Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tankyrase-2

Gene

Tnks2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation 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. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. Stimulates 26S proteasome activity (By similarity).By similarity

Catalytic activityi

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.PROSITE-ProRule annotation

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1081 – 10811ZincBy similarity
Metal bindingi1084 – 10841ZincBy similarity
Metal bindingi1089 – 10891ZincBy similarity
Metal bindingi1092 – 10921ZincBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-201681. TCF dependent signaling in response to WNT.
R-MMU-4641257. Degradation of AXIN.

Names & Taxonomyi

Protein namesi
Recommended name:
Tankyrase-2 (EC:2.4.2.30)
Short name:
TANK2
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 6
Short name:
ARTD6
TNKS-2
TRF1-interacting ankyrin-related ADP-ribose polymerase 2
Tankyrase II
Gene namesi
Name:Tnks2
Synonyms:Tank2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1921743. Tnks2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Golgi apparatus, Membrane, Nucleus, Telomere

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3232703.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11661166Tankyrase-2PRO_0000409512Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei238 – 2381(3S)-3-hydroxyhistidine; by HIF1ANBy similarity
Modified residuei271 – 2711(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei427 – 4271(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei518 – 5181(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei553 – 5531(3S)-3-hydroxyhistidine; by HIF1ANBy similarity
Modified residuei586 – 5861(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei671 – 6711(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei706 – 7061(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei739 – 7391(3S)-3-hydroxyasparagine; by HIF1ANBy similarity

Post-translational modificationi

Ubiquitinated by RNF146 when auto-poly-ADP-ribosylated, leading to its degradation.By similarity
ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination (By similarity).By similarity

Keywords - PTMi

ADP-ribosylation, Hydroxylation, Ubl conjugation

Proteomic databases

PaxDbiQ3UES3.
PRIDEiQ3UES3.

PTM databases

iPTMnetiQ3UES3.
PhosphoSiteiQ3UES3.
SwissPalmiQ3UES3.

Expressioni

Gene expression databases

BgeeiENSMUSG00000024811.
ExpressionAtlasiQ3UES3. baseline and differential.
GenevisibleiQ3UES3. MM.

Interactioni

Subunit structurei

Oligomerizes and associates with TNKS. Interacts with the cytoplasmic domain of LNPEP/Otase in SLC2A4/GLUT4-vesicles. Binds to the N-terminus of Grb14 and TRF1 with its ankyrin repeat region. Interacts with HIF1AN (By similarity). Interacts with RNF146; this interaction leads to ubiquitination and proteasomal degradation (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi216798. 18 interactions.
IntActiQ3UES3. 18 interactions.
STRINGi10090.ENSMUSP00000025729.

Chemistry

BindingDBiQ3UES3.

Structurei

3D structure databases

ProteinModelPortaliQ3UES3.
SMRiQ3UES3. Positions 26-797, 952-1161.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati23 – 5230ANK 1Add
BLAST
Repeati57 – 8630ANK 2Add
BLAST
Repeati90 – 11930ANK 3Add
BLAST
Repeati123 – 15230ANK 4Add
BLAST
Repeati210 – 23930ANK 5Add
BLAST
Repeati243 – 27230ANK 6Add
BLAST
Repeati276 – 30530ANK 7Add
BLAST
Repeati363 – 39533ANK 8Add
BLAST
Repeati399 – 42830ANK 9Add
BLAST
Repeati432 – 46130ANK 10Add
BLAST
Repeati463 – 48927ANK 11Add
BLAST
Repeati525 – 55430ANK 12Add
BLAST
Repeati558 – 58730ANK 13Add
BLAST
Repeati591 – 62030ANK 14Add
BLAST
Repeati624 – 65229ANK 15Add
BLAST
Repeati678 – 70730ANK 16Add
BLAST
Repeati711 – 74030ANK 17Add
BLAST
Repeati744 – 77330ANK 18Add
BLAST
Domaini873 – 93664SAMPROSITE-ProRule annotationAdd
BLAST
Domaini959 – 1164206PARP catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni545 – 5539HIF1AN-bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi826 – 85833Ser-richAdd
BLAST

Sequence similaritiesi

Contains 18 ANK repeats.PROSITE-ProRule annotation
Contains 1 PARP catalytic domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG4177. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129677.
HOGENOMiHOG000246964.
HOVERGENiHBG059472.
InParanoidiQ3UES3.
KOiK10799.
OMAiLSSGCDP.
OrthoDBiEOG091G00W8.
TreeFamiTF326036.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
1.25.40.20. 7 hits.
3.90.228.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 5 hits.
PF00644. PARP. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 15 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF48403. SSF48403. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 15 hits.
PS51059. PARP_CATALYTIC. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3UES3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGRRCAGGG AACASAGAEA VEPSARELFE ACRNGDVERV KRLVTPEKVN
60 70 80 90 100
SRDTAGRKST PLHFAAGFGR KDVVEYLLQN GANVQARDDG GLIPLHNACS
110 120 130 140 150
FGHAEVVNLL LQHGADPNAR DNWNYTPLHE AAIKGKIDVC IVLLQHGAEP
160 170 180 190 200
TIRNTDGRTA LDLADPSAKA VLTGDYKKDE LLESARSGNE EKMMALLTPL
210 220 230 240 250
NVNCHASDGR KSTPLHLAAG YNRVKIVQLL LHHGADVHAK DKGDLVPLHN
260 270 280 290 300
ACSYGHYEVT ELLVKHGACV NAMDLWQFTP LHEAASKNRI EVCSLLLSYG
310 320 330 340 350
ADPTLLNCHN KSAIDLAPTA QLKERLSYEF KGHSLLQAAR EADVTRIKKH
360 370 380 390 400
LSLEMVNFKH PQTHETALHC AAASPYPKRK QICELLLRKG ANTNEKTKEF
410 420 430 440 450
LTPLHVASEN AHNDVVEVVV KHEAKVNALD SLGQTSLHRA AHCGHLQTCR
460 470 480 490 500
LLLSYGCDPN IISLQGFTAL QMGNENVQQL LQEGASLGHS EADRQLLEAA
510 520 530 540 550
KAGDVETVKK LCTVQSVNCR DIEGRQSTPL HFAAGYNRVS VVEYLLQHGA
560 570 580 590 600
DVHAKDKGGL VPLHNACSYG HYEVAELLVK HGAVVNVADL WKFTPLHEAA
610 620 630 640 650
AKGKYEICKL LLQHGADPTK KNRDGNTPLD LVKDGDTDIQ DLLRGDAALL
660 670 680 690 700
DAAKKGCLAR VKKLSSPDNV NCRDTQGRHS TPLHLAAGYN NLEVAEYLLQ
710 720 730 740 750
HGADVNAQDK GGLIPLHNAA SYGHVDVAAL LIKYNACVNA TDKWAFTPLH
760 770 780 790 800
EAAQKGRTQL CALLLAHGAD PTLKNQEGQT PLDLVSADDV SALLTAAMPP
810 820 830 840 850
SALPTCYKPQ VLSGVRGPGA TADALSSGPS SPSSLSAASS LDNLSGSFSE
860 870 880 890 900
LSAVVSSSAA EGATGLQRKE DSGIDFSITQ FIRNLGLEHL MDIFEREQIT
910 920 930 940 950
LDVLVEMGHK ELKEIGINAY GHRHKLIKGV ERLISGQQGL NPYLTLNNSG
960 970 980 990 1000
SGTILIDLSP DDKEFQSVEE EMQSTVREHR DGGHAGGVFN RYNILKIQKV
1010 1020 1030 1040 1050
CNKKLWERYT HRRKEVSEEN HNHANERMLF HGSPFVNAII HKGFDERHAY
1060 1070 1080 1090 1100
IGGMFGAGIY FAENSSKSNQ YVYGIGGGTG CPIHKDRSCY ICHRQLLFCR
1110 1120 1130 1140 1150
VTLGKSFLQF SAMKMAHSPP GHHSVTGRPS VNGLALAEYV IYRGEQAYPE
1160
YLITYQIVRP EGMVDG
Length:1,166
Mass (Da):126,744
Last modified:May 31, 2011 - v2
Checksum:i5C1E11B74BB11FC9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161D → H in BAC32960 (PubMed:16141072).Curated
Sequence conflicti178 – 1781K → E in BAC32960 (PubMed:16141072).Curated
Sequence conflicti220 – 2201G → E in BAC32960 (PubMed:16141072).Curated
Sequence conflicti809 – 8091P → T in BAE28838 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK047094 mRNA. Translation: BAC32960.2.
AK149368 mRNA. Translation: BAE28838.1.
AC116128 Genomic DNA. No translation available.
BC063101 mRNA. Translation: AAH63101.1.
CCDSiCCDS50426.1.
RefSeqiNP_001157107.1. NM_001163635.1.
UniGeneiMm.249310.

Genome annotation databases

EnsembliENSMUST00000025729; ENSMUSP00000025729; ENSMUSG00000024811.
GeneIDi74493.
KEGGimmu:74493.
UCSCiuc008hhu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK047094 mRNA. Translation: BAC32960.2.
AK149368 mRNA. Translation: BAE28838.1.
AC116128 Genomic DNA. No translation available.
BC063101 mRNA. Translation: AAH63101.1.
CCDSiCCDS50426.1.
RefSeqiNP_001157107.1. NM_001163635.1.
UniGeneiMm.249310.

3D structure databases

ProteinModelPortaliQ3UES3.
SMRiQ3UES3. Positions 26-797, 952-1161.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi216798. 18 interactions.
IntActiQ3UES3. 18 interactions.
STRINGi10090.ENSMUSP00000025729.

Chemistry

BindingDBiQ3UES3.
ChEMBLiCHEMBL3232703.

PTM databases

iPTMnetiQ3UES3.
PhosphoSiteiQ3UES3.
SwissPalmiQ3UES3.

Proteomic databases

PaxDbiQ3UES3.
PRIDEiQ3UES3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025729; ENSMUSP00000025729; ENSMUSG00000024811.
GeneIDi74493.
KEGGimmu:74493.
UCSCiuc008hhu.2. mouse.

Organism-specific databases

CTDi80351.
MGIiMGI:1921743. Tnks2.

Phylogenomic databases

eggNOGiKOG4177. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129677.
HOGENOMiHOG000246964.
HOVERGENiHBG059472.
InParanoidiQ3UES3.
KOiK10799.
OMAiLSSGCDP.
OrthoDBiEOG091G00W8.
TreeFamiTF326036.

Enzyme and pathway databases

ReactomeiR-MMU-201681. TCF dependent signaling in response to WNT.
R-MMU-4641257. Degradation of AXIN.

Miscellaneous databases

ChiTaRSiTnks2. mouse.
PROiQ3UES3.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024811.
ExpressionAtlasiQ3UES3. baseline and differential.
GenevisibleiQ3UES3. MM.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
1.25.40.20. 7 hits.
3.90.228.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 5 hits.
PF00644. PARP. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 15 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF48403. SSF48403. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 15 hits.
PS51059. PARP_CATALYTIC. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTNKS2_MOUSE
AccessioniPrimary (citable) accession number: Q3UES3
Secondary accession number(s): Q6P537, Q8BXH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: May 31, 2011
Last modified: September 7, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.