
ARTD51 Publication
Poly [ADP-ribose] polymerase 5A1 Publication
Protein poly-ADP-ribosyltransferase tankyrase-1Curated (EC:2.4.2.-2 Publications)
TNKS-1
TRF1-interacting ankyrin-related ADP-ribose polymerase
Tankyrase I
Tankyrase-11 Publication
Short name:
TANK11 Publication
<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:TNKSImported
Synonyms:PARP5A1 Publication, PARPL, TIN1, TINF1, TNKS1
<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 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000173273.15

Human Gene Nomenclature Database

More...
HGNCi
HGNC:11941 TNKS

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
603303 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O95271

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane, Nuclear pore complex, Nucleus, Telomere

<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>Mutagenesisi1184H → A: Loss of activity; when associated with A-1291. 1 Publication1
Mutagenesisi1291E → A: Loss of activity; when associated with A-1184. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
8658

Open Targets

More...
OpenTargetsi
ENSG00000173273

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA36631

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
O95271 Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL6164

DrugCentral

More...
DrugCentrali
O95271

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
3108

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
TNKS

<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_00002113331 – 1327Poly [ADP-ribose] polymerase tankyrase-1Add BLAST1327

<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

Phosphorylated on serine residues by MAPK kinases upon insulin stimulation. Phosphorylated during mitosis.1 Publication
Ubiquitinated by RNF146 when auto-poly-ADP-ribosylated, leading to its degradation.1 Publication
ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination.1 Publication

Keywords - PTMi

ADP-ribosylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
O95271

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
O95271

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
O95271

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O95271

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

More...
PaxDbi
O95271

PeptideAtlas

More...
PeptideAtlasi
O95271

PRoteomics IDEntifications database

More...
PRIDEi
O95271

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
50772 [O95271-1]
50773 [O95271-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O95271

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

More...
PhosphoSitePlusi
O95271

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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous; highest levels in testis.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000173273 Expressed in forebrain and 229 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
O95271 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O95271 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000173273 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

Oligomerizes and associates with TNKS2.

Interacts with the cytoplasmic domain of LNPEP/Otase in SLC2A4/GLUT4-vesicles. Binds to the N-terminus of telomeric TERF1 via the ANK repeats.

Found in a complex with POT1; TERF1 and TINF2 (PubMed:12768206).

Interacts with AXIN1 (PubMed:19759537, PubMed:21478859, PubMed:21799911).

Interacts with AXIN2 (PubMed:19759537, PubMed:21478859).

Interacts with BLZF1 and CASC3 (PubMed:21478859).

Interacts with NUMA1 (PubMed:12080061).

5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">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
114207, 66 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
O95271

Database of interacting proteins

More...
DIPi
DIP-36652N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
O95271

Protein interaction database and analysis system

More...
IntActi
O95271, 49 interactors

Molecular INTeraction database

More...
MINTi
O95271

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000311579

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
O95271

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
O95271 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

11327
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
O95271

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
O95271

<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 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati181 – 209ANK 1Sequence analysisAdd BLAST29
Repeati215 – 244ANK 2Sequence analysisAdd BLAST30
Repeati248 – 277ANK 3Sequence analysisAdd BLAST30
Repeati281 – 310ANK 4Sequence analysisAdd BLAST30
Repeati335 – 364ANK 5Sequence analysisAdd BLAST30
Repeati368 – 397ANK 6Sequence analysisAdd BLAST30
Repeati401 – 430ANK 7Sequence analysisAdd BLAST30
Repeati434 – 463ANK 8Sequence analysisAdd BLAST30
Repeati521 – 553ANK 9Sequence analysisAdd BLAST33
Repeati557 – 586ANK 10Sequence analysisAdd BLAST30
Repeati590 – 619ANK 11Sequence analysisAdd BLAST30
Repeati621 – 647ANK 12Sequence analysisAdd BLAST27
Repeati649 – 679ANK 13Sequence analysisAdd BLAST31
Repeati683 – 712ANK 14Sequence analysisAdd BLAST30
Repeati716 – 745ANK 15Sequence analysisAdd BLAST30
Repeati749 – 778ANK 16Sequence analysisAdd BLAST30
Repeati782 – 810ANK 17Sequence analysisAdd BLAST29
Repeati836 – 865ANK 18Sequence analysisAdd BLAST30
Repeati869 – 898ANK 19Sequence analysisAdd BLAST30
Repeati902 – 931ANK 20Sequence analysisAdd BLAST30
Repeati935 – 964ANK 21Sequence analysisAdd BLAST30
<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>Domaini1030 – 1089SAMPROSITE-ProRule annotationAdd BLAST60
Domaini1112 – 1317PARP catalyticPROSITE-ProRule annotationAdd BLAST206

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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi9 – 14Poly-HisPROSITE-ProRule annotation6
Compositional biasi20 – 83Pro-richPROSITE-ProRule annotationAdd BLAST64
Compositional biasi109 – 161Ser-richPROSITE-ProRule annotationAdd BLAST53

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4177 Eukaryota
COG0666 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156161

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O95271

KEGG Orthology (KO)

More...
KOi
K10799

Identification of Orthologs from Complete Genome Data

More...
OMAi
ETINCRD

Database of Orthologous Groups

More...
OrthoDBi
111565at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O95271

TreeFam database of animal gene trees

More...
TreeFami
TF326036

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.150.50, 1 hit
1.25.40.20, 5 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
IPR012317 Poly(ADP-ribose)pol_cat_dom
IPR001660 SAM
IPR013761 SAM/pointed_sf
IPR028731 TANK1

The PANTHER Classification System

More...
PANTHERi
PTHR24180:SF3 PTHR24180:SF3, 5 hits

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00023 Ank, 1 hit
PF12796 Ank_2, 4 hits
PF13606 Ank_3, 1 hit
PF00644 PARP, 1 hit
PF07647 SAM_2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01415 ANKYRIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00248 ANK, 17 hits
SM00454 SAM, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47769 SSF47769, 1 hit
SSF48403 SSF48403, 3 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 15 hits
PS51059 PARP_CATALYTIC, 1 hit
PS50105 SAM_DOMAIN, 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>Sequences (2+)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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O95271-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAASRRSQHH HHHHQQQLQP APGASAPPPP PPPPLSPGLA PGTTPASPTA
60 70 80 90 100
SGLAPFASPR HGLALPEGDG SRDPPDRPRS PDPVDGTSCC STTSTICTVA
110 120 130 140 150
AAPVVPAVST SSAAGVAPNP AGSGSNNSPS SSSSPTSSSS SSPSSPGSSL
160 170 180 190 200
AESPEAAGVS STAPLGPGAA GPGTGVPAVS GALRELLEAC RNGDVSRVKR
210 220 230 240 250
LVDAANVNAK DMAGRKSSPL HFAAGFGRKD VVEHLLQMGA NVHARDDGGL
260 270 280 290 300
IPLHNACSFG HAEVVSLLLC QGADPNARDN WNYTPLHEAA IKGKIDVCIV
310 320 330 340 350
LLQHGADPNI RNTDGKSALD LADPSAKAVL TGEYKKDELL EAARSGNEEK
360 370 380 390 400
LMALLTPLNV NCHASDGRKS TPLHLAAGYN RVRIVQLLLQ HGADVHAKDK
410 420 430 440 450
GGLVPLHNAC SYGHYEVTEL LLKHGACVNA MDLWQFTPLH EAASKNRVEV
460 470 480 490 500
CSLLLSHGAD PTLVNCHGKS AVDMAPTPEL RERLTYEFKG HSLLQAAREA
510 520 530 540 550
DLAKVKKTLA LEIINFKQPQ SHETALHCAV ASLHPKRKQV TELLLRKGAN
560 570 580 590 600
VNEKNKDFMT PLHVAAERAH NDVMEVLHKH GAKMNALDTL GQTALHRAAL
610 620 630 640 650
AGHLQTCRLL LSYGSDPSII SLQGFTAAQM GNEAVQQILS ESTPIRTSDV
660 670 680 690 700
DYRLLEASKA GDLETVKQLC SSQNVNCRDL EGRHSTPLHF AAGYNRVSVV
710 720 730 740 750
EYLLHHGADV HAKDKGGLVP LHNACSYGHY EVAELLVRHG ASVNVADLWK
760 770 780 790 800
FTPLHEAAAK GKYEICKLLL KHGADPTKKN RDGNTPLDLV KEGDTDIQDL
810 820 830 840 850
LRGDAALLDA AKKGCLARVQ KLCTPENINC RDTQGRNSTP LHLAAGYNNL
860 870 880 890 900
EVAEYLLEHG ADVNAQDKGG LIPLHNAASY GHVDIAALLI KYNTCVNATD
910 920 930 940 950
KWAFTPLHEA AQKGRTQLCA LLLAHGADPT MKNQEGQTPL DLATADDIRA
960 970 980 990 1000
LLIDAMPPEA LPTCFKPQAT VVSASLISPA STPSCLSAAS SIDNLTGPLA
1010 1020 1030 1040 1050
ELAVGGASNA GDGAAGTERK EGEVAGLDMN ISQFLKSLGL EHLRDIFETE
1060 1070 1080 1090 1100
QITLDVLADM GHEELKEIGI NAYGHRHKLI KGVERLLGGQ QGTNPYLTFH
1110 1120 1130 1140 1150
CVNQGTILLD LAPEDKEYQS VEEEMQSTIR EHRDGGNAGG IFNRYNVIRI
1160 1170 1180 1190 1200
QKVVNKKLRE RFCHRQKEVS EENHNHHNER MLFHGSPFIN AIIHKGFDER
1210 1220 1230 1240 1250
HAYIGGMFGA GIYFAENSSK SNQYVYGIGG GTGCPTHKDR SCYICHRQML
1260 1270 1280 1290 1300
FCRVTLGKSF LQFSTMKMAH APPGHHSVIG RPSVNGLAYA EYVIYRGEQA
1310 1320
YPEYLITYQI MKPEAPSQTA TAAEQKT
Length:1,327
Mass (Da):142,039
Last modified:April 14, 2009 - v2
<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:i44BDE985C715BEFF
GO
Isoform 2 (identifier: O95271-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     641-643: EST → GHS
     644-1327: Missing.

Show »
Length:643
Mass (Da):67,203
Checksum:iFA67DE30C2A2F3B8
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 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7EWY6E7EWY6_HUMAN
Poly [ADP-ribose] polymerase tankyr...
TNKS
617Annotation score:

Annotation score:2 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>
E5RHD2E5RHD2_HUMAN
Poly [ADP-ribose] polymerase tankyr...
TNKS
243Annotation score:

Annotation score:2 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>
E7EQ52E7EQ52_HUMAN
Poly [ADP-ribose] polymerase
TNKS
1,090Annotation score:

Annotation score:2 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>
A0A0C4DGE3A0A0C4DGE3_HUMAN
Poly [ADP-ribose] polymerase tankyr...
TNKS
68Annotation 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>
H0YAW5H0YAW5_HUMAN
Poly [ADP-ribose] polymerase tankyr...
TNKS
61Annotation 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 conflicti83P → Q in AAH98394 (PubMed:15489334).Curated1
Sequence conflicti802R → K in AAC79841 (PubMed:9822378).Curated1
Sequence conflicti802R → K in AAC79842 (PubMed:9822378).Curated1
Sequence conflicti1001E → G in AAH98394 (PubMed:15489334).Curated1
Sequence conflicti1266M → I in AAH98394 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004538641 – 643EST → GHS in isoform 2. 1 Publication3
Alternative sequenceiVSP_004539644 – 1327Missing in isoform 2. 1 PublicationAdd BLAST684

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
AF082556 mRNA Translation: AAC79841.1
AF082557 mRNA Translation: AAC79842.1
AF082558 mRNA Translation: AAC79843.1
AF082559 mRNA Translation: AAC79844.1
AC103834 Genomic DNA No translation available.
AC103877 Genomic DNA No translation available.
AC104052 Genomic DNA No translation available.
AC021242 Genomic DNA No translation available.
BC098394 mRNA Translation: AAH98394.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS5974.1 [O95271-1]

NCBI Reference Sequences

More...
RefSeqi
NP_003738.2, NM_003747.2 [O95271-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000310430; ENSP00000311579; ENSG00000173273 [O95271-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
8658

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:8658

UCSC genome browser

More...
UCSCi
uc003wss.4 human [O95271-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF082556 mRNA Translation: AAC79841.1
AF082557 mRNA Translation: AAC79842.1
AF082558 mRNA Translation: AAC79843.1
AF082559 mRNA Translation: AAC79844.1
AC103834 Genomic DNA No translation available.
AC103877 Genomic DNA No translation available.
AC104052 Genomic DNA No translation available.
AC021242 Genomic DNA No translation available.
BC098394 mRNA Translation: AAH98394.1
CCDSiCCDS5974.1 [O95271-1]
RefSeqiNP_003738.2, NM_003747.2 [O95271-1]

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
2RF5X-ray2.30A1091-1325[»]
3UDDX-ray1.95A/B1105-1327[»]
3UH2X-ray2.00A/B1105-1327[»]
3UH4X-ray2.00A/B1105-1327[»]
4DVIX-ray1.90A/B1104-1314[»]
4I9IX-ray2.40A/B/C/D1104-1314[»]
4K4EX-ray2.30A/B1104-1314[»]
4K4FX-ray2.90A/B1104-1314[»]
4KRSX-ray2.29A/B1105-1327[»]
4LI6X-ray2.05A/B1105-1327[»]
4LI7X-ray2.20A/B1105-1327[»]
4LI8X-ray2.52A/B1105-1327[»]
4MSGX-ray1.80A/B1104-1314[»]
4MSKX-ray2.30A/B/C/D1104-1314[»]
4MT9X-ray2.00A/B1104-1314[»]
4N3RX-ray1.90A/B1104-1314[»]
4N4VX-ray2.00A/B1104-1314[»]
4OA7X-ray2.30A/B/C/D1105-1313[»]
4TORX-ray1.50A/B/C/D1105-1315[»]
4TOSX-ray1.80A/B1105-1315[»]
4U6AX-ray2.37A1091-1325[»]
4UUHX-ray2.52A1091-1325[»]
4UW1X-ray3.37A/B/C/D/E/F/G/H1091-1325[»]
4W5SX-ray2.80A1105-1314[»]
4W6EX-ray1.95A1106-1314[»]
5EBTX-ray2.24A/B/C/D1106-1314[»]
5ECEX-ray2.20A/B/C/D1105-1316[»]
5ETYX-ray2.90A/B/C/D1091-1324[»]
5GP7X-ray1.50A799-957[»]
5JHQX-ray3.20A/B/C/D174-649[»]
5JTIX-ray2.90A/B/C/D/E/F1018-1093[»]
5JU5X-ray2.50A/B/C/D/E/F1018-1093[»]
5KNIX-ray2.50A/B/C/D/E/F/G1026-1091[»]
6QXUX-ray1.20A1104-1314[»]
SMRiO95271
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi114207, 66 interactors
CORUMiO95271
DIPiDIP-36652N
ELMiO95271
IntActiO95271, 49 interactors
MINTiO95271
STRINGi9606.ENSP00000311579

Chemistry databases

BindingDBiO95271
ChEMBLiCHEMBL6164
DrugCentraliO95271
GuidetoPHARMACOLOGYi3108

Protein family/group databases

TCDBi1.I.1.1.3 the nuclear pore complex (npc) family

PTM databases

iPTMnetiO95271
PhosphoSitePlusiO95271

Polymorphism and mutation databases

BioMutaiTNKS

Proteomic databases

EPDiO95271
jPOSTiO95271
MassIVEiO95271
MaxQBiO95271
PaxDbiO95271
PeptideAtlasiO95271
PRIDEiO95271
ProteomicsDBi50772 [O95271-1]
50773 [O95271-2]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
O95271 1 sequenced antibody

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
22078 359 antibodies

Genome annotation databases

EnsembliENST00000310430; ENSP00000311579; ENSG00000173273 [O95271-1]
GeneIDi8658
KEGGihsa:8658
UCSCiuc003wss.4 human [O95271-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8658
DisGeNETi8658
EuPathDBiHostDB:ENSG00000173273.15

GeneCards: human genes, protein and diseases

More...
GeneCardsi
TNKS
HGNCiHGNC:11941 TNKS
HPAiENSG00000173273 Low tissue specificity
MIMi603303 gene
neXtProtiNX_O95271
OpenTargetsiENSG00000173273
PharmGKBiPA36631

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4177 Eukaryota
COG0666 LUCA
GeneTreeiENSGT00940000156161
InParanoidiO95271
KOiK10799
OMAiETINCRD
OrthoDBi111565at2759
PhylomeDBiO95271
TreeFamiTF326036

Enzyme and pathway databases

BRENDAi2.4.2.30 2681
ReactomeiR-HSA-201681 TCF dependent signaling in response to WNT
R-HSA-4641257 Degradation of AXIN
R-HSA-5545619 XAV939 inhibits tankyrase, stabilizing AXIN
R-HSA-5689880 Ub-specific processing proteases
R-HSA-8948751 Regulation of PTEN stability and activity
SIGNORiO95271

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
8658 5 hits in 790 CRISPR screens

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

More...
ChiTaRSi
TNKS human
EvolutionaryTraceiO95271

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
TNKS

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

More...
GenomeRNAii
8658
PharosiO95271 Tchem

Protein Ontology

More...
PROi
PR:O95271
RNActiO95271 protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000173273 Expressed in forebrain and 229 other tissues
ExpressionAtlasiO95271 baseline and differential
GenevisibleiO95271 HS

Family and domain databases

Gene3Di1.10.150.50, 1 hit
1.25.40.20, 5 hits
InterProiView protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
IPR012317 Poly(ADP-ribose)pol_cat_dom
IPR001660 SAM
IPR013761 SAM/pointed_sf
IPR028731 TANK1
PANTHERiPTHR24180:SF3 PTHR24180:SF3, 5 hits
PfamiView protein in Pfam
PF00023 Ank, 1 hit
PF12796 Ank_2, 4 hits
PF13606 Ank_3, 1 hit
PF00644 PARP, 1 hit
PF07647 SAM_2, 1 hit
PRINTSiPR01415 ANKYRIN
SMARTiView protein in SMART
SM00248 ANK, 17 hits
SM00454 SAM, 1 hit
SUPFAMiSSF47769 SSF47769, 1 hit
SSF48403 SSF48403, 3 hits
PROSITEiView protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 15 hits
PS51059 PARP_CATALYTIC, 1 hit
PS50105 SAM_DOMAIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTNKS1_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: O95271
Secondary accession number(s): O95272, Q4G0F2
<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: March 27, 2002
Last sequence update: April 14, 2009
Last modified: June 17, 2020
This is version 202 of the entry and version 2 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
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